HEADER LIGASE 19-MAR-05 1Z5S TITLE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN UBC9, SUMO-1, TITLE 2 RANGAP1 AND NUP358/RANBP2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 I; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: UBIQUITIN-PROTEIN LIGASE I, UBIQUITIN CARRIER COMPND 5 PROTEIN I, SUMO-1-PROTEIN LIGASE, SUMO- 1 CONJUGATING COMPND 6 ENZYME, UBIQUITIN CARRIER PROTEIN 9, P18; COMPND 7 EC: 6.3.2.19; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3C; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: UBIQUITIN-HOMOLOGY DOMAIN PROTEIN PIC1, UBIQUITIN- COMPND 13 LIKE PROTEIN UBL1, UBIQUITIN-RELATED PROTEIN SUMO-1, GAP COMPND 14 MODIFYING PROTEIN 1, GMP1, SENTRIN, OK/SW-CL.43; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 3; COMPND 17 MOLECULE: RAN GTPASE-ACTIVATING PROTEIN 1; COMPND 18 CHAIN: C; COMPND 19 FRAGMENT: C-TERMINAL DOMAIN; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 4; COMPND 22 MOLECULE: RAN-BINDING PROTEIN 2; COMPND 23 CHAIN: D; COMPND 24 FRAGMENT: IR1-M DOMAIN; COMPND 25 SYNONYM: RANBP2, NUCLEAR PORE COMPLEX PROTEIN NUP358, COMPND 26 NUCLEOPORIN NUP358, 358 KDA NUCLEOPORIN, P270; COMPND 27 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: UBE2I, UBC9, UBCE9; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: UBL1, SMT3C, SMT3H3; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET28B; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 GENE: RANGAP1; SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 27 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PSMT3; SOURCE 31 MOL_ID: 4; SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 33 ORGANISM_COMMON: HUMAN; SOURCE 34 ORGANISM_TAXID: 9606; SOURCE 35 GENE: RANBP2, NUP358; SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 37 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PSMT3 KEYWDS E3, LIGASE, SUMO, UBC9, NUCLEAR PORE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.REVERTER,C.D.LIMA REVDAT 2 24-FEB-09 1Z5S 1 VERSN REVDAT 1 07-JUN-05 1Z5S 0 JRNL AUTH D.REVERTER,C.D.LIMA JRNL TITL INSIGHTS INTO E3 LIGASE ACTIVITY REVEALED BY A JRNL TITL 2 SUMO-RANGAP1-UBC9-NUP358 COMPLEX. JRNL REF NATURE V. 435 687 2005 JRNL REFN ISSN 0028-0836 JRNL PMID 15931224 JRNL DOI 10.1038/NATURE03588 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.01 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.69 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2281669.870 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5 REMARK 3 NUMBER OF REFLECTIONS : 16461 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.247 REMARK 3 FREE R VALUE : 0.290 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 832 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.01 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2299 REMARK 3 BIN R VALUE (WORKING SET) : 0.4250 REMARK 3 BIN FREE R VALUE : 0.4320 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 122 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3564 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 28 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 74.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -15.45000 REMARK 3 B22 (A**2) : -15.45000 REMARK 3 B33 (A**2) : 30.91000 REMARK 3 B12 (A**2) : 17.61000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.47 REMARK 3 ESD FROM SIGMAA (A) : 0.99 REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.57 REMARK 3 ESD FROM C-V SIGMAA (A) : 1.16 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.270 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.980 ; 3.500 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.800 ; 2.500 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.720 ; 4.000 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.27 REMARK 3 BSOL : 13.94 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : ION.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : ION.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED REMARK 4 REMARK 4 1Z5S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-05. REMARK 100 THE RCSB ID CODE IS RCSB032333. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-AUG-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 31-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : DIAMOND REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16464 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.46400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: RANGAP1-UBC9 COMPLEX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG4000 (W/V), 0.1 M SODIUM REMARK 280 CITRATE, 0.2 M AMMONIUM ACETATE, PH 5.0, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.74200 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.87100 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 19.87100 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.74200 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 SER A 158 REMARK 465 MET B 16 REMARK 465 GLY B 17 REMARK 465 GLU B 18 REMARK 465 GLY B 19 REMARK 465 SER C 416 REMARK 465 LEU C 417 REMARK 465 ASN C 418 REMARK 465 THR C 419 REMARK 465 GLY C 420 REMARK 465 GLU C 421 REMARK 465 PRO C 422 REMARK 465 ALA C 423 REMARK 465 PRO C 424 REMARK 465 VAL C 425 REMARK 465 LEU C 426 REMARK 465 SER C 427 REMARK 465 SER C 428 REMARK 465 PRO C 429 REMARK 465 PRO C 430 REMARK 465 PRO C 431 REMARK 465 GLU D 2694 REMARK 465 LYS D 2695 REMARK 465 CYS D 2696 REMARK 465 ARG D 2697 REMARK 465 PRO D 2698 REMARK 465 LEU D 2699 REMARK 465 GLU D 2700 REMARK 465 GLU D 2701 REMARK 465 ASN D 2702 REMARK 465 THR D 2703 REMARK 465 ALA D 2704 REMARK 465 ASP D 2705 REMARK 465 ASN D 2706 REMARK 465 GLU D 2707 REMARK 465 LYS D 2708 REMARK 465 GLU D 2709 REMARK 465 CYS D 2710 REMARK 465 ILE D 2711 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 2 CB OG REMARK 470 LYS A 18 CG CD CE NZ REMARK 470 LYS A 49 CG CD CE NZ REMARK 470 GLU B 83 CG CD OE1 OE2 REMARK 470 LYS C 452 CG CD CE NZ REMARK 470 LYS C 553 CG CD CE NZ REMARK 470 LYS C 586 CG CD CE NZ REMARK 470 LYS D2650 CD CE NZ REMARK 470 ARG D2663 CD NE CZ NH1 NH2 REMARK 470 ASP D2665 OD1 OD2 REMARK 470 TYR D2666 CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU D2669 CD OE1 OE2 REMARK 470 GLU D2670 CD OE1 OE2 