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 18 18 ILE A 4 ASP A 19 1 16 HELIX 19 19 LEU A 94 GLU A 98 1 5 HELIX 20 20 THR A 108 GLU A 122 1 15 HELIX 21 21 GLN A 130 LYS A 154 1 25 HELIX 22 22 HIS B 43 ARG B 54 1 12 HELIX 23 23 THR B 76 GLY B 81 1 6 HELIX 24 24 ALA C 432 PHE C 440 1 9 HELIX 25 25 LEU C 446 SER C 454 1 9 HELIX 26 26 LEU C 456 THR C 461 1 6 HELIX 27 27 ASP C 465 SER C 478 1 14 HELIX 28 28 ALA C 484 PHE C 502 1 19 HELIX 29 29 ASN C 508 MET C 520 1 13 HELIX 30 30 LEU C 535 VAL C 546 1 12 HELIX 31 31 LEU C 555 LYS C 565 1 11 HELIX 32 32 SER C 568 VAL C 587 1 20 HELIX 33 33 THR D 2641 LEU D 2651 1 11 HELIX 34 34 ASP D 2676 LEU D 2684 1 9 SHEET 11 11 1 VAL A 25 LYS A 30 0 SHEET 12 12 1 MET A 36 PRO A 46 0 SHEET 13 13 1 LEU A 57 LEU A 63 0 SHEET 14 14 1 LYS A 74 PHE A 77 0 SHEET 15 15 1 ILE B 22 ILE B 27 0 SHEET 16 16 1 GLU B 33 VAL B 38 0 SHEET 17 17 1 PHE B 64 PHE B 66 0 SHEET 18 18 1 GLN B 69 ARG B 70 0 SHEET 19 19 1 VAL B 87 VAL B 90 0 SHEET 20 20 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 67.209 29.860 32.126 1.00137.38 N ATOM 1246 CA GLU B 20 68.074 28.960 32.937 1.00137.58 C ATOM 1247 C GLU B 20 68.836 29.678 34.045 1.00138.27 C ATOM 1248 O GLU B 20 68.302 29.887 35.136 1.00138.04 O ATOM 1249 CB GLU B 20 69.059 28.216 32.032 1.00136.35 C ATOM 1250 CG GLU B 20 68.448 27.009 31.358 1.00136.73 C ATOM 1251 CD GLU B 20 67.839 26.048 32.365 1.00136.96 C ATOM 1252 OE1 GLU B 20 68.587 25.533 33.224 1.00137.05 O ATOM 1253 OE2 GLU B 20 66.615 25.813 32.303 1.00137.00 O ATOM 1254 N TYR B 21 70.081 30.057 33.770 1.00138.79 N ATOM 1255 CA TYR B 21 70.899 30.734 34.772 1.00137.55 C ATOM 1256 C TYR B 21 71.759 31.888 34.257 1.00134.87 C ATOM 1257 O TYR B 21 72.615 31.711 33.387 1.00132.40 O ATOM 1258 CB TYR B 21 71.803 29.717 35.481 1.00140.21 C ATOM 1259 CG TYR B 21 71.062 28.697 36.322 1.00142.70 C ATOM 1260 CD1 TYR B 21 70.258 29.097 37.391 1.00143.17 C ATOM 1261 CD2 TYR B 21 71.171 27.332 36.055 1.00142.73 C ATOM 1262 CE1 TYR B 21 69.583 28.165 38.174 1.00143.12 C ATOM 1263 CE2 TYR B 21 70.500 26.391 36.832 1.00143.39 C ATOM 1264 CZ TYR B 21 69.708 26.816 37.891 1.00143.45 C ATOM 1265 OH TYR B 21 69.048 25.892 38.669 1.00143.47 O ATOM 1266 N ILE B 22 71.521 33.070 34.819 1.00133.97 N ATOM 1267 CA ILE B 22 72.277 34.272 34.479 1.00131.70 C ATOM 1268 C ILE B 22 72.674 34.986 35.771 1.00127.04 C ATOM 1269 O ILE B 22 71.818 35.384 36.569 1.00124.95 O ATOM 1270 CB ILE B 22 71.457 35.239 33.595 1.00133.68 C ATOM 1271 CG1 ILE B 22 70.096 35.512 34.239 1.00135.12 C ATOM 1272 CG2 ILE B 22 71.305 34.660 32.197 1.00133.18 C ATOM 1273 CD1 ILE B 22 69.243 36.500 33.469 1.00136.48 C ATOM 1274 N LYS B 23 73.981 35.123 35.976 1.00121.32 N ATOM 1275 CA LYS B 23 74.523 35.775 37.158 1.00115.15 C ATOM 1276 C LYS B 23 74.280 37.277 37.075 1.00114.57 C ATOM 1277 O LYS B 23 74.656 37.923 36.097 1.00115.41 O ATOM 1278 CB LYS B 23 76.022 35.486 37.264 1.00110.69 C ATOM 1279 CG LYS B 23 76.731 36.186 38.407 1.00105.64 C ATOM 1280 CD LYS B 23 78.202 35.807 38.443 1.00103.74 C ATOM 1281 CE LYS B 23 78.375 34.308 38.656 1.00104.55 C ATOM 1282 NZ LYS B 23 79.805 33.891 38.688 1.00103.76 N ATOM 1283 N LEU B 24 73.645 37.825 38.105 1.00112.64 N ATOM 1284 CA LEU B 24 73.338 39.247 38.158 1.00110.21 C ATOM 1285 C LEU B 24 74.173 39.956 39.216 1.00110.26 C ATOM 1286 O LEU B 24 74.584 39.350 40.205 1.00109.54 O ATOM 1287 CB LEU B 24 71.857 39.451 38.480 1.00109.91 C ATOM 1288 CG LEU B 24 70.809 38.915 37.502 1.00109.51 C ATOM 1289 CD1 LEU B 24 69.426 39.035 38.130 1.00106.85 C ATOM 1290 CD2 LEU B 24 70.882 39.684 36.187 1.00107.70 C ATOM 1291 N LYS B 25 74.420 41.243 38.996 1.00111.16 N ATOM 1292 CA LYS B 25 75.185 42.060 39.935 1.00113.68 C ATOM 1293 C LYS B 25 74.306 43.159 40.533 1.00115.28 C ATOM 1294 O LYS B 25 74.039 44.170 39.880 1.00118.16 O ATOM 1295 CB LYS B 25 76.379 42.725 39.241 1.00112.86 C ATOM 1296 CG LYS B 25 77.611 41.860 39.065 1.00110.70 C ATOM 1297 CD LYS B 25 78.802 42.734 38.698 1.00108.55 C ATOM 1298 CE LYS B 25 80.094 41.944 38.644 1.00107.66 C ATOM 1299 NZ LYS B 25 81.258 42.830 38.373 1.00106.70 N ATOM 1300 N VAL B 26 73.852 42.969 41.767 1.00113.30 N ATOM 1301 CA VAL B 26 73.022 43.976 42.413 1.00110.66 C ATOM 1302 C VAL B 26 73.927 44.926 43.182 1.00110.63 C ATOM 1303 O VAL B 26 74.450 44.586 44.244 1.00110.12 O ATOM 1304 CB VAL B 26 72.012 43.337 43.382 1.00109.24 C ATOM 1305 CG1 VAL B 26 71.108 44.405 43.967 1.00106.08 C ATOM 1306 CG2 VAL B 26 71.191 42.294 42.653 1.00108.86 C ATOM 1307 N ILE B 27 74.122 46.115 42.628 1.00110.16 N ATOM 1308 CA ILE B 27 74.972 47.115 