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 59.273 23.652 24.253 1.00137.38 N ATOM 1246 CA GLU B 20 60.138 22.755 25.067 1.00137.58 C ATOM 1247 C GLU B 20 60.900 23.478 26.172 1.00138.27 C ATOM 1248 O GLU B 20 60.366 23.690 27.262 1.00138.04 O ATOM 1249 CB GLU B 20 61.124 22.009 24.164 1.00136.35 C ATOM 1250 CG GLU B 20 60.514 20.799 23.494 1.00136.73 C ATOM 1251 CD GLU B 20 59.907 19.841 24.505 1.00136.96 C ATOM 1252 OE1 GLU B 20 60.654 19.330 25.365 1.00137.05 O ATOM 1253 OE2 GLU B 20 58.682 19.605 24.443 1.00137.00 O ATOM 1254 N TYR B 21 62.145 23.857 25.896 1.00138.79 N ATOM 1255 CA TYR B 21 62.961 24.538 26.896 1.00137.55 C ATOM 1256 C TYR B 21 63.821 25.691 26.377 1.00134.87 C ATOM 1257 O TYR B 21 64.677 25.512 25.507 1.00132.40 O ATOM 1258 CB TYR B 21 63.867 23.525 27.608 1.00140.21 C ATOM 1259 CG TYR B 21 63.127 22.506 28.453 1.00142.70 C ATOM 1260 CD1 TYR B 21 62.322 22.909 29.520 1.00143.17 C ATOM 1261 CD2 TYR B 21 63.237 21.140 28.190 1.00142.73 C ATOM 1262 CE1 TYR B 21 61.648 21.979 30.307 1.00143.12 C ATOM 1263 CE2 TYR B 21 62.567 20.201 28.970 1.00143.39 C ATOM 1264 CZ TYR B 21 61.774 20.629 30.027 1.00143.45 C ATOM 1265 OH TYR B 21 61.115 19.707 30.809 1.00143.47 O ATOM 1266 N ILE B 22 63.582 26.874 26.935 1.00133.97 N ATOM 1267 CA ILE B 22 64.337 28.076 26.592 1.00131.70 C ATOM 1268 C ILE B 22 64.733 28.795 27.881 1.00127.04 C ATOM 1269 O ILE B 22 63.876 29.195 28.678 1.00124.95 O ATOM 1270 CB ILE B 22 63.516 29.039 25.704 1.00133.68 C ATOM 1271 CG1 ILE B 22 62.154 29.313 26.347 1.00135.12 C ATOM 1272 CG2 ILE B 22 63.365 28.456 24.308 1.00133.18 C ATOM 1273 CD1 ILE B 22 61.301 30.298 25.574 1.00136.48 C ATOM 1274 N LYS B 23 66.040 28.933 28.085 1.00121.32 N ATOM 1275 CA LYS B 23 66.581 29.590 29.266 1.00115.15 C ATOM 1276 C LYS B 23 66.336 31.092 29.177 1.00114.57 C ATOM 1277 O LYS B 23 66.712 31.735 28.197 1.00115.41 O ATOM 1278 CB LYS B 23 68.080 29.303 29.372 1.00110.69 C ATOM 1279 CG LYS B 23 68.789 30.008 30.513 1.00105.64 C ATOM 1280 CD LYS B 23 70.261 29.630 30.551 1.00103.74 C ATOM 1281 CE LYS B 23 70.435 28.132 30.768 1.00104.55 C ATOM 1282 NZ LYS B 23 71.865 27.716 30.802 1.00103.76 N ATOM 1283 N LEU B 24 65.702 31.642 30.206 1.00112.64 N ATOM 1284 CA LEU B 24 65.393 33.065 30.254 1.00110.21 C ATOM 1285 C LEU B 24 66.227 33.777 31.309 1.00110.26 C ATOM 1286 O LEU B 24 66.639 33.175 32.301 1.00109.54 O ATOM 1287 CB LEU B 24 63.912 33.268 30.576 1.00109.91 C ATOM 1288 CG LEU B 24 62.864 32.728 29.599 1.00109.51 C ATOM 1289 CD1 LEU B 24 61.481 32.849 30.227 1.00106.85 C ATOM 1290 CD2 LEU B 24 62.937 33.492 28.282 