REMARK 470 LYS D2683 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 28 -174.63 -63.89 REMARK 500 THR A 29 -164.26 -111.71 REMARK 500 ASP A 33 -7.93 -48.76 REMARK 500 THR A 35 -171.71 -56.25 REMARK 500 TYR A 68 143.62 -29.38 REMARK 500 PRO A 84 -34.88 -35.87 REMARK 500 TYR A 87 162.92 -49.41 REMARK 500 LYS A 101 -90.01 -136.46 REMARK 500 GLU A 122 67.87 -119.45 REMARK 500 ASN A 124 63.57 -107.83 REMARK 500 ILE A 125 -17.78 -49.80 REMARK 500 ASP A 127 79.63 178.40 REMARK 500 ASP B 30 27.84 -166.34 REMARK 500 MET B 40 23.01 -68.20 REMARK 500 GLN B 55 -5.54 -144.84 REMARK 500 MET B 59 -34.00 -39.55 REMARK 500 SER B 61 -41.91 -20.73 REMARK 500 ARG B 63 133.53 -171.33 REMARK 500 THR B 76 145.81 -178.64 REMARK 500 PRO B 77 -12.96 -46.04 REMARK 500 GLU B 83 -152.79 -73.50 REMARK 500 GLU B 85 -0.73 67.23 REMARK 500 ASP B 86 174.38 -49.61 REMARK 500 PRO C 441 174.39 -46.34 REMARK 500 SER C 442 136.08 178.79 REMARK 500 ARG C 448 32.65 -68.54 REMARK 500 LYS C 452 30.87 -91.86 REMARK 500 SER C 454 2.98 -55.66 REMARK 500 VAL C 455 -20.09 -148.58 REMARK 500 ALA C 458 44.85 -69.09 REMARK 500 GLN C 459 -47.72 -166.21 REMARK 500 ASP C 462 82.70 -68.40 REMARK 500 THR C 463 2.96 -63.74 REMARK 500 SER C 464 -81.21 -61.18 REMARK 500 SER C 478 6.59 -56.14 REMARK 500 ASP C 482 -2.93 -52.41 REMARK 500 GLU C 483 172.26 -47.27 REMARK 500 LYS C 500 -71.26 -66.23 REMARK 500 SER C 504 83.80 167.31 REMARK 500 SER C 505 -25.27 -29.95 REMARK 500 SER C 506 44.34 -72.22 REMARK 500 LEU C 513 -35.53 -39.16 REMARK 500 MET C 520 32.67 -90.33 REMARK 500 ASP C 527 -158.91 -141.67 REMARK 500 ALA C 533 -81.57 -53.56 REMARK 500 TYR C 550 4.95 -58.49 REMARK 500 LYS C 553 8.55 -58.04 REMARK 500 SER C 568 -72.75 -30.12 REMARK 500 LEU C 570 12.09 -65.44 REMARK 500 CYS C 573 46.80 -153.06 REMARK 500 PHE C 575 -72.87 -57.97 REMARK 500 PRO D2655 -35.18 -32.18 REMARK 500 THR D2656 52.22 -94.57 REMARK 500 ASP D2665 -145.49 -60.17 REMARK 500 TYR D2666 99.24 -46.22 REMARK 500 SER D2668 -124.74 -163.17 REMARK 500 GLU D2669 49.75 -171.41 REMARK 500 GLU D2670 125.83 -172.04 REMARK 500 GLU D2671 137.23 176.29 REMARK 500 ASP D2674 -31.22 -161.38 REMARK 500 GLU D2675 139.14 -32.83 REMARK 500 ASN D2685 -75.16 18.02 REMARK 500 LYS D2687 173.59 -47.89 REMARK 500 ASP D2691 108.30 -44.98 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KPS RELATED DB: PDB REMARK 900 PUTATIVE SUBSTRATE COMPLEX BETWEEN UBC9 AND RANGAP1 REMARK 999 REMARK 999 SEQUENCE REMARK 999 COVALENT ISOPEPTIDE BOND BETWEEN RANGAP1 LYS524 AND REMARK 999 SUMO C-TERMINUS GLY97. DBREF 1Z5S A 1 158 UNP P63279 UBE2I_HUMAN 1 158 DBREF 1Z5S B 18 97 UNP P63165 SUMO1_HUMAN 18 97 DBREF 1Z5S C 418 587 UNP P46060 RGP1_HUMAN 418 587 DBREF 1Z5S D 2631 2711 UNP P49792 RBP2_HUMAN 2631 2711 SEQADV 1Z5S MET B 16 UNP P63165 CLONING ARTIFACT SEQADV 1Z5S GLY B 17 UNP P63165 CLONING ARTIFACT SEQADV 1Z5S SER C 416 UNP P46060 CLONING ARTIFACT SEQADV 1Z5S LEU C 417 UNP P46060 CLONING ARTIFACT SEQADV 1Z5S SER D 2629 UNP P49792 CLONING ARTIFACT SEQADV 1Z5S LEU D 2630 UNP P49792 CLONING ARTIFACT SEQRES 1 A 158 MET SER GLY ILE ALA LEU SER ARG LEU ALA GLN GLU ARG SEQRES 2 A 158 LYS ALA TRP ARG LYS ASP HIS PRO PHE GLY PHE VAL ALA SEQRES 3 A 158 VAL PRO THR LYS ASN PRO ASP GLY THR MET ASN LEU MET SEQRES 4 A 158 ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS GLY THR PRO SEQRES 5 A 158 TRP GLU GLY GLY LEU PHE LYS LEU ARG MET LEU PHE LYS SEQRES 6 A 158 ASP ASP TYR PRO SER SER PRO PRO LYS CYS LYS PHE GLU SEQRES 7 A 158 PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO SER GLY THR SEQRES 8 A 158 VAL CYS LEU SER ILE LEU GLU GLU ASP LYS ASP TRP ARG SEQRES 9 A 158 PRO ALA ILE THR ILE LYS GLN ILE LEU LEU GLY ILE GLN SEQRES 10 A 158 GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP PRO ALA GLN SEQRES 11 A 158 ALA GLU ALA TYR THR ILE TYR CYS GLN ASN ARG VAL GLU SEQRES 12 A 158 TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS LYS PHE ALA SEQRES 13 A 158 PRO SER SEQRES 1 B 82 MET GLY GLU GLY GLU TYR ILE LYS LEU LYS VAL ILE GLY SEQRES 2 B 82 GLN ASP SER SER GLU ILE HIS PHE LYS VAL LYS MET THR SEQRES 3 B 82 THR HIS LEU LYS LYS LEU LYS GLU SER TYR CYS GLN ARG SEQRES 4 B 82 GLN GLY VAL PRO MET ASN SER LEU ARG PHE LEU PHE GLU SEQRES 5 B 82 GLY GLN ARG ILE ALA ASP ASN HIS THR PRO LYS GLU LEU SEQRES 6 B 82 GLY MET GLU GLU GLU ASP VAL ILE GLU VAL TYR GLN GLU SEQRES 7 B 82 GLN THR GLY GLY SEQRES 1 C 172 SER LEU ASN THR GLY GLU PRO ALA PRO VAL LEU SER SER SEQRES 2 C 172 PRO PRO PRO ALA ASP VAL SER THR PHE LEU ALA PHE PRO SEQRES 3 C 172 SER PRO GLU LYS LEU LEU ARG LEU GLY PRO LYS SER SER SEQRES 4 C 172 VAL LEU ILE ALA GLN GLN THR ASP THR SER ASP PRO GLU SEQRES 5 C 172 LYS VAL VAL SER ALA PHE LEU LYS VAL SER SER VAL PHE SEQRES 6 C 172 LYS ASP GLU ALA THR VAL ARG MET ALA VAL GLN ASP ALA SEQRES 7 C 172 VAL ASP ALA LEU MET GLN LYS ALA PHE ASN SER SER SER SEQRES 8 C 172 PHE ASN SER ASN THR PHE LEU THR ARG LEU LEU VAL HIS SEQRES 9 C 172 MET GLY LEU LEU LYS SER GLU ASP LYS VAL LYS ALA ILE SEQRES 10 C 172 ALA ASN LEU TYR GLY PRO LEU MET ALA LEU ASN HIS MET SEQRES 11 C 172 VAL GLN GLN ASP TYR PHE PRO LYS ALA LEU ALA PRO LEU SEQRES 12 C 172 LEU LEU ALA PHE VAL THR LYS PRO ASN SER ALA LEU GLU SEQRES 13 C 172 SER CYS SER PHE ALA ARG HIS SER LEU LEU GLN THR LEU SEQRES 14 C 172 TYR LYS VAL SEQRES 1 D 83 SER LEU ASP VAL LEU ILE VAL TYR GLU LEU THR PRO THR SEQRES 2 D 83 ALA GLU GLN LYS ALA LEU ALA THR LYS LEU LYS LEU PRO SEQRES 3 D 83 PRO THR PHE PHE CYS TYR LYS ASN ARG PRO ASP TYR VAL SEQRES 4 D 83 SER GLU GLU GLU GLU ASP ASP GLU ASP PHE GLU THR ALA SEQRES 5 D 83 VAL LYS LYS LEU ASN GLY LYS LEU TYR LEU ASP GLY SER SEQRES 6 D 83 GLU LYS CYS ARG PRO LEU GLU GLU ASN THR ALA ASP ASN SEQRES 7 D 83 GLU LYS GLU CYS ILE FORMUL 5 HOH *28(H2 O) HELIX 35 35 ILE A 4 ASP A 19 1 16 HELIX 36 36 LEU A 94 GLU A 98 1 5 HELIX 37 37 THR A 108 GLU A 122 1 15 HELIX 38 38 GLN A 130 LYS A 154 1 25 HELIX 39 39 HIS B 43 ARG B 54 1 12 HELIX 40 40 THR B 76 GLY B 81 1 6 HELIX 41 41 ALA C 432 PHE C 440 1 9 HELIX 42 42 LEU C 446 SER C 454 1 9 HELIX 43 43 LEU C 456 THR C 461 1 6 HELIX 44 44 ASP C 465 SER C 478 1 14 HELIX 45 45 ALA C 484 PHE C 502 1 19 HELIX 46 46 ASN C 508 MET C 520 1 13 HELIX 47 47 LEU C 535 VAL C 546 1 12 HELIX 48 48 