43.250 1.00110.49 C ATOM 1309 C ILE B 27 74.153 48.143 44.010 1.00110.98 C ATOM 1310 O ILE B 27 73.326 48.846 43.430 1.00110.60 O ATOM 1311 CB ILE B 27 75.821 47.842 42.201 1.00111.09 C ATOM 1312 CG1 ILE B 27 76.848 46.876 41.611 1.00111.88 C ATOM 1313 CG2 ILE B 27 76.514 49.034 42.827 1.00113.32 C ATOM 1314 CD1 ILE B 27 77.760 47.506 40.578 1.00112.93 C ATOM 1315 N GLY B 28 74.398 48.226 45.314 1.00112.35 N ATOM 1316 CA GLY B 28 73.681 49.171 46.151 1.00113.66 C ATOM 1317 C GLY B 28 74.222 50.583 46.040 1.00113.71 C ATOM 1318 O GLY B 28 74.970 50.896 45.113 1.00114.16 O ATOM 1319 N GLN B 29 73.853 51.439 46.988 1.00113.16 N ATOM 1320 CA GLN B 29 74.311 52.821 46.965 1.00111.98 C ATOM 1321 C GLN B 29 75.193 53.148 48.160 1.00108.32 C ATOM 1322 O GLN B 29 75.043 54.189 48.794 1.00103.89 O ATOM 1323 CB GLN B 29 73.110 53.768 46.923 1.00114.67 C ATOM 1324 CG GLN B 29 73.379 55.006 46.097 1.00115.93 C ATOM 1325 CD GLN B 29 73.968 54.656 44.744 1.00115.77 C ATOM 1326 OE1 GLN B 29 73.295 54.075 43.889 1.00115.45 O ATOM 1327 NE2 GLN B 29 75.240 54.993 44.547 1.00115.17 N ATOM 1328 N ASP B 30 76.119 52.242 48.451 1.00108.53 N ATOM 1329 CA ASP B 30 77.044 52.402 49.566 1.00110.49 C ATOM 1330 C ASP B 30 78.187 51.396 49.452 1.00110.33 C ATOM 1331 O ASP B 30 78.785 50.992 50.454 1.00107.25 O ATOM 1332 CB ASP B 30 76.301 52.231 50.900 1.00112.62 C ATOM 1333 CG ASP B 30 75.407 51.001 50.928 1.00114.01 C ATOM 1334 OD1 ASP B 30 74.685 50.812 51.932 1.00112.52 O ATOM 1335 OD2 ASP B 30 75.425 50.225 49.950 1.00116.02 O ATOM 1336 N SER B 31 78.480 51.012 48.210 1.00111.75 N ATOM 1337 CA SER B 31 79.539 50.060 47.884 1.00112.50 C ATOM 1338 C SER B 31 79.189 48.616 48.268 1.00111.25 C ATOM 1339 O SER B 31 80.055 47.734 48.291 1.00110.13 O ATOM 1340 CB SER B 31 80.854 50.481 48.547 1.00113.52 C ATOM 1341 OG SER B 31 81.913 49.617 48.171 1.00116.77 O ATOM 1342 N SER B 32 77.912 48.385 48.560 1.00108.59 N ATOM 1343 CA SER B 32 77.427 47.061 48.920 1.00105.70 C ATOM 1344 C SER B 32 77.091 46.290 47.651 1.00107.28 C ATOM 1345 O SER B 32 76.035 46.502 47.057 1.00106.95 O ATOM 1346 CB SER B 32 76.176 47.178 49.791 1.00102.39 C ATOM 1347 OG SER B 32 75.583 45.910 50.009 1.00 99.70 O ATOM 1348 N GLU B 33 77.988 45.402 47.231 1.00109.37 N ATOM 1349 CA GLU B 33 77.759 44.607 46.029 1.00110.31 C ATOM 1350 C GLU B 33 77.391 43.163 46.369 1.00106.90 C ATOM 1351 O GLU B 33 77.968 42.560 47.275 1.00104.00 O ATOM 1352 CB GLU B 33 78.998 44.627 45.126 1.00116.59 C ATOM 1353 CG GLU B 33 78.823 43.833 43.827 1.00125.53 C ATOM 1354 CD GLU B 33 80.029 43.918 42.892 1.00129.71 C ATOM 1355 OE1 GLU B 33 80.362 45.036 42.442 1.00132.45 O ATOM 1356 OE2 GLU B 33 80.641 42.865 42.604 1.00131.04 O ATOM 1357 N ILE B 34 76.423 42.623 45.631 1.00104.73 N ATOM 1358 CA ILE B 34 75.952 41.256 45.831 1.00103.80 C ATOM 1359 C ILE B 34 75.654 40.579 44.496 1.00105.49 C ATOM 1360 O ILE B 34 75.027 41.176 43.621 1.00106.12 O ATOM 1361 CB ILE B 34 74.671 41.234 46.686 1.00101.25 C ATOM 1362 CG1 ILE B 34 74.984 41.745 48.091 1.00100.45 C ATOM 1363 CG2 ILE B 34 74.110 39.825 46.750 1.00100.23 C ATOM 1364 CD1 ILE B 34 73.771 41.889 48.972 1.00 99.24 C ATOM 1365 N HIS B 35 76.100 39.333 44.353 1.00106.50 N ATOM 1366 CA HIS B 35 75.896 38.566 43.127 1.00106.66 C ATOM 1367 C HIS B 35 74.873 37.452 43.290 1.00105.44 C ATOM 1368 O HIS B 35 74.932 36.675 44.242 1.00104.42 O ATOM 1369 CB HIS B 35 77.220 37.970 42.655 1.00109.27 C ATOM 1370 CG HIS B 35 78.173 38.985 42.105 1.00113.01 C ATOM 1371 ND1 HIS B 35 79.441 38.658 41.673 1.00115.57 N ATOM 1372 CD2 HIS B 35 78.038 40.316 41.901 1.00114.15 C ATOM 1373 CE1 HIS B 35 80.046 39.744 41.228 1.00116.16 C ATOM 1374 NE2 HIS B 35 79.217 40.764 41.355 1.00115.62 N ATOM 1375 N PHE B 36 73.943 37.377 42.345 1.00105.58 N ATOM 1376 CA PHE B 36 72.892 36.367 42.370 1.00106.97 C ATOM 1377 C PHE B 36 72.850 35.552 41.080 1.00110.17 C ATOM 1378 O PHE B 36 73.105 36.077 39.994 1.00111.69 O ATOM 1379 CB PHE B 36 71.516 37.027 42.546 1.00104.17 C ATOM 1380 CG PHE B 36 71.333 37.740 43.854 1.00101.87 C ATOM 1381 CD1 PHE B 36 71.292 37.034 45.052 1.00101.69 C ATOM 1382 CD2 PHE B 36 71.176 39.120 43.885 1.00100.11 C ATOM 1383 CE1 PHE B 36 71.096 37.695 46.263 1.00 99.64 C ATOM 1384 CE2 PHE B 36 70.981 39.788 45.089 1.00 99.86 C ATOM 1385 CZ PHE B 36 70.940 39.073 46.280 1.00 99.54 C ATOM 1386 N LYS B 37 72.540 34.263 41.206 1.00111.94 N ATOM 1387 CA LYS B 37 72.383 33.387 40.048 1.00113.55 C ATOM 1388 C LYS B 37 70.882 33.152 40.041 1.00115.25 C ATOM 1389 O LYS B 37 70.329 32.628 41.011 1.00114.21 O ATOM 1390 CB LYS B 37 73.113 32.053 