1.00107.70 C ATOM 1291 N LYS B 25 66.473 35.064 31.086 1.00111.16 N ATOM 1292 CA LYS B 25 67.237 35.885 32.022 1.00113.68 C ATOM 1293 C LYS B 25 66.357 36.985 32.616 1.00115.28 C ATOM 1294 O LYS B 25 66.090 37.994 31.960 1.00118.16 O ATOM 1295 CB LYS B 25 68.431 36.548 31.325 1.00112.86 C ATOM 1296 CG LYS B 25 69.663 35.684 31.153 1.00110.70 C ATOM 1297 CD LYS B 25 70.854 36.557 30.782 1.00108.55 C ATOM 1298 CE LYS B 25 72.146 35.769 30.732 1.00107.66 C ATOM 1299 NZ LYS B 25 73.310 36.655 30.457 1.00106.70 N ATOM 1300 N VAL B 26 65.904 36.799 33.851 1.00113.30 N ATOM 1301 CA VAL B 26 65.073 37.806 34.494 1.00110.66 C ATOM 1302 C VAL B 26 65.977 38.760 35.260 1.00110.63 C ATOM 1303 O VAL B 26 66.500 38.424 36.323 1.00110.12 O ATOM 1304 CB VAL B 26 64.063 37.170 35.464 1.00109.24 C ATOM 1305 CG1 VAL B 26 63.158 38.239 36.046 1.00106.08 C ATOM 1306 CG2 VAL B 26 63.243 36.124 34.739 1.00108.86 C ATOM 1307 N ILE B 27 66.171 39.948 34.701 1.00110.16 N ATOM 1308 CA ILE B 27 67.019 40.950 35.320 1.00110.49 C ATOM 1309 C ILE B 27 66.200 41.980 36.076 1.00110.98 C ATOM 1310 O ILE B 27 65.372 42.681 35.494 1.00110.60 O ATOM 1311 CB ILE B 27 67.868 41.675 34.269 1.00111.09 C ATOM 1312 CG1 ILE B 27 68.896 40.708 33.682 1.00111.88 C ATOM 1313 CG2 ILE B 27 68.560 42.869 34.891 1.00113.32 C ATOM 1314 CD1 ILE B 27 69.808 41.335 32.647 1.00112.93 C ATOM 1315 N GLY B 28 66.444 42.068 37.380 1.00112.35 N ATOM 1316 CA GLY B 28 65.727 43.014 38.214 1.00113.66 C ATOM 1317 C GLY B 28 66.267 44.427 38.099 1.00113.71 C ATOM 1318 O GLY B 28 67.014 44.737 37.170 1.00114.16 O ATOM 1319 N GLN B 29 65.896 45.286 39.044 1.00113.16 N ATOM 1320 CA GLN B 29 66.353 46.668 39.017 1.00111.98 C ATOM 1321 C GLN B 29 67.235 46.999 40.211 1.00108.32 C ATOM 1322 O GLN B 29 67.084 48.042 40.841 1.00103.89 O ATOM 1323 CB GLN B 29 65.152 47.614 38.971 1.00114.67 C ATOM 1324 CG GLN B 29 65.419 48.849 38.141 1.00115.93 C ATOM 1325 CD GLN B 29 66.009 48.496 36.789 1.00115.77 C ATOM 1326 OE1 GLN B 29 65.337 47.911 35.936 1.00115.45 O ATOM 1327 NE2 GLN B 29 67.280 48.833 36.592 1.00115.17 N ATOM 1328 N ASP B 30 68.162 46.096 40.505 1.00108.53 N ATOM 1329 CA ASP B 30 69.087 46.260 41.619 1.00110.49 C ATOM 1330 C ASP B 30 70.230 45.255 41.508 1.00110.33 C ATOM 1331 O ASP B 30 70.829 44.855 42.511 1.00107.25 O ATOM 1332 CB ASP B 30 68.344 46.092 42.954 1.00112.62 C ATOM 1333 CG ASP B 30 67.451 44.862 42.985 1.00114.01 C ATOM 1334 OD1 ASP B 30 66.729 44.676 43.990 1.00112.52 O ATOM 1335 OD2 ASP B 30 67.469 44.083 42.010 1.00116.02 O ATOM 1336 N SER B 31 70.524 44.867 40.267 1.00111.75 N ATOM 1337 CA