LEU C 555 LYS C 565 1 11 HELIX 49 49 SER C 568 VAL C 587 1 20 HELIX 50 50 THR D 2641 LEU D 2651 1 11 HELIX 51 51 ASP D 2676 LEU D 2684 1 9 SHEET 21 21 1 VAL A 25 LYS A 30 0 SHEET 22 22 1 MET A 36 PRO A 46 0 SHEET 23 23 1 LEU A 57 LEU A 63 0 SHEET 24 24 1 LYS A 74 PHE A 77 0 SHEET 25 25 1 ILE B 22 ILE B 27 0 SHEET 26 26 1 GLU B 33 VAL B 38 0 SHEET 27 27 1 PHE B 64 PHE B 66 0 SHEET 28 28 1 GLN B 69 ARG B 70 0 SHEET 29 29 1 VAL B 87 VAL B 90 0 SHEET 30 30 1 VAL D2632 GLU D2637 0 LINK C GLY B 97 NZ LYS C 524 1555 1555 1.33 CISPEP 1 TYR A 68 PRO A 69 0 -0.05 CISPEP 2 GLU A 78 PRO A 79 0 -0.09 CRYST1 157.123 157.123 59.613 90.00 90.00 120.00 P 32 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.006364 0.003675 0.000000 0.00000 SCALE2 0.000000 0.007349 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016775 0.00000 TER 1244 PRO A 157 ATOM 1245 N GLU B 20 91.314 29.660 -69.762 1.00137.38 N ATOM 1246 CA GLU B 20 92.180 28.763 -68.949 1.00137.58 C ATOM 1247 C GLU B 20 92.941 29.486 -67.843 1.00138.27 C ATOM 1248 O GLU B 20 92.407 29.697 -66.753 1.00138.04 O ATOM 1249 CB GLU B 20 93.166 28.018 -69.852 1.00136.35 C ATOM 1250 CG GLU B 20 92.557 26.808 -70.522 1.00136.73 C ATOM 1251 CD GLU B 20 91.950 25.849 -69.512 1.00136.96 C ATOM 1252 OE1 GLU B 20 92.698 25.338 -68.652 1.00137.05 O ATOM 1253 OE2 GLU B 20 90.726 25.612 -69.574 1.00137.00 O ATOM 1254 N TYR B 21 94.186 29.866 -68.119 1.00138.79 N ATOM 1255 CA TYR B 21 95.002 30.547 -67.119 1.00137.55 C ATOM 1256 C TYR B 21 95.861 31.701 -67.637 1.00134.87 C ATOM 1257 O TYR B 21 96.717 31.523 -68.507 1.00132.40 O ATOM 1258 CB TYR B 21 95.908 29.534 -66.407 1.00140.21 C ATOM 1259 CG TYR B 21 95.169 28.515 -65.563 1.00142.70 C ATOM 1260 CD1 TYR B 21 94.364 28.917 -64.495 1.00143.17 C ATOM 1261 CD2 TYR B 21 95.280 27.149 -65.826 1.00142.73 C ATOM 1262 CE1 TYR B 21 93.690 27.986 -63.709 1.00143.12 C ATOM 1263 CE2 TYR B 21 94.610 26.209 -65.046 1.00143.39 C ATOM 1264 CZ TYR B 21 93.817 26.636 -63.989 1.00143.45 C ATOM 1265 OH TYR B 21 93.159 25.714 -63.208 1.00143.47 O ATOM 1266 N ILE B 22 95.621 32.884 -67.079 1.00133.97 N ATOM 1267 CA ILE B 22 96.375 34.086 -67.422 1.00131.70 C ATOM 1268 C ILE B 22 96.771 34.805 -66.132 1.00127.04 C ATOM 1269 O ILE B 22 95.914 35.204 -65.335 1.00124.95 O ATOM 1270 CB ILE B 22 95.554 35.049 -68.309 1.00133.68 C ATOM 1271 CG1 ILE B 22 94.192 35.322 -67.666 1.00135.12 C ATOM 1272 CG2 ILE B 22 95.403 34.466 -69.705 1.00133.18 C ATOM 1273 CD1 ILE B 22 93.338 36.307 -68.439 1.00136.48 C ATOM 1274 N LYS B 23 98.078 34.944 -65.928 1.00121.32 N ATOM 1275 CA LYS B 23 98.619 35.601 -64.747 1.00115.15 C ATOM 1276 C LYS B 23 98.373 37.102 -64.835 1.00114.57 C ATOM 1277 O LYS B 23 98.748 37.746 -65.815 1.00115.41 O ATOM 1278 CB LYS B 23 100.118 35.314 -64.641 1.00110.69 C ATOM 1279 CG LYS B 23 100.826 36.019 -63.500 1.00105.64 C ATOM 1280 CD LYS B 23 102.298 35.642 -63.462 1.00103.74 C ATOM 1281 CE LYS B 23 102.473 34.144 -63.245 1.00104.55 C ATOM 1282 NZ LYS B 23 103.904 33.729 -63.212 1.00103.76 N ATOM 1283 N LEU B 24 97.738 37.652 -63.806 1.00112.64 N ATOM 1284 CA LEU B 24 97.428 39.074 -63.758 1.00110.21 C ATOM 1285 C LEU B 24 98.262 39.787 -62.702 1.00110.26 C ATOM 1286 O LEU B 24 98.674 39.184 -61.711 1.00109.54 O ATOM 1287 CB LEU B 24 95.947 39.276 -63.436 1.00109.91 C ATOM 1288 CG LEU B 24 94.900 38.736 -64.413 1.00109.51 C ATOM 1289 CD1 LEU B 24 93.517 38.856 -63.785 1.00106.85 C ATOM 1290 CD2 LEU B 24 94.972 39.501 -65.730 1.00107.70 C ATOM 1291 N LYS B 25 98.507 41.074 -62.925 1.00111.16 N ATOM 1292 CA LYS B 25 99.271 41.895 -61.989 1.00113.68 C ATOM 1293 C LYS B 25 98.390 42.994 -61.394 1.00115.28 C ATOM 1294 O LYS B 25 98.122 44.003 -62.050 1.00118.16 O ATOM 1295 CB LYS B 25 100.464 42.559 -62.685 1.00112.86 C ATOM 1296 CG LYS B 25 101.697 41.696 -62.858 1.00110.70 C ATOM 1297 CD LYS B 25 102.887 42.570 -63.228 1.00108.55 C ATOM 1298 CE LYS B 25 104.180 41.782 -63.279 1.00107.66 C ATOM 1299 NZ LYS B 25 105.343 42.669 -63.553 1.00106.70 N ATOM 1300 N VAL B 26 97.937 42.807 -60.159 1.00113.30 N ATOM 1301 CA VAL B 26 97.105 43.814 -59.516 1.00110.66 C ATOM 1302 C VAL B 26 98.009 44.768 -58.750 1.00110.63 C ATOM 1303 O VAL B 26 98.532 44.432 -57.687 1.00110.12 O ATOM 1304 CB VAL B 26 96.096 43.177 -58.546 1.00109.24 C ATOM 1305 CG1 VAL B 26 95.190 44.245 -57.964 1.00106.08 C ATOM 1306 CG2 VAL B 26 95.277 42.130 -59.272 1.00108.86 C ATOM 1307 N ILE B 27 98.202 45.956 -59.308 1.00110.16 N ATOM 1308 CA ILE B 27 99.050 46.959 -58.689 1.00110.49 C ATOM 1309 C ILE B 27 98.230 47.988 -57.932 1.00110.98 C ATOM 1310 O ILE B 27 97.402 48.688 -58.514 1.00110.60 O ATOM 1311 CB ILE B 27 99.898 47.684 -59.740 1.00111.09 C ATOM 1312 CG1 ILE B 27 100.927 46.718 -60.327 1.00111.88 C ATOM 1313 CG2 ILE B 27 100.589 48.879 -59.117 1.00113.32 C ATOM 1314 CD1 ILE B 27 101.838 47.346 -61.362 1.00112.93 C ATOM 1315 N GLY B 28 98.474 48.075 -56.628 1.00112.35 N ATOM 1316 CA GLY B 28 97.756 49.021 -55.794 1.00113.66 C ATOM 1317 C GLY B 28 98.295 50.434 -55.909 1.00113.71 C ATOM 1318 O GLY B 28 99.042 50.745 -56.837 1.00114.16 O ATOM 1319 N GLN B 29 97.924 51.292 -54.963 1.00113.16 N ATOM 1320 CA GLN B 29 98.380 52.675 -54.990 1.00111.98 C ATOM 1321 C GLN B 29 99.262 53.006 -53.796 1.00108.32 C ATOM 1322 O GLN B 29 99.110 54.049 -53.165 1.00103.89 O ATOM 1323 CB GLN B 29 97.178 53.620 -55.035 1.00114.67 C ATOM 1324 CG GLN B 29 97.445 54.856 -55.865 1.00115.93 C ATOM 1325 CD GLN B 29 98.035 54.503 -57.217 1.00115.77 C ATOM 1326 OE1 GLN B 29 97.363 53.918 -58.070 1.00115.45 O ATOM 1327 NE2 GLN B 29 99.306 54.841 -57.414 1.00115.17 N ATOM 1328 N ASP B 30 100.189 52.103 -53.502 1.00108.53 N ATOM 1329 CA ASP B 30 101.114 52.267 -52.388 1.00110.49 C ATOM 1330 C ASP B 30 102.258 51.263 -52.499 1.00110.33 C ATOM 1331 O ASP B 30 102.857 50.863 -51.496 1.00107.25 O ATOM 1332 CB ASP B 30 100.371 52.099 -51.053 1.00112.62 C ATOM 1333 CG ASP B 30 99.479 50.868 -51.022 1.00114.01 C ATOM 1334 OD1 ASP B 30 98.757 50.681 -50.017 1.00112.52 O ATOM 1335 OD2 ASP B 30 99.498 50.089 -51.998 1.00116.02 O ATOM 1336 N SER B 31 102.552 50.876 -53.740 1.00111.75 N ATOM 1337 CA SER B 31 103.613 49.924 -54.063 1.00112.50 C ATOM 1338 C SER B 31 103.265 48.481 -53.675 1.00111.25 C ATOM 1339 O SER B 31 104.132 47.600 -53.649 1.00110.13 O ATOM 1340 CB SER B 31 104.927 50.349 -53.401 1.00113.52 C ATOM 1341 OG SER B 31 105.987 49.486 -53.775 1.00116.77 O ATOM 1342 N SER B 32 101.988 48.249 -53.382 1.00108.59 N ATOM 1343 CA SER B 32 101.505 46.925 -53.018 1.00105.70 C ATOM 1344 C SER B 32 101.170 46.150 -54.285 1.00107.28 C ATOM 1345 O SER B 32 100.114 46.359 -54.880 1.00106.95 O ATOM 1346 CB SER B 32 100.254 47.043 -52.148 1.00102.39 C ATOM 1347 OG SER B 32 99.663 45.775 -51.926 1.00 99.70 O ATOM 1348 N GLU B 33 102.069 45.262 -54.702 1.00109.37 N ATOM 1349 CA GLU B 33 101.841 44.463 -55.902 1.00110.31 C ATOM 1350 C GLU B 33 101.475 43.020 -55.558 1.00106.90 C ATOM 1351 O GLU B 33 102.053 42.420 -54.650 1.00104.00 O ATOM 1352 CB GLU B 33 103.080 44.482 -56.805 1.00116.59 C ATOM 1353 CG GLU B 33 102.906 43.684 -58.102 1.00125.53 C ATOM 1354 CD GLU B 33 104.112 43.769 -59.037 1.00129.71 C ATOM 1355 OE1 GLU B 33 104.443 44.886 -59.490 1.00132.45 O ATOM 1356 OE2 GLU B 33 104.726 42.716 -59.322 1.00131.04 O ATOM 1357 N ILE B 34 100.508 42.476 -56.294 1.00104.73 N ATOM 1358 CA ILE B 34 100.039 41.109 -56.090 1.00103.80 C ATOM 1359 C ILE B 34 99.742 40.428 -57.423 1.00105.49 C ATOM 1360 O ILE B 34 99.114 41.021 -58.300 1.00106.12 O ATOM 1361 CB ILE B 34 98.758 41.087 -55.235 1.00101.25 C ATOM 1362 CG1 ILE B 34 99.070 41.603 -53.832 1.00100.45 C ATOM 1363 CG2 ILE B 34 98.199 39.678 -55.167 1.00100.23 C ATOM 1364 CD1 ILE B 34 97.857 41.748 -52.951 1.00 99.24 C ATOM 1365 N HIS B 35 100.190 39.182 -57.563 1.00106.50 N ATOM 1366 CA HIS B 35 99.987 38.411 -58.787 1.00106.66 C ATOM 1367 C HIS B 35 98.966 37.296 -58.620 1.00105.44 C ATOM 1368 O HIS B 35 99.026 36.522 -57.666 1.00104.42 O ATOM 1369 CB HIS B 35 101.312 37.816 -59.257 1.00109.27 C ATOM 1370 CG HIS B 35 102.264 38.830 -59.810 1.00113.01 C ATOM 1371 ND1 HIS B 35 103.532 38.504 -60.241 1.00115.57 N ATOM 1372 CD2 HIS B 35 102.127 40.161 -60.018 1.00114.15 C ATOM 1373 CE1 HIS B 35 104.136 39.590 -60.689 1.00116.16 C ATOM 1374 NE2 HIS B 35 103.305 40.609 -60.565 1.00115.62 N ATOM 1375 N PHE B 36 98.036 37.217 -59.565 1.00105.58 N ATOM 1376 CA PHE B 36 96.987 36.205 -59.537 1.00106.97 C ATOM 1377 C PHE B 36 96.946 35.386 -60.825 1.00110.17 C ATOM 1378 O PHE B 36 97.200 35.909 -61.912 1.00111.69 O ATOM 1379 CB PHE B 36 95.610 36.864 -59.363 1.00104.17 C ATOM 1380 CG PHE B 36 95.425 37.580 -58.057 1.00101.87 C ATOM 1381 CD1 PHE B 36 95.386 36.878 -56.857 1.00101.69 C ATOM 1382 CD2 PHE B 36 95.266 38.960 -58.030 1.00100.11 C ATOM 1383 CE1 PHE B 36 95.188 37.542 -55.648 1.00 99.64 C ATOM 1384 CE2 PHE B 36 95.070 39.631 -56.828 1.00 99.86 C ATOM 1385 CZ PHE B 36 95.030 38.920 -55.635 1.00 99.54 C ATOM 1386 N LYS B 37 96.638 34.097 -60.695 1.00111.94 N ATOM 1387 CA LYS B 37 96.482 33.218 -61.851 1.00113.55 C ATOM 1388 C LYS B 37 94.982 32.980 -61.857 1.00115.25 C ATOM 1389 O LYS B 37 94.429 32.458 -60.885 1.00114.21 O ATOM 1390 CB LYS B 37 97.214 31.885 -61.662 1.00114.03 C ATOM 1391 CG LYS B 37 98.652 31.861 -62.174 1.00114.35 C ATOM 1392 CD LYS B 37 99.253 30.466 -62.010 1.00114.05 C ATOM 1393 CE LYS B 37 100.744 30.436 -62.324 1.00112.21 C ATOM 1394 NZ LYS B 37 101.340 29.093 -62.041 1.00109.34 N ATOM 1395 N VAL B 38 94.314 33.373 -62.934 1.00117.18 N ATOM 1396 CA VAL B 38 92.874 33.208 -62.974 1.00120.42 C ATOM 1397 C VAL B 38 92.326 32.552 -64.226 1.00124.51 C ATOM 1398 O VAL B 38 92.879 32.695 -65.319 1.00123.47 O ATOM 1399 CB VAL B 38 92.170 34.559 -62.806 1.00118.74 C ATOM 1400 CG1 VAL B 38 90.697 34.340 -62.565 1.00119.02 C ATOM 1401 CG2 VAL B 38 92.787 35.328 -61.663 1.00119.18 C ATOM 1402 N LYS B 39 91.223 31.831 -64.043 1.00129.95 N ATOM 1403 CA LYS B 39 90.538 31.157 -65.136 1.00134.80 C ATOM 1404 C LYS B 39 89.674 32.196 -65.842 1.00135.00 C ATOM 1405 O LYS B 39 88.847 32.866 -65.217 1.00135.09 O ATOM 1406 CB LYS B 39 89.665 30.018 -64.600 1.00138.94 C ATOM 1407 CG LYS B 39 90.455 28.862 -63.989 1.00142.83 C ATOM 1408 CD LYS B 39 89.531 27.749 -63.503 1.00145.43 C ATOM 1409 CE LYS B 39 90.321 26.560 -62.966 1.00146.23 C ATOM 1410 NZ LYS B 39 89.440 25.460 -62.471 1.00145.42 N ATOM 1411 N MET B 40 89.873 32.325 -67.148 1.00133.96 N ATOM 1412 CA MET B 40 89.147 33.298 -67.948 1.00132.37 C ATOM 1413 C MET B 40 87.660 32.993 -68.093 1.00133.20 C ATOM 1414 O MET B 40 87.009 33.450 -69.031 1.00131.50 O ATOM 1415 CB MET B 40 89.822 33.402 -69.309 1.00128.82 C ATOM 1416 CG MET B 40 91.315 33.595 -69.161 1.00126.43 C ATOM 1417 SD MET B 40 92.193 33.687 -70.706 1.00128.56 S ATOM 1418 CE MET B 40 92.628 31.967 -70.960 1.00128.03 C ATOM 1419 N THR B 41 87.134 32.223 -67.145 1.00135.90 N ATOM 1420 CA THR B 41 85.721 31.852 -67.120 1.00138.28 C ATOM 1421 C THR B 41 85.163 32.260 -65.761 1.00139.09 C ATOM 1422 O THR B 41 83.964 32.152 -65.504 1.00138.98 O ATOM 1423 CB THR B 41 85.527 30.327 -67.274 1.00138.35 C ATOM 1424 OG1 THR B 41 86.224 29.870 -68.439 1.00140.68 O ATOM 1425 CG2 THR B 41 84.044 29.987 -67.410 1.00135.49 C ATOM 1426 N THR B 42 86.054 32.730 -64.895 1.00139.33 N ATOM 1427 CA THR B 42 85.680 33.145 -63.552 1.00137.29 C ATOM 1428 C THR B 42 85.402 34.643 -63.484 1.00134.35 C ATOM 1429 O THR B 42 86.092 35.445 -64.120 1.00132.10 O ATOM 1430 CB THR B 42 86.796 32.794 -62.539 1.00137.92 C ATOM 1431 OG1 THR B 42 87.985 33.521 -62.866 1.00138.06 O ATOM 1432 CG2 THR B 42 87.110 31.302 -62.582 1.00137.04 C ATOM 1433 N HIS B 43 84.381 35.005 -62.712 1.00132.89 N ATOM 1434 CA HIS B 43 83.993 36.401 -62.533 1.00131.83 C ATOM 1435 C HIS B 43 85.118 37.134 -61.819 1.00128.30 C ATOM 1436 O HIS B 43 85.601 36.676 -60.780 1.00128.83 O ATOM 1437 CB HIS B 43 82.730 36.508 -61.673 1.00134.44 C ATOM 1438 CG HIS B 43 81.608 35.629 -62.123 1.00136.21 C ATOM 1439 ND1 HIS B 43 80.445 35.484 -61.397 1.00136.48 N ATOM 1440 CD2 HIS B 43 81.471 34.841 -63.215 1.00136.53 C ATOM 1441 CE1 HIS B 43 79.641 34.644 -62.022 1.00137.21 C ATOM 1442 NE2 HIS B 43 80.239 34.239 -63.128 1.00137.29 N ATOM 1443 N LEU B 44 85.527 38.275 -62.362 1.00121.77 N ATOM 1444 CA LEU B 44 86.591 39.042 -61.743 1.00114.70 C ATOM 1445 C LEU B 44 86.299 39.343 -60.285 1.00113.03 C ATOM 1446 O LEU B 44 87.221 39.599 -59.516 1.00115.59 