40.233 1.00114.03 C ATOM 1391 CG LYS B 37 74.551 32.028 39.721 1.00114.35 C ATOM 1392 CD LYS B 37 75.150 30.632 39.881 1.00114.05 C ATOM 1393 CE LYS B 37 76.640 30.600 39.566 1.00112.21 C ATOM 1394 NZ LYS B 37 77.234 29.255 39.845 1.00109.34 N ATOM 1395 N VAL B 38 70.215 33.549 38.965 1.00117.18 N ATOM 1396 CA VAL B 38 68.775 33.386 38.925 1.00120.42 C ATOM 1397 C VAL B 38 68.226 32.735 37.671 1.00124.51 C ATOM 1398 O VAL B 38 68.779 32.880 36.578 1.00123.47 O ATOM 1399 CB VAL B 38 68.073 34.738 39.097 1.00118.74 C ATOM 1400 CG1 VAL B 38 66.599 34.520 39.337 1.00119.02 C ATOM 1401 CG2 VAL B 38 68.691 35.502 40.242 1.00119.18 C ATOM 1402 N LYS B 39 67.122 32.015 37.852 1.00129.95 N ATOM 1403 CA LYS B 39 66.436 31.345 36.757 1.00134.80 C ATOM 1404 C LYS B 39 65.573 32.387 36.054 1.00135.00 C ATOM 1405 O LYS B 39 64.747 33.057 36.681 1.00135.09 O ATOM 1406 CB LYS B 39 65.561 30.206 37.290 1.00138.94 C ATOM 1407 CG LYS B 39 66.349 29.047 37.897 1.00142.83 C ATOM 1408 CD LYS B 39 65.423 27.934 38.380 1.00145.43 C ATOM 1409 CE LYS B 39 66.212 26.742 38.913 1.00146.23 C ATOM 1410 NZ LYS B 39 65.329 25.642 39.405 1.00145.42 N ATOM 1411 N MET B 40 65.772 32.520 34.748 1.00133.96 N ATOM 1412 CA MET B 40 65.048 33.496 33.951 1.00132.37 C ATOM 1413 C MET B 40 63.560 33.194 33.805 1.00133.20 C ATOM 1414 O MET B 40 62.910 33.655 32.869 1.00131.50 O ATOM 1415 CB MET B 40 65.723 33.603 32.590 1.00128.82 C ATOM 1416 CG MET B 40 67.216 33.793 32.739 1.00126.43 C ATOM 1417 SD MET B 40 68.094 33.889 31.194 1.00128.56 S ATOM 1418 CE MET B 40 68.527 32.169 30.935 1.00128.03 C ATOM 1419 N THR B 41 63.033 32.422 34.751 1.00135.90 N ATOM 1420 CA THR B 41 61.620 32.053 34.775 1.00138.28 C ATOM 1421 C THR B 41 61.062 32.458 36.135 1.00139.09 C ATOM 1422 O THR B 41 59.863 32.351 36.392 1.00138.98 O ATOM 1423 CB THR B 41 61.423 30.529 34.617 1.00138.35 C ATOM 1424 OG1 THR B 41 62.119 30.074 33.450 1.00140.68 O ATOM 1425 CG2 THR B 41 59.940 30.191 34.480 1.00135.49 C ATOM 1426 N THR B 42 61.954 32.924 37.003 1.00139.33 N ATOM 1427 CA THR B 42 61.581 33.336 38.347 1.00137.29 C ATOM 1428 C THR B 42 61.305 34.834 38.419 1.00134.35 C ATOM 1429 O THR B 42 61.996 35.637 37.785 1.00132.10 O ATOM 1430 CB THR B 42 62.696 32.980 39.359 1.00137.92 C ATOM 1431 OG1 THR B 42 63.886 33.706 39.034 1.00138.06 O ATOM 1432 CG2 THR B 42 63.008 31.488 39.311 1.00137.04 C ATOM 1433 N HIS B 43 60.284 35.195 39.192 1.00132.89 N ATOM 1434 CA HIS B 43 59.899 36.591 39.375 1.00131.83 C ATOM 1435 C HIS B 43 61.025 37.321 40.091 1.00128.30 C ATOM 1436 O HIS B 43 61.507 36.859 41.129 1.00128.83 O ATOM 1437 CB HIS B 43 58.636 36.698 40.236 1.00134.44 C ATOM 1438 CG HIS B 43 57.512 35.822 39.783 1.00136.21 C ATOM 1439 ND1 HIS B 43 56.349 35.676 40.509 1.00136.48 N ATOM 1440 CD2 HIS B 43 57.374 35.037 38.689 1.00136.53 C ATOM 1441 CE1 HIS B 43 55.544 34.839 39.881 1.00137.21 C ATOM 1442 NE2 HIS B 43 56.141 34.437 38.774 1.00137.29 N ATOM 1443 N LEU B 44 61.435 38.462 39.552 1.00121.77 N ATOM 1444 CA LEU B 44 62.501 39.226 40.173 1.00114.70 C ATOM 1445 C LEU B 44 62.209 39.523 41.632 1.00113.03 C ATOM 1446 O LEU B 44 63.132 39.776 42.402 1.00115.59 O ATOM 1447 CB LEU B 44 62.747 40.531 39.417 1.00109.75 C ATOM 1448 CG LEU B 44 63.622 40.386 38.171 1.00107.57 C ATOM 1449 CD1 LEU B 44 63.848 41.745 37.545 1.00108.52 C ATOM 1450 CD2 LEU B 44 64.950 39.765 38.549 1.00105.38 C ATOM 1451 N LYS B 45 60.939 39.487 42.027 1.00109.37 N ATOM 1452 CA LYS B 45 60.619 39.759 43.422 1.00108.03 C ATOM 1453 C LYS B 45 61.457 38.869 44.323 1.00108.20 C ATOM 1454 O LYS B 45 61.958 39.315 45.353 1.00108.14 O ATOM 1455 CB LYS B 45 59.143 39.515 43.728 1.00107.46 C ATOM 1456 CG LYS B 45 58.823 39.783 45.197 1.00107.36 C ATOM 1457 CD LYS B 45 57.368 39.536 45.553 1.00108.78 C ATOM 1458 CE LYS B 45 57.112 39.873 47.020 1.00108.17 C ATOM 1459 NZ LYS B 45 55.695 39.647 47.420 1.00108.76 N ATOM 1460 N LYS B 46 61.606 37.607 43.928 1.00109.39 N ATOM 1461 CA LYS B 46 62.392 36.656 44.706 1.00110.15 C ATOM 1462 C LYS B 46 63.784 37.227 44.951 1.00107.75 C ATOM 1463 O LYS B 46 64.320 37.130 46.058 1.00107.32 O ATOM 1464 CB LYS B 46 62.495 35.319 43.965 1.00112.35 C ATOM 1465 CG LYS B 46 61.149 34.721 43.587 1.00115.86 C ATOM 1466 CD LYS B 46 60.248 34.530 44.807 1.00118.25 C ATOM 1467 CE LYS B 46 58.846 34.075 44.395 1.00120.04 C ATOM 1468 NZ LYS B 46 57.919 33.896 45.551 1.00119.97 N ATOM 1469 N LEU B 47 64.360 37.825 43.911 1.00104.16 N ATOM 1470 CA LEU B 47 65.681 38.435 44.012 1.00100.75 C ATOM 1471 C LEU B 47 65.561 39.583 45.009 1.00102.12 C ATOM 1472 O LEU B 47 66.290 39.643 