O ATOM 1447 CB LEU B 44 86.835 40.345 -62.503 1.00109.75 C ATOM 1448 CG LEU B 44 87.711 40.198 -63.748 1.00107.57 C ATOM 1449 CD1 LEU B 44 87.935 41.555 -64.378 1.00108.52 C ATOM 1450 CD2 LEU B 44 89.040 39.580 -63.368 1.00105.38 C ATOM 1451 N LYS B 45 85.029 39.306 -59.890 1.00109.37 N ATOM 1452 CA LYS B 45 84.708 39.582 -58.496 1.00108.03 C ATOM 1453 C LYS B 45 85.548 38.695 -57.592 1.00108.20 C ATOM 1454 O LYS B 45 86.048 39.145 -56.563 1.00108.14 O ATOM 1455 CB LYS B 45 83.233 39.336 -58.189 1.00107.46 C ATOM 1456 CG LYS B 45 82.912 39.608 -56.721 1.00107.36 C ATOM 1457 CD LYS B 45 81.458 39.360 -56.364 1.00108.78 C ATOM 1458 CE LYS B 45 81.201 39.701 -54.898 1.00108.17 C ATOM 1459 NZ LYS B 45 79.784 39.474 -54.497 1.00108.76 N ATOM 1460 N LYS B 46 85.699 37.433 -57.983 1.00109.39 N ATOM 1461 CA LYS B 46 86.486 36.485 -57.202 1.00110.15 C ATOM 1462 C LYS B 46 87.877 37.059 -56.959 1.00107.75 C ATOM 1463 O LYS B 46 88.413 36.966 -55.852 1.00107.32 O ATOM 1464 CB LYS B 46 86.591 35.146 -57.940 1.00112.35 C ATOM 1465 CG LYS B 46 85.246 34.545 -58.316 1.00115.86 C ATOM 1466 CD LYS B 46 84.345 34.356 -57.095 1.00118.25 C ATOM 1467 CE LYS B 46 82.944 33.898 -57.506 1.00120.04 C ATOM 1468 NZ LYS B 46 82.017 33.721 -56.350 1.00119.97 N ATOM 1469 N LEU B 47 88.452 37.655 -58.001 1.00104.16 N ATOM 1470 CA LEU B 47 89.772 38.267 -57.902 1.00100.75 C ATOM 1471 C LEU B 47 89.651 39.418 -56.908 1.00102.12 C ATOM 1472 O LEU B 47 90.380 39.482 -55.915 1.00103.68 O ATOM 1473 CB LEU B 47 90.220 38.792 -59.272 1.00 93.49 C ATOM 1474 CG LEU B 47 91.673 39.261 -59.398 1.00 90.12 C ATOM 1475 CD1 LEU B 47 92.015 39.530 -60.852 1.00 90.67 C ATOM 1476 CD2 LEU B 47 91.879 40.503 -58.571 1.00 88.97 C ATOM 1477 N LYS B 48 88.717 40.320 -57.184 1.00101.13 N ATOM 1478 CA LYS B 48 88.466 41.461 -56.321 1.00100.45 C ATOM 1479 C LYS B 48 88.451 41.006 -54.864 1.00 99.23 C ATOM 1480 O LYS B 48 89.337 41.357 -54.088 1.00 99.23 O ATOM 1481 CB LYS B 48 87.122 42.091 -56.689 1.00103.00 C ATOM 1482 CG LYS B 48 86.684 43.217 -55.779 1.00108.56 C ATOM 1483 CD LYS B 48 85.359 43.806 -56.235 1.00112.75 C ATOM 1484 CE LYS B 48 84.905 44.924 -55.305 1.00116.89 C ATOM 1485 NZ LYS B 48 83.609 45.518 -55.741 1.00119.49 N ATOM 1486 N GLU B 49 87.449 40.207 -54.511 1.00 98.70 N ATOM 1487 CA GLU B 49 87.291 39.691 -53.151 1.00 99.08 C ATOM 1488 C GLU B 49 88.590 39.208 -52.512 1.00 95.59 C ATOM 1489 O GLU B 49 88.942 39.624 -51.407 1.00 93.96 O ATOM 1490 CB GLU B 49 86.298 38.533 -53.139 1.00103.46 C ATOM 1491 CG GLU B 49 84.963 38.824 -53.781 1.00107.76 C ATOM 1492 CD GLU B 49 84.023 37.647 -53.670 1.00111.19 C ATOM 1493 OE1 GLU B 49 83.612 37.322 -52.534 1.00112.65 O ATOM 1494 OE2 GLU B 49 83.707 37.040 -54.716 1.00112.86 O ATOM 1495 N SER B 50 89.281 38.306 -53.201 1.00 92.32 N ATOM 1496 CA SER B 50 90.535 37.756 -52.701 1.00 91.43 C ATOM 1497 C SER B 50 91.447 38.867 -52.206 1.00 91.14 C ATOM 1498 O SER B 50 91.916 38.846 -51.065 1.00 90.39 O ATOM 1499 CB SER B 50 91.248 36.974 -53.805 1.00 91.53 C ATOM 1500 OG SER B 50 92.495 36.474 -53.348 1.00 92.02 O ATOM 1501 N TYR B 51 91.694 39.832 -53.085 1.00 89.24 N ATOM 1502 CA TYR B 51 92.547 40.967 -52.775 1.00 86.14 C ATOM 1503 C TYR B 51 92.214 41.487 -51.384 1.00 84.08 C ATOM 1504 O TYR B 51 93.013 41.404 -50.454 1.00 82.62 O ATOM 1505 CB TYR B 51 92.318 42.080 -53.799 1.00 86.46 C ATOM 1506 CG TYR B 51 93.416 43.113 -53.827 1.00 87.59 C ATOM 1507 CD1 TYR B 51 94.582 42.898 -54.560 1.00 88.34 C ATOM 1508 CD2 TYR B 51 93.313 44.284 -53.080 1.00 87.81 C ATOM 1509 CE1 TYR B 51 95.622 43.822 -54.544 1.00 91.12 C ATOM 1510 CE2 TYR B 51 94.347 45.214 -53.055 1.00 90.14 C ATOM 1511 CZ TYR B 51 95.500 44.978 -53.787 1.00 92.11 C ATOM 1512 OH TYR B 51 96.536 45.887 -53.742 1.00 92.89 O ATOM 1513 N CYS B 52 91.002 42.004 -51.263 1.00 83.69 N ATOM 1514 CA CYS B 52 90.493 42.571 -50.027 1.00 85.14 C ATOM 1515 C CYS B 52 90.750 41.777 -48.752 1.00 83.93 C ATOM 1516 O CYS B 52 91.254 42.328 -47.779 1.00 82.84 O ATOM 1517 CB CYS B 52 89.001 42.820 -50.187 1.00 88.25 C ATOM 1518 SG CYS B 52 88.639 43.793 -51.659 1.00 94.15 S ATOM 1519 N GLN B 53 90.400 40.495 -48.745 1.00 85.39 N ATOM 1520 CA GLN B 53 90.606 39.671 -47.556 1.00 86.42 C ATOM 1521 C GLN B 53 92.076 39.318 -47.334 1.00 84.41 C ATOM 1522 O GLN B 53 92.527 39.193 -46.194 1.00 81.66 O ATOM 1523 CB GLN B 53 89.746 38.402 -47.634 1.00 90.66 C ATOM 1524 CG GLN B 53 89.984 37.524 -48.851 1.00 95.08 C ATOM 1525 CD GLN B 53 91.014 36.446 -48.591 1.00 99.56 C ATOM 1526 OE1 GLN B 53 90.896 35.680 -47.630 1.00101.22 O ATOM 1527 NE2 GLN B 53 92.030 36.371 -49.451 1.00101.75 N ATOM 1528 N ARG B 54 92.822 39.162 -48.423 1.00 83.91 N ATOM 1529 CA ARG B 54 94.242 38.854 -48.323 1.00 83.87 C ATOM 1530 C ARG B 54 94.961 40.175 -48.105 1.00 82.95 C ATOM 1531 O ARG B 54 96.173 40.279 -48.279 1.00 82.79 O ATOM 1532 CB ARG B 54 94.737 38.175 -49.608 1.00 87.44 C ATOM 1533 CG ARG B 54 96.261 38.103 -49.760 1.00 91.81 C ATOM 1534 CD ARG B 54 96.946 37.410 -48.589 1.00 97.29 C ATOM 1535 NE ARG B 54 97.109 35.971 -48.793 1.00104.04 N ATOM 1536 CZ ARG B 54 97.941 35.429 -49.679 1.00105.16 C ATOM 1537 NH1 ARG B 54 98.691 36.205 -50.451 1.00104.58 N ATOM 1538 NH2 ARG B 54 98.029 34.109 -49.790 1.00104.24 N ATOM 1539 N GLN B 55 94.198 41.189 -47.715 1.00 83.44 N ATOM 1540 CA GLN B 55 94.760 42.510 -47.474 1.00 83.74 C ATOM 1541 C GLN B 55 94.051 43.210 -46.315 1.00 84.06 C ATOM 1542 O GLN B 55 94.454 44.294 -45.897 1.00 84.62 O ATOM 1543 CB GLN B 55 94.647 43.357 -48.742 1.00 82.88 C ATOM 1544 CG GLN B 55 95.630 44.509 -48.798 1.00 86.84 C ATOM 1545 CD GLN B 55 97.076 44.043 -48.871 1.00 90.06 C ATOM 1546 OE1 GLN B 55 97.515 43.485 -49.882 1.00 88.09 O ATOM 1547 NE2 GLN B 55 97.825 44.266 -47.791 1.00 91.86 N ATOM 1548 N GLY B 56 92.996 42.582 -45.802 1.00 84.66 N ATOM 1549 CA GLY B 56 92.241 43.147 -44.695 1.00 84.15 C ATOM 1550 C GLY B 56 91.576 44.473 -45.012 1.00 83.88 C ATOM 1551 O GLY B 56 91.809 45.464 -44.328 1.00 84.37 O ATOM 1552 N VAL B 57 90.734 44.488 -46.038 1.00 85.02 N ATOM 1553 CA VAL B 57 90.049 45.707 -46.457 1.00 87.68 C ATOM 1554 C VAL B 57 88.685 45.378 -47.058 1.00 90.25 C ATOM 1555 O VAL B 57 88.600 44.621 -48.019 1.00 93.20 