46.002 1.00103.68 O ATOM 1473 CB LEU B 47 66.129 38.963 42.643 1.00 93.49 C ATOM 1474 CG LEU B 47 67.583 39.430 42.518 1.00 90.12 C ATOM 1475 CD1 LEU B 47 67.925 39.703 41.065 1.00 90.67 C ATOM 1476 CD2 LEU B 47 67.791 40.670 43.349 1.00 88.97 C ATOM 1477 N LYS B 48 64.629 40.488 44.736 1.00101.13 N ATOM 1478 CA LYS B 48 64.380 41.626 45.602 1.00100.45 C ATOM 1479 C LYS B 48 64.364 41.167 47.058 1.00 99.23 C ATOM 1480 O LYS B 48 65.250 41.515 47.835 1.00 99.23 O ATOM 1481 CB LYS B 48 63.036 42.260 45.236 1.00103.00 C ATOM 1482 CG LYS B 48 62.600 43.384 46.149 1.00108.56 C ATOM 1483 CD LYS B 48 61.276 43.976 45.695 1.00112.75 C ATOM 1484 CE LYS B 48 60.824 45.092 46.628 1.00116.89 C ATOM 1485 NZ LYS B 48 59.529 45.689 46.194 1.00119.49 N ATOM 1486 N GLU B 49 63.361 40.369 47.408 1.00 98.70 N ATOM 1487 CA GLU B 49 63.202 39.849 48.767 1.00 99.08 C ATOM 1488 C GLU B 49 64.500 39.362 49.404 1.00 95.59 C ATOM 1489 O GLU B 49 64.853 39.774 50.510 1.00 93.96 O ATOM 1490 CB GLU B 49 62.207 38.692 48.775 1.00103.46 C ATOM 1491 CG GLU B 49 60.873 38.987 48.134 1.00107.76 C ATOM 1492 CD GLU B 49 59.931 37.811 48.242 1.00111.19 C ATOM 1493 OE1 GLU B 49 59.519 37.484 49.377 1.00112.65 O ATOM 1494 OE2 GLU B 49 59.614 37.208 47.194 1.00112.86 O ATOM 1495 N SER B 50 65.190 38.461 48.713 1.00 92.32 N ATOM 1496 CA SER B 50 66.443 37.908 49.211 1.00 91.43 C ATOM 1497 C SER B 50 67.357 39.016 49.709 1.00 91.14 C ATOM 1498 O SER B 50 67.826 38.991 50.850 1.00 90.39 O ATOM 1499 CB SER B 50 67.155 37.128 48.105 1.00 91.53 C ATOM 1500 OG SER B 50 68.401 36.625 48.560 1.00 92.02 O ATOM 1501 N TYR B 51 67.605 39.983 48.833 1.00 89.24 N ATOM 1502 CA TYR B 51 68.460 41.116 49.146 1.00 86.14 C ATOM 1503 C TYR B 51 68.128 41.632 50.539 1.00 84.08 C ATOM 1504 O TYR B 51 68.927 41.545 51.469 1.00 82.62 O ATOM 1505 CB TYR B 51 68.233 42.232 48.126 1.00 86.46 C ATOM 1506 CG TYR B 51 69.332 43.264 48.101 1.00 87.59 C ATOM 1507 CD1 TYR B 51 70.498 43.049 47.367 1.00 88.34 C ATOM 1508 CD2 TYR B 51 69.231 44.433 48.851 1.00 87.81 C ATOM 1509 CE1 TYR B 51 71.539 43.971 47.386 1.00 91.12 C ATOM 1510 CE2 TYR B 51 70.266 45.361 48.879 1.00 90.14 C ATOM 1511 CZ TYR B 51 71.419 45.125 48.146 1.00 92.11 C ATOM 1512 OH TYR B 51 72.456 46.033 48.193 1.00 92.89 O ATOM 1513 N CYS B 52 66.916 42.151 50.661 1.00 83.69 N ATOM 1514 CA CYS B 52 66.408 42.715 51.899 1.00 85.14 C ATOM 1515 C CYS B 52 66.664 41.917 53.172 1.00 83.93 C ATOM 1516 O CYS B 52 67.169 42.464 54.146 1.00 82.84 O ATOM 1517 CB CYS B 52 64.917 42.967 51.740 1.00 88.25 C ATOM 1518 SG CYS B 52 64.556 43.945 50.271 1.00 94.15 S ATOM 1519 N GLN B 53 66.312 40.635 53.175 1.00 85.39 N ATOM 1520 CA GLN B 53 66.517 39.808 54.362 1.00 86.42 C ATOM 1521 C GLN B 53 67.987 39.452 54.582 1.00 84.41 C ATOM 1522 O GLN B 53 68.437 39.323 55.722 1.00 81.66 O ATOM 1523 CB GLN B 53 65.655 38.540 54.280 1.00 90.66 C ATOM 1524 CG GLN B 53 65.892 37.665 53.060 1.00 95.08 C ATOM 1525 CD GLN B 53 66.920 36.585 53.317 1.00 99.56 C ATOM 1526 OE1 GLN B 53 66.801 35.816 54.276 1.00101.22 O ATOM 1527 NE2 GLN B 53 67.936 36.511 52.457 1.00101.75 N ATOM 1528 N ARG B 54 68.732 39.298 53.493 1.00 83.91 N ATOM 1529 CA ARG B 54 70.152 38.987 53.592 1.00 83.87 C ATOM 1530 C ARG B 54 70.873 40.307 53.814 1.00 82.95 C ATOM 1531 O ARG B 54 72.085 40.409 53.640 1.00 82.79 O ATOM 1532 CB ARG B 54 70.646 38.311 52.305 1.00 87.44 C ATOM 1533 CG ARG B 54 72.170 38.237 52.153 1.00 91.81 C ATOM 1534 CD ARG B 54 72.854 37.540 53.322 1.00 97.29 C ATOM 1535 NE ARG B 54 73.014 36.101 53.114 1.00104.04 N ATOM 1536 CZ ARG B 54 73.845 35.561 52.226 1.00105.16 C ATOM 1537 NH1 ARG B 54 74.597 36.338 51.456 1.00104.58 N ATOM 1538 NH2 ARG B 54 73.931 34.241 52.111 1.00104.24 N ATOM 1539 N GLN B 55 70.111 41.321 54.207 1.00 83.44 N ATOM 1540 CA GLN B 55 70.675 42.640 54.452 1.00 83.74 C ATOM 1541 C GLN B 55 69.967 43.338 55.613 1.00 84.06 C ATOM 1542 O GLN B 55 70.372 44.420 56.034 1.00 84.62 O ATOM 1543 CB GLN B 55 70.564 43.491 53.186 1.00 82.88 C ATOM 1544 CG GLN B 55 71.548 44.642 53.133 1.00 86.84 C ATOM 1545 CD GLN B 55 72.994 44.174 53.059 1.00 90.06 C ATOM 1546 OE1 GLN B 55 73.432 43.618 52.046 1.00 88.09 O ATOM 1547 NE2 GLN B 55 73.743 44.392 54.140 1.00 91.86 N ATOM 1548 N GLY B 56 68.912 42.710 56.124 1.00 84.66 N ATOM 1549 CA GLY B 56 68.157 43.273 57.233 1.00 84.15 C ATOM 1550 C GLY B 56 67.494 44.601 56.920 1.00 83.88 C ATOM 1551 O GLY B 56 67.729 45.589 57.606 1.00 84.37 O ATOM 1552 N VAL B 57 66.652 44.620 55.894 1.00 85.02 N ATOM 1553 CA VAL B 57 65.969 45.841 55.478 1.00 87.68 C ATOM 1554 C VAL B 57 64.605 45.516 54.876 1.00 90.25 C ATOM 1555 O VAL B 57 64.519 44.762 53.913 1.00 93.20 O ATOM 1556 CB VAL B 57 66.796 46.585 54.412 1.00 88.15 C ATOM 1557 CG1 VAL B 57 66.031 47.783 53.899 1.00 88.73 C ATOM 1558 CG2 VAL B 57 68.129 47.014 54.997 1.00 89.76 C ATOM 1559 N PRO B 58 63.524 46.099 55.421 1.00 90.88 N ATOM 1560 CA PRO B 58 62.169 45.848 54.913 1.00 92.54 C ATOM 1561 C PRO B 58 62.013 45.949 53.395 1.00 94.72 C ATOM 1562 O PRO B 58 62.559 46.850 52.759 1.00 92.83 O ATOM 1563 CB PRO B 58 61.321 46.874 55.666 1.00 91.15 C ATOM 1564 CG PRO B 58 62.292 47.962 55.984 1.00 89.63 C ATOM 1565 CD PRO B 58 63.505 47.185 56.411 1.00 90.54 C ATOM 1566 N MET B 59 61.258 45.008 52.834 1.00 98.17 N ATOM 1567 CA MET B 59 61.000 44.924 51.396 1.00102.39 C ATOM 1568 C MET B 59 60.781 46.282 50.722 1.00103.95 C ATOM 1569 O MET B 59 61.154 46.483 49.560 1.00101.59 O ATOM 1570 CB MET B 59 59.770 44.039 51.156 1.00104.38 C ATOM 1571 CG MET B 59 59.546 43.612 49.709 1.00106.07 C ATOM 1572 SD MET B 59 60.737 42.370 49.167 1.00109.24 S ATOM 1573 CE MET B 59 60.548 41.142 50.487 1.00109.82 C ATOM 1574 N ASN B 60 60.170 47.208 51.455 1.00105.96 N ATOM 1575 CA ASN B 60 59.876 48.539 50.936 1.00107.32 C ATOM 1576 C ASN B 60 61.074 49.475 50.991 1.00106.77 C ATOM 1577 O ASN B 60 61.484 50.029 49.975 1.00107.19 O ATOM 1578 CB ASN B 60 58.720 49.166 51.722 1.00108.99 C ATOM 1579 CG ASN B 60 59.044 49.341 53.199 1.00109.90 C ATOM 1580 OD1 ASN B 60 59.227 48.365 53.927 1.00110.89 O ATOM 1581 ND2 ASN B 60 59.121 50.593 53.643 1.00108.80 N ATOM 1582 N SER B 61 61.615 49.645 52.191 1.00105.11 N ATOM 1583 CA SER B 61 62.752 50.519 52.444 1.00103.26 C ATOM 1584 C SER B 61 63.603 50.851 51.220 1.00100.04 C ATOM 1585 O SER B 61 64.004 51.997 51.043 1.00101.63 O ATOM 1586 CB SER B 61 63.634 49.908 53.539 1.00105.92 C ATOM 1587 OG SER B 61 64.672 50.792 53.946 1.00108.14 O ATOM 1588 N LEU B 62 63.871 49.868 50.369 1.00 96.52 N ATOM 1589 CA LEU B 62 64.700 50.114 49.193 1.00 96.90 C ATOM 1590 C LEU B 62 63.914 50.326 47.899 1.00 98.84 C ATOM 1591 O LEU B 62 62.727 50.644 47.917 1.00 99.71 O ATOM 1592 CB LEU B 62 65.672 48.954 48.991 1.00 95.39 C ATOM 1593 CG LEU B 62 66.355 48.388 50.236 1.00 93.30 C ATOM 1594 CD1 LEU B 62 67.296 47.280 49.807 1.00 92.00 C ATOM 1595 CD2 LEU B 62 67.106 49.482 50.979 1.00 93.63 C ATOM 1596 N ARG B 63 64.613 50.155 46.780 1.00100.55 N ATOM 1597 CA ARG B 63 64.053 50.289 45.435 1.00102.07 C ATOM 1598 C ARG B 63 65.132 49.798 44.474 1.00101.66 C ATOM 1599 O ARG B 63 66.298 50.173 44.612 1.00102.86 O ATOM 1600 CB ARG B 63 63.713 51.749 45.124 1.00105.13 C ATOM 1601 CG ARG B 63 63.287 51.983 43.682 1.00108.71 C ATOM 1602 CD ARG B 63 63.262 53.466 43.322 1.00113.29 C ATOM 1603 NE ARG B 63 62.093 54.172 43.844 1.00115.43 N ATOM 1604 CZ ARG B 63 61.859 55.468 43.647 1.00115.94 C ATOM 1605 NH1 ARG B 63 62.717 56.199 42.944 1.00114.96 N ATOM 1606 NH2 ARG B 63 60.763 56.033 44.140 1.00116.32 N ATOM 1607 N PHE B 64 64.753 48.960 43.511 1.00 99.51 N ATOM 1608 CA PHE B 64 65.716 48.411 42.558 1.00 97.92 C ATOM 1609 C PHE B 64 65.463 48.924 41.146 1.00100.47 C ATOM 1610 O PHE B 64 64.316 49.073 40.733 1.00102.03 O ATOM 1611 CB PHE B 64 65.652 46.881 42.575 1.00 93.20 C ATOM 1612 CG PHE B 64 65.769 46.286 43.950 1.00 89.08 C ATOM 1613 CD1 PHE B 64 64.772 46.491 44.901 1.00 89.23 C ATOM 1614 CD2 PHE B 64 66.884 45.542 44.307 1.00 87.73 C ATOM 1615 CE1 PHE B 64 64.884 45.967 46.189 1.00 86.69 C ATOM 1616 CE2 PHE B 64 67.008 45.014 45.591 1.00 88.60 C ATOM 1617 CZ PHE B 64 66.004 45.229 46.533 1.00 87.63 C ATOM 1618 N LEU B 65 66.538 49.179 40.405 1.00103.33 N ATOM 1619 CA LEU B 65 66.415 49.693 39.045 1.00107.48 C ATOM 1620 C LEU B 65 67.234 48.923 38.012 1.00110.46 C ATOM 1621 O LEU B 65 68.185 48.214 38.349 1.00110.78 O ATOM 1622 CB LEU B 65 66.845 51.161 39.003 1.00109.58 C ATOM 1623 CG LEU B 65 66.302 52.111 40.070 1.00111.80 C ATOM 1624 CD1 LEU B 65 66.889 53.492 39.835 1.00113.23 C ATOM 1625 CD2 LEU B 65 64.781 52.154 40.024 1.00112.65 C ATOM 1626 N PHE B 66 66.853 49.085 36.748 1.00111.89 N ATOM 1627 CA PHE B 66 67.537 48.453 35.627 1.00111.36 C ATOM 1628 C PHE B 66 67.362 49.345 34.397 1.00112.80 C ATOM 1629 O PHE B 66 66.305 49.953 34.211 1.00112.03 O ATOM 1630 CB PHE B 66 66.959 47.063 35.356 1.00109.17 C ATOM 1631 CG PHE B 66 67.612 46.360 34.205 1.00108.88 C ATOM 1632 CD1 PHE B 66 68.986 46.159 34.188 1.00109.04 C ATOM 1633 CD2 PHE B 66 66.859 45.916 33.123 1.00109.11 C ATOM 1634 CE1 PHE B 66 69.604 45.529 33.108 1.00108.06 C ATOM 1635 CE2 PHE B 66 67.466 45.284 32.037 1.00107.87 C ATOM 1636 CZ PHE B 66 68.841 