O ATOM 1556 CB VAL B 57 90.875 46.449 -47.525 1.00 88.15 C ATOM 1557 CG1 VAL B 57 90.108 47.644 -48.042 1.00 88.73 C ATOM 1558 CG2 VAL B 57 92.207 46.882 -46.942 1.00 89.76 C ATOM 1559 N PRO B 58 87.603 45.961 -46.515 1.00 90.88 N ATOM 1560 CA PRO B 58 86.249 45.706 -47.022 1.00 92.54 C ATOM 1561 C PRO B 58 86.093 45.803 -48.541 1.00 94.72 C ATOM 1562 O PRO B 58 86.637 46.703 -49.179 1.00 92.83 O ATOM 1563 CB PRO B 58 85.399 46.733 -46.272 1.00 91.15 C ATOM 1564 CG PRO B 58 86.368 47.824 -45.957 1.00 89.63 C ATOM 1565 CD PRO B 58 87.583 47.050 -45.528 1.00 90.54 C ATOM 1566 N MET B 59 85.339 44.859 -49.099 1.00 98.17 N ATOM 1567 CA MET B 59 85.081 44.770 -50.537 1.00102.39 C ATOM 1568 C MET B 59 84.860 46.126 -51.215 1.00103.95 C ATOM 1569 O MET B 59 85.233 46.324 -52.377 1.00101.59 O ATOM 1570 CB MET B 59 83.853 43.883 -50.774 1.00104.38 C ATOM 1571 CG MET B 59 83.629 43.451 -52.220 1.00106.07 C ATOM 1572 SD MET B 59 84.822 42.209 -52.758 1.00109.24 S ATOM 1573 CE MET B 59 84.635 40.985 -51.435 1.00109.82 C ATOM 1574 N ASN B 60 84.248 47.053 -50.484 1.00105.96 N ATOM 1575 CA ASN B 60 83.952 48.382 -51.007 1.00107.32 C ATOM 1576 C ASN B 60 85.148 49.320 -50.955 1.00106.77 C ATOM 1577 O ASN B 60 85.558 49.872 -51.972 1.00107.19 O ATOM 1578 CB ASN B 60 82.795 49.010 -50.223 1.00108.99 C ATOM 1579 CG ASN B 60 83.118 49.190 -48.747 1.00109.90 C ATOM 1580 OD1 ASN B 60 83.303 48.216 -48.016 1.00110.89 O ATOM 1581 ND2 ASN B 60 83.194 50.443 -48.306 1.00108.80 N ATOM 1582 N SER B 61 85.689 49.495 -49.755 1.00105.11 N ATOM 1583 CA SER B 61 86.825 50.371 -49.505 1.00103.26 C ATOM 1584 C SER B 61 87.675 50.701 -50.730 1.00100.04 C ATOM 1585 O SER B 61 88.074 51.847 -50.910 1.00101.63 O ATOM 1586 CB SER B 61 87.708 49.765 -48.408 1.00105.92 C ATOM 1587 OG SER B 61 88.744 50.651 -48.004 1.00108.14 O ATOM 1588 N LEU B 62 87.945 49.716 -51.578 1.00 96.52 N ATOM 1589 CA LEU B 62 88.773 49.960 -52.755 1.00 96.90 C ATOM 1590 C LEU B 62 87.987 50.167 -54.049 1.00 98.84 C ATOM 1591 O LEU B 62 86.800 50.483 -54.032 1.00 99.71 O ATOM 1592 CB LEU B 62 89.747 48.800 -52.953 1.00 95.39 C ATOM 1593 CG LEU B 62 90.431 48.239 -51.707 1.00 93.30 C ATOM 1594 CD1 LEU B 62 91.374 47.131 -52.132 1.00 92.00 C ATOM 1595 CD2 LEU B 62 91.180 49.336 -50.967 1.00 93.63 C ATOM 1596 N ARG B 63 88.686 49.993 -55.168 1.00100.55 N ATOM 1597 CA ARG B 63 88.126 50.123 -56.513 1.00102.07 C ATOM 1598 C ARG B 63 89.206 49.630 -57.473 1.00101.66 C ATOM 1599 O ARG B 63 90.371 50.008 -57.336 1.00102.86 O ATOM 1600 CB ARG B 63 87.784 51.581 -56.828 1.00105.13 C ATOM 1601 CG ARG B 63 87.358 51.810 -58.271 1.00108.71 C ATOM 1602 CD ARG B 63 87.331 53.292 -58.635 1.00113.29 C ATOM 1603 NE ARG B 63 86.160 53.998 -58.115 1.00115.43 N ATOM 1604 CZ ARG B 63 85.924 55.293 -58.316 1.00115.94 C ATOM 1605 NH1 ARG B 63 86.781 56.023 -59.021 1.00114.96 N ATOM 1606 NH2 ARG B 63 84.828 55.858 -57.825 1.00116.32 N ATOM 1607 N PHE B 64 88.828 48.789 -58.433 1.00 99.51 N ATOM 1608 CA PHE B 64 89.792 48.239 -59.385 1.00 97.92 C ATOM 1609 C PHE B 64 89.539 48.747 -60.798 1.00100.47 C ATOM 1610 O PHE B 64 88.391 48.893 -61.212 1.00102.03 O ATOM 1611 CB PHE B 64 89.731 46.709 -59.363 1.00 93.20 C ATOM 1612 CG PHE B 64 89.848 46.118 -57.986 1.00 89.08 C ATOM 1613 CD1 PHE B 64 88.851 46.324 -57.036 1.00 89.23 C ATOM 1614 CD2 PHE B 64 90.965 45.377 -57.627 1.00 87.73 C ATOM 1615 CE1 PHE B 64 88.964 45.804 -55.747 1.00 86.69 C ATOM 1616 CE2 PHE B 64 91.089 44.853 -56.342 1.00 88.60 C ATOM 1617 CZ PHE B 64 90.085 45.069 -55.400 1.00 87.63 C ATOM 1618 N LEU B 65 90.613 49.002 -61.540 1.00103.33 N ATOM 1619 CA LEU B 65 90.489 49.512 -62.901 1.00107.48 C ATOM 1620 C LEU B 65 91.310 48.740 -63.932 1.00110.46 C ATOM 1621 O LEU B 65 92.262 48.033 -63.593 1.00110.78 O ATOM 1622 CB LEU B 65 90.917 50.980 -62.948 1.00109.58 C ATOM 1623 CG LEU B 65 90.373 51.932 -61.883 1.00111.80 C ATOM 1624 CD1 LEU B 65 90.958 53.314 -62.122 1.00113.23 C ATOM 1625 CD2 LEU B 65 88.852 51.973 -61.930 1.00112.65 C ATOM 1626 N PHE B 66 90.928 48.898 -65.196 1.00111.89 N ATOM 1627 CA PHE B 66 91.613 48.263 -66.316 1.00111.36 C ATOM 1628 C PHE B 66 91.437 49.151 -67.548 1.00112.80 C ATOM 1629 O PHE B 66 90.379 49.757 -67.736 1.00112.03 O ATOM 1630 CB PHE B 66 91.038 46.872 -66.583 1.00109.17 C ATOM 1631 CG PHE B 66 91.692 46.166 -67.732 1.00108.88 C ATOM 1632 CD1 PHE B 66 93.066 45.967 -67.748 1.00109.04 C ATOM 1633 CD2 PHE B 66 90.939 45.718 -68.812 1.00109.11 C ATOM 1634 CE1 PHE B 66 93.685 45.335 -68.826 1.00108.06 C ATOM 1635 CE2 PHE B 66 91.547 45.084 -69.896 1.00107.87 C ATOM 1636 CZ PHE B 66 92.923 44.893 -69.901 1.00106.51 C ATOM 1637 N GLU B 67 92.470 49.229 -68.383 1.00114.44 N ATOM 1638 CA GLU B 67 92.423 50.069 -69.577 1.00117.24 C ATOM 1639 C GLU B 67 91.917 51.451 -69.179 1.00118.65 C ATOM 1640 O GLU B 67 91.274 52.146 -69.966 1.00120.62 O ATOM 1641 CB GLU B 67 91.489 49.469 -70.633 1.00120.96 C ATOM 1642 CG GLU B 67 92.020 48.229 -71.344 1.00125.12 C ATOM 1643 CD GLU B 67 91.058 47.705 -72.410 1.00127.52 C ATOM 1644 OE1 GLU B 67 89.916 47.333 -72.058 1.00127.22 O ATOM 1645 OE2 GLU B 67 91.443 47.664 -73.601 1.00127.81 O ATOM 1646 N GLY B 68 92.207 51.841 -67.943 1.00118.79 N ATOM 1647 CA GLY B 68 91.765 53.132 -67.461 1.00119.45 C ATOM 1648 C GLY B 68 90.358 53.074 -66.902 1.00120.62 C ATOM 1649 O GLY B 68 90.095 53.613 -65.826 1.00120.92 O ATOM 1650 N GLN B 69 89.450 52.414 -67.617 1.00120.78 N ATOM 1651 CA GLN B 69 88.066 52.316 -67.165 1.00121.40 C ATOM 1652 C GLN B 69 87.833 51.295 -66.054 1.00120.80 C ATOM 1653 O GLN B 69 88.516 50.272 -65.969 1.00119.77 O ATOM 1654 CB GLN B 69 87.135 52.029 -68.349 1.00122.00 C ATOM 1655 CG GLN B 69 87.017 53.201 -69.317 1.00122.38 C ATOM 1656 CD GLN B 69 85.829 53.083 -70.255 1.00121.48 C ATOM 1657 OE1 GLN B 69 85.712 52.119 -71.011 1.00122.01 O ATOM 1658 NE2 GLN B 69 84.942 54.072 -70.211 1.00119.53 N ATOM 1659 N ARG B 70 86.853 51.597 -65.208 1.00119.70 N ATOM 1660 CA ARG B 70 86.492 50.760 -64.071 1.00118.23 C ATOM 1661 C ARG B 70 86.231 49.304 -64.437 1.00119.24 C ATOM 1662 O ARG B 70 86.114 48.957 -65.612 1.00118.96 O ATOM 1663 CB ARG B 70 85.266 51.352 -63.378 1.00115.97 C ATOM 1664 CG ARG B 70 84.958 50.750 -62.033 