45.091 32.032 1.00106.51 C ATOM 1637 N GLU B 67 68.395 49.423 33.562 1.00114.44 N ATOM 1638 CA GLU B 67 68.349 50.267 32.371 1.00117.24 C ATOM 1639 C GLU B 67 67.845 51.649 32.773 1.00118.65 C ATOM 1640 O GLU B 67 67.203 52.347 31.988 1.00120.62 O ATOM 1641 CB GLU B 67 67.414 49.671 31.313 1.00120.96 C ATOM 1642 CG GLU B 67 67.943 48.433 30.599 1.00125.12 C ATOM 1643 CD GLU B 67 66.981 47.913 29.531 1.00127.52 C ATOM 1644 OE1 GLU B 67 65.838 47.542 29.882 1.00127.22 O ATOM 1645 OE2 GLU B 67 67.365 47.875 28.340 1.00127.81 O ATOM 1646 N GLY B 68 68.136 52.034 34.010 1.00118.79 N ATOM 1647 CA GLY B 68 67.696 53.325 34.496 1.00119.45 C ATOM 1648 C GLY B 68 66.289 53.267 35.055 1.00120.62 C ATOM 1649 O GLY B 68 66.027 53.804 36.132 1.00120.92 O ATOM 1650 N GLN B 69 65.380 52.611 34.338 1.00120.78 N ATOM 1651 CA GLN B 69 63.996 52.514 34.790 1.00121.40 C ATOM 1652 C GLN B 69 63.761 51.490 35.898 1.00120.80 C ATOM 1653 O GLN B 69 64.443 50.465 35.980 1.00119.77 O ATOM 1654 CB GLN B 69 63.064 52.231 33.605 1.00122.00 C ATOM 1655 CG GLN B 69 62.948 53.406 32.640 1.00122.38 C ATOM 1656 CD GLN B 69 61.760 53.293 31.702 1.00121.48 C ATOM 1657 OE1 GLN B 69 61.641 52.331 30.943 1.00122.01 O ATOM 1658 NE2 GLN B 69 60.874 54.283 31.749 1.00119.53 N ATOM 1659 N ARG B 70 62.782 51.791 36.745 1.00119.70 N ATOM 1660 CA ARG B 70 62.419 50.951 37.879 1.00118.23 C ATOM 1661 C ARG B 70 62.156 49.496 37.509 1.00119.24 C ATOM 1662 O ARG B 70 62.039 49.153 36.333 1.00118.96 O ATOM 1663 CB ARG B 70 61.194 51.543 38.574 1.00115.97 C ATOM 1664 CG ARG B 70 60.885 50.937 39.917 1.00115.74 C ATOM 1665 CD ARG B 70 60.012 51.872 40.722 1.00118.92 C ATOM 1666 NE ARG B 70 59.939 51.469 42.122 1.00123.64 N ATOM 1667 CZ ARG B 70 59.466 52.238 43.097 1.00126.18 C ATOM 1668 NH1 ARG B 70 59.020 53.458 42.821 1.00127.77 N ATOM 1669 NH2 ARG B 70 59.443 51.793 44.348 1.00126.21 N ATOM 1670 N ILE B 71 62.068 48.644 38.525 1.00121.20 N ATOM 1671 CA ILE B 71 61.824 47.221 38.320 1.00122.34 C ATOM 1672 C ILE B 71 60.513 46.753 38.945 1.00123.66 C ATOM 1673 O ILE B 71 60.269 46.949 40.139 1.00122.04 O ATOM 1674 CB ILE B 71 62.975 46.363 38.893 1.00120.83 C ATOM 1675 CG1 ILE B 71 64.223 46.531 38.023 1.00121.17 C ATOM 1676 CG2 ILE B 71 62.559 44.902 38.958 1.00118.50 C ATOM 1677 CD1 ILE B 71 65.416 45.722 38.493 1.00121.87 C ATOM 1678 N ALA B 72 59.681 46.125 38.115 1.00124.69 N ATOM 1679 CA ALA B 72 58.387 45.607 38.543 1.00123.31 C ATOM 1680 C ALA B 72 58.595 44.478 39.533 1.00121.97 C ATOM 1681 O ALA B 72 59.612 43.785 39.497 1.00121.55 O ATOM 1682 CB ALA B 72 57.589 45.106 37.337 1.00121.30 C ATOM 1683 N ASP B 73 57.621 44.294 40.414 1.00120.96 N ATOM 1684 CA ASP B 73 57.693 43.254 41.424 1.00121.43 C ATOM 1685 C ASP B 73 57.471 41.866 40.816 1.00122.56 C ATOM 1686 O ASP B 73 57.884 40.854 41.385 1.00121.24 O ATOM 1687 CB ASP B 73 56.651 43.532 42.503 1.00121.68 C ATOM 1688 CG ASP B 73 57.000 42.893 43.820 1.00122.33 C ATOM 1689 OD1 ASP B 73 58.094 43.192 44.349 1.00120.08 O ATOM 1690 OD2 ASP B 73 56.182 42.096 44.326 1.00124.11 O ATOM 1691 N ASN B 74 56.821 41.829 39.656 1.00125.07 N ATOM 1692 CA ASN B 74 56.538 40.579 38.953 1.00125.90 C ATOM 1693 C ASN B 74 57.474 40.401 37.770 1.00128.02 C ATOM 1694 O ASN B 74 57.410 39.399 37.060 1.00127.04 O ATOM 1695 CB ASN B 74 55.091 40.565 38.462 1.00124.25 C ATOM 1696 CG ASN B 74 54.094 40.437 39.595 1.00124.47 C ATOM 1697 OD1 ASN B 74 52.892 40.617 39.402 1.00124.44 O ATOM 1698 ND2 ASN B 74 54.590 40.113 40.785 1.00124.64 N ATOM 1699 N HIS B 75 58.345 41.385 37.569 1.00132.15 N ATOM 1700 CA HIS B 75 59.316 41.366 36.480 1.00136.28 C ATOM 1701 C HIS B 75 60.147 40.079 36.478 1.00136.45 C ATOM 1702 O HIS B 75 60.106 39.301 37.431 1.00138.15 O ATOM 1703 CB HIS B 75 60.254 42.572 36.601 1.00139.50 C ATOM 1704 CG HIS B 75 60.286 43.440 35.382 1.00142.04 C ATOM 1705 ND1 HIS B 75 60.576 42.951 34.126 1.00142.47 N ATOM 1706 CD2 HIS B 75 60.061 44.766 35.226 1.00142.36 C ATOM 1707 CE1 HIS B 75 60.525 43.938 33.250 1.00142.60 C ATOM 1708 NE2 HIS B 75 60.214 45.050 33.892 1.00142.80 N ATOM 1709 N THR B 76 60.900 39.877 35.401 1.00133.74 N ATOM 1710 CA THR B 76 61.766 38.714 35.230 1.00132.45 C ATOM 1711 C THR B 76 62.449 38.915 33.893 1.00130.73 C ATOM 1712 O THR B 76 61.846 39.475 32.984 1.00129.04 O ATOM 1713 CB THR B 76 60.961 37.393 35.175 1.00134.70 C ATOM 1714 OG1 THR B 76 60.337 37.153 36.441 1.00137.57 O ATOM 1715 CG2 THR B 76 61.872 36.218 34.845 1.00134.69 C ATOM 1716 N PRO B 77 63.716 38.477 33.756 1.00131.67 N ATOM 1717 CA PRO B 77 64.448 38.629 32.492 1.00132.49 C ATOM 1718 C PRO B 77 63.582 38.214 31.308 1.00134.35 C ATOM 1719 O PRO B 77 63.911 38.476 30.149 1.00133.51 O ATOM 1720 CB PRO B 77 65.653 37.720 32.686 1.00130.98 C ATOM 1721 CG PRO B 77 65.945 37.902 34.132 1.00130.10 C ATOM 1722 CD PRO B 77 64.568 37.831 34.771 1.00131.07 C ATOM 1723 N LYS B 78 62.472 37.555 31.627 1.00136.34 N ATOM 1724 CA LYS B 78 61.504 37.108 30.639 1.00137.74 C ATOM 1725 C LYS B 78 60.969 38.363 29.956 1.00138.88 C ATOM 1726 O LYS B 78 60.469 38.315 28.832 1.00139.63 O ATOM 1727 CB LYS B 78 60.364 36.362 31.343 1.00137.27 C ATOM 1728 CG LYS B 78 59.232 35.897 30.435 1.00137.09 C ATOM 1729 CD LYS B 78 58.107 35.270 31.250 1.00136.51 C ATOM 1730 CE LYS B 78 56.918 34.901 30.375 1.00136.59 C ATOM 1731 NZ LYS B 78 55.777 34.374 31.180 1.00136.28 N ATOM 1732 N GLU B 79 61.097 39.488 30.653 1.00139.23 N ATOM 1733 CA GLU B 79 60.632 40.773 30.155 1.00139.27 C ATOM 1734 C GLU B 79 61.783 41.753 29.937 1.00139.93 C ATOM 1735 O GLU B 79 61.731 42.584 29.032 1.00141.81 O ATOM 1736 CB GLU B 79 59.641 41.383 31.148 1.00138.96 C ATOM 1737 CG GLU B 79 58.527 40.447 31.572 1.00140.83 C ATOM 1738 CD GLU B 79 57.674 39.996 30.405 1.00143.23 C ATOM 1739 OE1 GLU B 79 57.133 40.867 29.692 1.00145.11 O ATOM 1740 OE2 GLU B 79 57.543 38.770 30.204 1.00143.96 O ATOM 1741 N LEU B 80 62.819 41.652 30.770 1.00138.87 N ATOM 1742 CA LEU B 80 63.975 42.544 30.688 1.00136.13 C ATOM 1743 C LEU B 80 65.087 42.065 29.769 1.00135.52 C ATOM 1744 O LEU B 80 66.004 42.826 29.454 1.00133.21 O ATOM 1745 CB LEU B 80 64.554 42.780 32.081 1.00134.56 C ATOM 1746 CG LEU B 80 63.679 43.611 33.013 1.00133.54 C ATOM 1747 CD1 LEU B 80 64.297 43.689 34.398 1.00133.42 C ATOM 1748 CD2 LEU B 80 63.517 44.996 32.416 1.00134.44 C ATOM 1749 N GLY B 81 65.008 40.810 29.345 1.00136.64 N ATOM 1750 CA GLY B 81 66.028 40.268 28.468 1.00138.78 C ATOM 1751 C GLY B 81 67.421 40.507 29.016 1.00139.61 C ATOM 1752 O GLY B 81 68.387 40.645 28.268 1.00137.88 O ATOM 1753 N MET B 82 67.521 40.562 30.338 1.00141.93 N ATOM 1754 CA MET B 82 68.802 40.784 30.983 1.00144.62 C ATOM 1755 C MET B 82 69.755 39.638 30.672 1.00145.50 C ATOM 1756 O MET B 82 69.485 38.491 31.027 1.00146.03 O ATOM 1757 CB MET B 82 68.617 40.893 32.499 1.00147.33 C ATOM 1758 CG MET B 82 67.648 41.979 32.935 1.00151.33 C ATOM 1759 SD MET B 82 67.628 42.233 34.728 1.00154.69 S ATOM 1760 CE MET B 82 66.339 41.101 35.231 1.00154.31 C ATOM 1761 N GLU B 83 70.862 39.945 30.002 1.00146.38 N ATOM 1762 CA GLU B 83 71.858 38.928 29.674 1.00147.49 C ATOM 1763 C GLU B 83 72.599 38.575 30.962 1.00149.08 C ATOM 1764 O GLU B 83 72.046 38.693 32.054 1.00148.84 O ATOM 1765 CB GLU B 83 72.837 39.463 28.631 1.00144.99 C ATOM 1766 N GLU B 84 73.845 38.133 30.840 1.00151.53 N ATOM 1767 CA GLU B 84 74.623 37.802 32.026 1.00153.89 C ATOM 1768 C GLU B 84 75.456 39.034 32.344 1.00153.70 C ATOM 1769 O GLU B 84 75.538 39.954 31.529 1.00153.89 O ATOM 1770 CB GLU B 84 75.557 36.614 31.768 1.00157.34 C ATOM 1771 CG GLU B 84 74.916 35.405 31.093 1.00160.65 C ATOM 1772 CD GLU B 84 74.920 35.506 29.573 1.00161.12 C ATOM 1773 OE1 GLU B 84 76.018 35.612 28.985 1.00159.84 O ATOM 1774 OE2 GLU B 84 73.827 35.474 28.967 1.00161.97 O ATOM 1775 N GLU B 85 76.062 39.058 33.526 1.00153.07 N ATOM 1776 CA GLU B 85 76.907 40.178 33.937 1.00152.32 C ATOM 1777 C GLU B 85 76.127 41.477 34.150 1.00148.22 C ATOM 1778 O GLU B 85 76.704 42.502 34.511 1.00147.01 O ATOM 1779 CB GLU B 85 78.008 40.407 32.892 1.00156.35 C ATOM 1780 CG GLU B 85 79.043 41.454 33.274 1.00158.61 C ATOM 1781 CD GLU B 85 79.868 41.040 34.473 1.00159.19 C ATOM 1782 OE1 GLU B 85 80.593 40.027 34.370 1.00158.87 O ATOM 1783 OE2 GLU B 85 79.788 41.723 35.516 1.00159.78 O ATOM 1784 N ASP B 86 74.818 41.433 33.927 1.00144.48 N ATOM 1785 CA ASP B 86 73.982 42.615 34.104 1.00140.49 C ATOM 1786 C ASP B 86 74.226 43.285 35.443 1.00135.09 C ATOM 1787 O ASP B 86 74.966 42.773 36.285 1.00135.34 O ATOM 1788 CB ASP B 86 72.501 42.249 33.996 1.00144.55 C ATOM 1789 CG ASP B 86 71.929 42.554 32.634 1.00148.40 C ATOM 1790 OD1 ASP B 86 71.990 43.730 32.220 1.00150.84 O ATOM 1791 OD2 ASP B 86 71.419 41.622 31.978 1.00150.51 O ATOM 1792 N VAL B 87 73.589 44.434 35.638 1.00127.22 N ATOM 1793 CA VAL B 87 73.731 45.183 36.876 1.00118.79 C ATOM 1794 C VAL B 87 72.394 45.744 37.324 1.00113.49 C ATOM 1795 O VAL B 87 71.544 46.079 36.502 1.00112.63 O ATOM 1796 CB VAL B 87 74.721 46.358 36.709 1.00117.27 C ATOM 1797 CG1 VAL B 87 74.728 47.220 37.961 1.00115.77 C ATOM 1798 CG2 VAL B 87 76.116 45.825 36.429 1.00116.38 C ATOM 1799 N ILE B 88 72.207 45.821 38.636 1.00108.74 N ATOM 1800 CA ILE B 88 70.993 