1.00115.74 C ATOM 1665 CD ARG B 70 84.083 51.686 -61.231 1.00118.92 C ATOM 1666 NE ARG B 70 84.011 51.287 -59.830 1.00123.64 N ATOM 1667 CZ ARG B 70 83.536 52.058 -58.857 1.00126.18 C ATOM 1668 NH1 ARG B 70 83.089 53.276 -59.136 1.00127.77 N ATOM 1669 NH2 ARG B 70 83.514 51.616 -57.605 1.00126.21 N ATOM 1670 N ILE B 71 86.144 48.454 -63.418 1.00121.20 N ATOM 1671 CA ILE B 71 85.902 47.030 -63.619 1.00122.34 C ATOM 1672 C ILE B 71 84.592 46.562 -62.993 1.00123.66 C ATOM 1673 O ILE B 71 84.348 46.761 -61.799 1.00122.04 O ATOM 1674 CB ILE B 71 87.055 46.176 -63.044 1.00120.83 C ATOM 1675 CG1 ILE B 71 88.302 46.343 -63.914 1.00121.17 C ATOM 1676 CG2 ILE B 71 86.641 44.714 -62.974 1.00118.50 C ATOM 1677 CD1 ILE B 71 89.497 45.537 -63.442 1.00121.87 C ATOM 1678 N ALA B 72 83.761 45.931 -63.821 1.00124.69 N ATOM 1679 CA ALA B 72 82.468 45.412 -63.392 1.00123.31 C ATOM 1680 C ALA B 72 82.677 44.286 -62.398 1.00121.97 C ATOM 1681 O ALA B 72 83.695 43.595 -62.432 1.00121.55 O ATOM 1682 CB ALA B 72 81.670 44.906 -64.596 1.00121.30 C ATOM 1683 N ASP B 73 81.704 44.103 -61.517 1.00120.96 N ATOM 1684 CA ASP B 73 81.777 43.066 -60.504 1.00121.43 C ATOM 1685 C ASP B 73 81.557 41.676 -61.108 1.00122.56 C ATOM 1686 O ASP B 73 81.972 40.666 -60.536 1.00121.24 O ATOM 1687 CB ASP B 73 80.735 43.346 -59.426 1.00121.68 C ATOM 1688 CG ASP B 73 81.085 42.711 -58.107 1.00122.33 C ATOM 1689 OD1 ASP B 73 82.178 43.013 -57.579 1.00120.08 O ATOM 1690 OD2 ASP B 73 80.268 41.914 -57.598 1.00124.11 O ATOM 1691 N ASN B 74 80.907 41.635 -62.268 1.00125.07 N ATOM 1692 CA ASN B 74 80.626 40.382 -62.967 1.00125.90 C ATOM 1693 C ASN B 74 81.563 40.202 -64.149 1.00128.02 C ATOM 1694 O ASN B 74 81.500 39.198 -64.857 1.00127.04 O ATOM 1695 CB ASN B 74 79.179 40.365 -63.458 1.00124.25 C ATOM 1696 CG ASN B 74 78.183 40.238 -62.325 1.00124.47 C ATOM 1697 OD1 ASN B 74 76.980 40.416 -62.518 1.00124.44 O ATOM 1698 ND2 ASN B 74 78.679 39.919 -61.134 1.00124.64 N ATOM 1699 N HIS B 75 82.432 41.187 -64.353 1.00132.15 N ATOM 1700 CA HIS B 75 83.403 41.166 -65.442 1.00136.28 C ATOM 1701 C HIS B 75 84.236 39.881 -65.440 1.00136.45 C ATOM 1702 O HIS B 75 84.196 39.105 -64.485 1.00138.15 O ATOM 1703 CB HIS B 75 84.339 42.374 -65.325 1.00139.50 C ATOM 1704 CG HIS B 75 84.370 43.239 -66.546 1.00142.04 C ATOM 1705 ND1 HIS B 75 84.661 42.746 -67.801 1.00142.47 N ATOM 1706 CD2 HIS B 75 84.143 44.564 -66.706 1.00142.36 C ATOM 1707 CE1 HIS B 75 84.608 43.731 -68.680 1.00142.60 C ATOM 1708 NE2 HIS B 75 84.296 44.844 -68.041 1.00142.80 N ATOM 1709 N THR B 76 84.990 39.677 -66.517 1.00133.74 N ATOM 1710 CA THR B 76 85.857 38.514 -66.684 1.00132.45 C ATOM 1711 C THR B 76 86.540 38.713 -68.022 1.00130.73 C ATOM 1712 O THR B 76 85.936 39.269 -68.933 1.00129.04 O ATOM 1713 CB THR B 76 85.054 37.192 -66.736 1.00134.70 C ATOM 1714 OG1 THR B 76 84.431 36.955 -65.469 1.00137.57 O ATOM 1715 CG2 THR B 76 85.967 36.017 -67.062 1.00134.69 C ATOM 1716 N PRO B 77 87.808 38.276 -68.158 1.00131.67 N ATOM 1717 CA PRO B 77 88.540 38.426 -69.422 1.00132.49 C ATOM 1718 C PRO B 77 87.674 38.006 -70.605 1.00134.35 C ATOM 1719 O PRO B 77 88.003 38.265 -71.765 1.00133.51 O ATOM 1720 CB PRO B 77 89.746 37.519 -69.225 1.00130.98 C ATOM 1721 CG PRO B 77 90.038 37.706 -67.780 1.00130.10 C ATOM 1722 CD PRO B 77 88.661 37.634 -67.141 1.00131.07 C ATOM 1723 N LYS B 78 86.565 37.346 -70.284 1.00136.34 N ATOM 1724 CA LYS B 78 85.598 36.895 -71.271 1.00137.74 C ATOM 1725 C LYS B 78 85.061 38.147 -71.957 1.00138.88 C ATOM 1726 O LYS B 78 84.561 38.095 -73.081 1.00139.63 O ATOM 1727 CB LYS B 78 84.459 36.149 -70.565 1.00137.27 C ATOM 1728 CG LYS B 78 83.328 35.680 -71.471 1.00137.09 C ATOM 1729 CD LYS B 78 82.204 35.053 -70.655 1.00136.51 C ATOM 1730 CE LYS B 78 81.015 34.680 -71.528 1.00136.59 C ATOM 1731 NZ LYS B 78 79.875 34.154 -70.722 1.00136.28 N ATOM 1732 N GLU B 79 85.187 39.274 -71.264 1.00139.23 N ATOM 1733 CA GLU B 79 84.720 40.557 -71.765 1.00139.27 C ATOM 1734 C GLU B 79 85.870 41.538 -71.986 1.00139.93 C ATOM 1735 O GLU B 79 85.817 42.366 -72.894 1.00141.81 O ATOM 1736 CB GLU B 79 83.728 41.168 -70.774 1.00138.96 C ATOM 1737 CG GLU B 79 82.616 40.232 -70.348 1.00140.83 C ATOM 1738 CD GLU B 79 81.764 39.776 -71.513 1.00143.23 C ATOM 1739 OE1 GLU B 79 81.221 40.644 -72.229 1.00145.11 O ATOM 1740 OE2 GLU B 79 81.634 38.549 -71.711 1.00143.96 O ATOM 1741 N LEU B 80 86.906 41.441 -71.153 1.00138.87 N ATOM 1742 CA LEU B 80 88.061 42.335 -71.238 1.00136.13 C ATOM 1743 C LEU B 80 89.173 41.855 -72.155 1.00135.52 C ATOM 1744 O LEU B 80 90.089 42.616 -72.472 1.00133.21 O ATOM 1745 CB LEU B 80 88.639 42.575 -69.845 1.00134.56 C ATOM 1746 CG LEU B 80 87.763 43.408 -68.916 1.00133.54 C ATOM 1747 CD1 LEU B 80 88.381 43.491 -67.531 1.00133.42 C ATOM 1748 CD2 LEU B 80 87.599 44.791 -69.517 1.00134.44 C ATOM 1749 N GLY B 81 89.096 40.598 -72.575 1.00136.64 N ATOM 1750 CA GLY B 81 90.117 40.055 -73.451 1.00138.78 C ATOM 1751 C GLY B 81 91.510 40.298 -72.903 1.00139.61 C ATOM 1752 O GLY B 81 92.476 40.435 -73.652 1.00137.88 O ATOM 1753 N MET B 82 91.610 40.357 -71.582 1.00141.93 N ATOM 1754 CA MET B 82 92.890 40.583 -70.937 1.00144.62 C ATOM 1755 C MET B 82 93.845 39.437 -71.245 1.00145.50 C ATOM 1756 O MET B 82 93.577 38.291 -70.887 1.00146.03 O ATOM 1757 CB MET B 82 92.705 40.696 -69.422 1.00147.33 C ATOM 1758 CG MET B 82 91.734 41.782 -68.989 1.00151.33 C ATOM 1759 SD MET B 82 91.714 42.041 -67.197 1.00154.69 S ATOM 1760 CE MET B 82 90.427 40.908 -66.690 1.00154.31 C ATOM 1761 N GLU B 83 94.952 39.744 -71.916 1.00146.38 N ATOM 1762 CA GLU B 83 95.949 38.728 -72.241 1.00147.49 C ATOM 1763 C GLU B 83 96.691 38.380 -70.952 1.00149.08 C ATOM 1764 O GLU B 83 96.137 38.500 -69.860 1.00148.84 O ATOM 1765 CB GLU B 83 96.927 39.261 -73.285 1.00144.99 C ATOM 1766 N GLU B 84 97.937 37.939 -71.072 1.00151.53 N ATOM 1767 CA GLU B 84 98.716 37.613 -69.885 1.00153.89 C ATOM 1768 C GLU B 84 99.547 38.847 -69.571 1.00153.70 C ATOM 1769 O GLU B 84 99.628 39.765 -70.389 1.00153.89 O ATOM 1770 CB GLU B 84 99.652 36.425 -70.140 1.00157.34 C ATOM 1771 CG GLU B 84 99.012 35.213 -70.811 1.00160.65 C ATOM 1772 CD GLU B 84 99.016 35.310 -72.332 1.00161.12 C ATOM 1773 OE1 GLU B 84 100.114 35.416 -72.920 