46.378 39.206 1.00106.10 C ATOM 1801 C ILE B 88 71.415 47.378 40.267 1.00105.23 C ATOM 1802 O ILE B 88 72.346 47.128 41.035 1.00102.95 O ATOM 1803 CB ILE B 88 70.092 45.310 39.873 1.00105.13 C ATOM 1804 CG1 ILE B 88 69.526 44.356 38.822 1.00105.16 C ATOM 1805 CG2 ILE B 88 68.930 45.989 40.586 1.00105.09 C ATOM 1806 CD1 ILE B 88 68.519 43.356 39.375 1.00101.73 C ATOM 1807 N GLU B 89 70.735 48.518 40.292 1.00105.16 N ATOM 1808 CA GLU B 89 71.024 49.563 41.261 1.00104.38 C ATOM 1809 C GLU B 89 69.931 49.565 42.317 1.00 99.74 C ATOM 1810 O GLU B 89 68.762 49.347 42.005 1.00 98.62 O ATOM 1811 CB GLU B 89 71.061 50.934 40.579 1.00109.87 C ATOM 1812 CG GLU B 89 72.411 51.635 40.630 1.00116.14 C ATOM 1813 CD GLU B 89 73.380 51.120 39.582 1.00119.54 C ATOM 1814 OE1 GLU B 89 73.078 51.273 38.377 1.00120.65 O ATOM 1815 OE2 GLU B 89 74.438 50.567 39.961 1.00120.27 O ATOM 1816 N VAL B 90 70.316 49.794 43.565 1.00 95.94 N ATOM 1817 CA VAL B 90 69.346 49.849 44.650 1.00 95.75 C ATOM 1818 C VAL B 90 69.490 51.222 45.279 1.00 97.13 C ATOM 1819 O VAL B 90 70.605 51.685 45.523 1.00 98.83 O ATOM 1820 CB VAL B 90 69.612 48.783 45.741 1.00 95.11 C ATOM 1821 CG1 VAL B 90 68.443 48.734 46.718 1.00 91.08 C ATOM 1822 CG2 VAL B 90 69.823 47.428 45.110 1.00 98.09 C ATOM 1823 N TYR B 91 68.367 51.881 45.523 1.00 96.26 N ATOM 1824 CA TYR B 91 68.406 53.194 46.132 1.00 95.88 C ATOM 1825 C TYR B 91 67.530 53.209 47.366 1.00 94.74 C ATOM 1826 O TYR B 91 66.435 52.652 47.362 1.00 92.95 O ATOM 1827 CB TYR B 91 67.920 54.261 45.156 1.00 99.87 C ATOM 1828 CG TYR B 91 68.794 54.434 43.937 1.00104.35 C ATOM 1829 CD1 TYR B 91 68.754 53.517 42.888 1.00105.14 C ATOM 1830 CD2 TYR B 91 69.663 55.520 43.831 1.00107.01 C ATOM 1831 CE1 TYR B 91 69.557 53.677 41.758 1.00107.43 C ATOM 1832 CE2 TYR B 91 70.470 55.691 42.705 1.00109.50 C ATOM 1833 CZ TYR B 91 70.412 54.766 41.671 1.00108.51 C ATOM 1834 OH TYR B 91 71.210 54.928 40.557 1.00107.29 O ATOM 1835 N GLN B 92 68.031 53.830 48.427 1.00 96.07 N ATOM 1836 CA GLN B 92 67.283 53.948 49.670 1.00 95.96 C ATOM 1837 C GLN B 92 66.008 54.692 49.290 1.00 96.08 C ATOM 1838 O GLN B 92 66.058 55.677 48.546 1.00 96.75 O ATOM 1839 CB GLN B 92 68.110 54.742 50.689 1.00 95.34 C ATOM 1840 CG GLN B 92 67.367 55.217 51.934 1.00 96.90 C ATOM 1841 CD GLN B 92 66.825 54.091 52.792 1.00 96.49 C ATOM 1842 OE1 GLN B 92 67.387 52.994 52.833 1.00 96.22 O ATOM 1843 NE2 GLN B 92 65.735 54.366 53.506 1.00 94.42 N ATOM 1844 N GLU B 93 64.863 54.215 49.768 1.00 94.82 N ATOM 1845 CA GLU B 93 63.609 54.868 49.430 1.00 93.56 C ATOM 1846 C GLU B 93 63.413 56.104 50.292 1.00 89.01 C ATOM 1847 O GLU B 93 63.751 56.118 51.479 1.00 87.41 O ATOM 1848 CB GLU B 93 62.424 53.912 49.594 1.00 99.05 C ATOM 1849 CG GLU B 93 61.179 54.379 48.844 1.00106.29 C ATOM 1850 CD GLU B 93 61.420 54.540 47.345 1.00109.61 C ATOM 1851 OE1 GLU B 93 61.391 53.519 46.618 1.00107.95 O ATOM 1852 OE2 GLU B 93 61.652 55.690 46.900 1.00110.99 O ATOM 1853 N GLN B 94 62.855 57.140 49.672 1.00 83.24 N ATOM 1854 CA GLN B 94 62.630 58.414 50.333 1.00 75.74 C ATOM 1855 C GLN B 94 61.446 59.117 49.688 1.00 75.28 C ATOM 1856 O GLN B 94 60.934 58.665 48.664 1.00 77.03 O ATOM 1857 CB GLN B 94 63.867 59.275 50.149 1.00 70.72 C ATOM 1858 CG GLN B 94 64.146 59.536 48.681 1.00 63.12 C ATOM 1859 CD GLN B 94 65.496 60.153 48.443 1.00 59.91 C ATOM 1860 OE1 GLN B 94 66.533 59.516 48.655 1.00 59.21 O ATOM 1861 NE2 GLN B 94 65.499 61.403 47.998 1.00 58.74 N ATOM 1862 N THR B 95 61.036 60.232 50.290 1.00 73.77 N ATOM 1863 CA THR B 95 59.925 61.046 49.800 1.00 72.52 C ATOM 1864 C THR B 95 60.237 62.508 50.108 1.00 71.82 C ATOM 1865 O THR B 95 61.144 62.801 50.890 1.00 71.54 O ATOM 1866 CB THR B 95 58.600 60.685 50.499 1.00 74.12 C ATOM 1867 OG1 THR B 95 58.706 60.968 51.900 1.00 77.88 O ATOM 1868 CG2 THR B 95 58.276 59.209 50.309 1.00 74.59 C ATOM 1869 N GLY B 96 59.489 63.423 49.499 1.00 71.42 N ATOM 1870 CA GLY B 96 59.718 64.837 49.747 1.00 70.51 C ATOM 1871 C GLY B 96 59.389 65.217 51.178 1.00 71.19 C ATOM 1872 O GLY B 96 59.187 64.351 52.029 1.00 73.22 O ATOM 1873 N GLY B 97 59.335 66.515 51.448 1.00 71.62 N ATOM 1874 CA GLY B 97 59.020 67.020 52.785 1.00 72.10 C ATOM 1875 C GLY B 97 58.422 68.420 52.675 1.00 73.30 C ATOM 1876 O GLY B 97 58.368 68.991 51.583 1.00 75.82 O TER 3801 HOH A 165 HETATM 3802 O HOH B 98 70.803 56.668 48.396 1.00 42.65 O HETATM 3803 O HOH B 99 77.048 43.748 52.062 1.00 33.02 O HETATM 3804 O HOH B 100 59.864 53.329 54.144 1.00 60.33 O HETATM 3805 O HOH B 101 76.003 43.021 55.029 1.00 49.30 O CONECT 1875 1874 1876 2676 CONECT 2676 1875 2675 END