1.00159.84 O ATOM 1774 OE2 GLU B 84 97.923 35.275 -72.938 1.00161.97 O ATOM 1775 N GLU B 85 100.153 38.875 -68.389 1.00153.07 N ATOM 1776 CA GLU B 85 100.996 39.998 -67.981 1.00152.32 C ATOM 1777 C GLU B 85 100.214 41.296 -67.772 1.00148.22 C ATOM 1778 O GLU B 85 100.790 42.323 -67.414 1.00147.01 O ATOM 1779 CB GLU B 85 102.097 40.225 -69.027 1.00156.35 C ATOM 1780 CG GLU B 85 103.130 41.275 -68.648 1.00158.61 C ATOM 1781 CD GLU B 85 103.956 40.866 -67.448 1.00159.19 C ATOM 1782 OE1 GLU B 85 104.682 39.854 -67.548 1.00158.87 O ATOM 1783 OE2 GLU B 85 103.875 41.552 -66.407 1.00159.78 O ATOM 1784 N ASP B 86 98.905 41.250 -67.995 1.00144.48 N ATOM 1785 CA ASP B 86 98.067 42.431 -67.821 1.00140.49 C ATOM 1786 C ASP B 86 98.310 43.105 -66.484 1.00135.09 C ATOM 1787 O ASP B 86 99.051 42.597 -65.641 1.00135.34 O ATOM 1788 CB ASP B 86 96.587 42.062 -67.928 1.00144.55 C ATOM 1789 CG ASP B 86 96.015 42.362 -69.291 1.00148.40 C ATOM 1790 OD1 ASP B 86 96.074 43.537 -69.709 1.00150.84 O ATOM 1791 OD2 ASP B 86 95.506 41.428 -69.945 1.00150.51 O ATOM 1792 N VAL B 87 97.672 44.254 -66.293 1.00127.22 N ATOM 1793 CA VAL B 87 97.812 45.006 -65.057 1.00118.79 C ATOM 1794 C VAL B 87 96.474 45.567 -64.611 1.00113.49 C ATOM 1795 O VAL B 87 95.624 45.898 -65.434 1.00112.63 O ATOM 1796 CB VAL B 87 98.801 46.182 -65.227 1.00117.27 C ATOM 1797 CG1 VAL B 87 98.806 47.048 -63.978 1.00115.77 C ATOM 1798 CG2 VAL B 87 100.196 45.651 -65.506 1.00116.38 C ATOM 1799 N ILE B 88 96.287 45.647 -63.299 1.00108.74 N ATOM 1800 CA ILE B 88 95.072 46.204 -62.730 1.00106.10 C ATOM 1801 C ILE B 88 95.493 47.208 -61.672 1.00105.23 C ATOM 1802 O ILE B 88 96.424 46.961 -60.904 1.00102.95 O ATOM 1803 CB ILE B 88 94.173 45.137 -62.060 1.00105.13 C ATOM 1804 CG1 ILE B 88 93.609 44.179 -63.109 1.00105.16 C ATOM 1805 CG2 ILE B 88 93.010 45.816 -61.349 1.00105.09 C ATOM 1806 CD1 ILE B 88 92.603 43.179 -62.553 1.00101.73 C ATOM 1807 N GLU B 89 94.811 48.347 -61.651 1.00105.16 N ATOM 1808 CA GLU B 89 95.099 49.395 -60.685 1.00104.38 C ATOM 1809 C GLU B 89 94.006 49.398 -59.629 1.00 99.74 C ATOM 1810 O GLU B 89 92.837 49.178 -59.940 1.00 98.62 O ATOM 1811 CB GLU B 89 95.133 50.764 -61.371 1.00109.87 C ATOM 1812 CG GLU B 89 96.482 51.467 -61.322 1.00116.14 C ATOM 1813 CD GLU B 89 97.452 50.951 -62.368 1.00119.54 C ATOM 1814 OE1 GLU B 89 97.150 51.100 -63.574 1.00120.65 O ATOM 1815 OE2 GLU B 89 98.511 50.400 -61.988 1.00120.27 O ATOM 1816 N VAL B 90 94.390 49.632 -58.381 1.00 95.94 N ATOM 1817 CA VAL B 90 93.420 49.688 -57.297 1.00 95.75 C ATOM 1818 C VAL B 90 93.562 51.063 -56.672 1.00 97.13 C ATOM 1819 O VAL B 90 94.676 51.529 -56.429 1.00 98.83 O ATOM 1820 CB VAL B 90 93.688 48.626 -56.203 1.00 95.11 C ATOM 1821 CG1 VAL B 90 92.519 48.578 -55.225 1.00 91.08 C ATOM 1822 CG2 VAL B 90 93.901 47.269 -56.830 1.00 98.09 C ATOM 1823 N TYR B 91 92.438 51.721 -56.430 1.00 96.26 N ATOM 1824 CA TYR B 91 92.475 53.036 -55.824 1.00 95.88 C ATOM 1825 C TYR B 91 91.599 53.053 -54.591 1.00 94.74 C ATOM 1826 O TYR B 91 90.505 52.495 -54.593 1.00 92.95 O ATOM 1827 CB TYR B 91 91.987 54.100 -56.804 1.00 99.87 C ATOM 1828 CG TYR B 91 92.861 54.270 -58.023 1.00104.35 C ATOM 1829 CD1 TYR B 91 92.822 53.350 -59.069 1.00105.14 C ATOM 1830 CD2 TYR B 91 93.728 55.357 -58.132 1.00107.01 C ATOM 1831 CE1 TYR B 91 93.625 53.508 -60.200 1.00107.43 C ATOM 1832 CE2 TYR B 91 94.535 55.526 -59.259 1.00109.50 C ATOM 1833 CZ TYR B 91 94.479 54.598 -60.290 1.00108.51 C ATOM 1834 OH TYR B 91 95.276 54.758 -61.404 1.00107.29 O ATOM 1835 N GLN B 92 92.099 53.678 -53.531 1.00 96.07 N ATOM 1836 CA GLN B 92 91.351 53.799 -52.289 1.00 95.96 C ATOM 1837 C GLN B 92 90.074 54.540 -52.671 1.00 96.08 C ATOM 1838 O GLN B 92 90.123 55.523 -53.418 1.00 96.75 O ATOM 1839 CB GLN B 92 92.176 54.597 -51.272 1.00 95.34 C ATOM 1840 CG GLN B 92 91.433 55.075 -50.028 1.00 96.90 C ATOM 1841 CD GLN B 92 90.892 53.950 -49.167 1.00 96.49 C ATOM 1842 OE1 GLN B 92 91.456 52.854 -49.123 1.00 96.22 O ATOM 1843 NE2 GLN B 92 89.802 54.226 -48.454 1.00 94.42 N ATOM 1844 N GLU B 93 88.930 54.062 -52.192 1.00 94.82 N ATOM 1845 CA GLU B 93 87.675 54.713 -52.531 1.00 93.56 C ATOM 1846 C GLU B 93 87.477 55.951 -51.673 1.00 89.01 C ATOM 1847 O GLU B 93 87.815 55.969 -50.486 1.00 87.41 O ATOM 1848 CB GLU B 93 86.492 53.755 -52.365 1.00 99.05 C ATOM 1849 CG GLU B 93 85.246 54.218 -53.116 1.00106.29 C ATOM 1850 CD GLU B 93 85.487 54.375 -54.616 1.00109.61 C ATOM 1851 OE1 GLU B 93 85.459 53.352 -55.340 1.00107.95 O ATOM 1852 OE2 GLU B 93 85.717 55.524 -55.064 1.00110.99 O ATOM 1853 N GLN B 94 86.918 56.984 -52.296 1.00 83.24 N ATOM 1854 CA GLN B 94 86.691 58.260 -51.639 1.00 75.74 C ATOM 1855 C GLN B 94 85.506 58.959 -52.286 1.00 75.28 C ATOM 1856 O GLN B 94 84.994 58.503 -53.309 1.00 77.03 O ATOM 1857 CB GLN B 94 87.926 59.122 -51.825 1.00 70.72 C ATOM 1858 CG GLN B 94 88.205 59.379 -53.294 1.00 63.12 C ATOM 1859 CD GLN B 94 89.554 59.997 -53.534 1.00 59.91 C ATOM 1860 OE1 GLN B 94 90.592 59.363 -53.320 1.00 59.21 O ATOM 1861 NE2 GLN B 94 89.555 61.246 -53.982 1.00 58.74 N ATOM 1862 N THR B 95 85.094 60.075 -51.687 1.00 73.77 N ATOM 1863 CA THR B 95 83.982 60.886 -52.180 1.00 72.52 C ATOM 1864 C THR B 95 84.292 62.349 -51.876 1.00 71.82 C ATOM 1865 O THR B 95 85.198 62.646 -51.095 1.00 71.54 O ATOM 1866 CB THR B 95 82.657 60.525 -51.480 1.00 74.12 C ATOM 1867 OG1 THR B 95 82.763 60.812 -50.079 1.00 77.88 O ATOM 1868 CG2 THR B 95 82.336 59.048 -51.665 1.00 74.59 C ATOM 1869 N GLY B 96 83.542 63.261 -52.488 1.00 71.42 N ATOM 1870 CA GLY B 96 83.769 64.676 -52.244 1.00 70.51 C ATOM 1871 C GLY B 96 83.439 65.060 -50.814 1.00 71.19 C ATOM 1872 O GLY B 96 83.239 64.196 -49.960 1.00 73.22 O ATOM 1873 N GLY B 97 83.383 66.359 -50.548 1.00 71.62 N ATOM 1874 CA GLY B 97 83.068 66.867 -49.212 1.00 72.10 C ATOM 1875 C GLY B 97 82.467 68.266 -49.326 1.00 73.30 C ATOM 1876 O GLY B 97 82.413 68.834 -50.420 1.00 75.82 O TER 3801 HOH A 165 HETATM 3802 O HOH B 98 94.866 56.520 -53.571 1.00 42.65 O HETATM 3803 O HOH B 99 101.131 43.621 -49.867 1.00 33.02 O HETATM 3804 O HOH B 100 83.932 53.182 -47.813 1.00 60.33 O HETATM 3805 O HOH B 101 100.087 42.901 -46.898 1.00 49.30 O CONECT 1875 1874 1876 2676 CONECT 2676 1875 2675 END