SER B 31 71.584 43.914 39.945 1.00112.50 C ATOM 1338 C SER B 31 71.235 42.472 40.333 1.00111.25 C ATOM 1339 O SER B 31 72.102 41.590 40.360 1.00110.13 O ATOM 1340 CB SER B 31 72.899 44.339 40.607 1.00113.52 C ATOM 1341 OG SER B 31 73.958 43.475 40.233 1.00116.77 O ATOM 1342 N SER B 32 69.958 42.241 40.626 1.00108.59 N ATOM 1343 CA SER B 32 69.474 40.917 40.991 1.00105.70 C ATOM 1344 C SER B 32 69.139 40.142 39.724 1.00107.28 C ATOM 1345 O SER B 32 68.083 40.351 39.129 1.00106.95 O ATOM 1346 CB SER B 32 68.224 41.036 41.861 1.00102.39 C ATOM 1347 OG SER B 32 67.632 39.769 42.083 1.00 99.70 O ATOM 1348 N GLU B 33 70.037 39.253 39.307 1.00109.37 N ATOM 1349 CA GLU B 33 69.809 38.454 38.108 1.00110.31 C ATOM 1350 C GLU B 33 69.442 37.011 38.452 1.00106.90 C ATOM 1351 O GLU B 33 70.020 36.411 39.360 1.00104.00 O ATOM 1352 CB GLU B 33 71.048 38.472 37.205 1.00116.59 C ATOM 1353 CG GLU B 33 70.873 37.673 35.908 1.00125.53 C ATOM 1354 CD GLU B 33 72.079 37.757 34.973 1.00129.71 C ATOM 1355 OE1 GLU B 33 72.411 38.874 34.520 1.00132.45 O ATOM 1356 OE2 GLU B 33 72.693 36.704 34.688 1.00131.04 O ATOM 1357 N ILE B 34 68.475 36.467 37.716 1.00104.73 N ATOM 1358 CA ILE B 34 68.005 35.101 37.921 1.00103.80 C ATOM 1359 C ILE B 34 67.707 34.419 36.588 1.00105.49 C ATOM 1360 O ILE B 34 67.080 35.013 35.711 1.00106.12 O ATOM 1361 CB ILE B 34 66.724 35.080 38.776 1.00101.25 C ATOM 1362 CG1 ILE B 34 67.036 35.596 40.179 1.00100.45 C ATOM 1363 CG2 ILE B 34 66.164 33.671 38.844 1.00100.23 C ATOM 1364 CD1 ILE B 34 65.823 35.742 41.060 1.00 99.24 C ATOM 1365 N HIS B 35 68.155 33.173 36.449 1.00106.50 N ATOM 1366 CA HIS B 35 67.951 32.402 35.225 1.00106.66 C ATOM 1367 C HIS B 35 66.930 31.288 35.392 1.00105.44 C ATOM 1368 O HIS B 35 66.989 30.514 36.347 1.00104.42 O ATOM 1369 CB HIS B 35 69.276 31.806 34.755 1.00109.27 C ATOM 1370 CG HIS B 35 70.228 32.819 34.202 1.00113.01 C ATOM 1371 ND1 HIS B 35 71.496 32.492 33.771 1.00115.57 N ATOM 1372 CD2 HIS B 35 70.092 34.150 33.993 1.00114.15 C ATOM 1373 CE1 HIS B 35 72.101 33.578 33.322 1.00116.16 C ATOM 1374 NE2 HIS B 35 71.271 34.597 33.446 1.00115.62 N ATOM 1375 N PHE B 36 66.000 31.209 34.447 1.00105.58 N ATOM 1376 CA PHE B 36 64.950 30.197 34.476 1.00106.97 C ATOM 1377 C PHE B 36 64.908 29.378 33.188 1.00110.17 C ATOM 1378 O PHE B 36 65.163 29.900 32.101 1.00111.69 O ATOM 1379 CB PHE B 36 63.573 30.857 34.650 1.00104.17 C ATOM 1380 CG PHE B 36 63.389 31.574 35.955 1.00101.87 C ATOM 1381 CD1 PHE B 36 63.349 30.872 37.156 1.00101.69 C ATOM 1382 CD2 PHE B 36 63.231 32.954 35.982 1.00100.11 C ATOM 1383 CE1 PHE B 36 63.152 31.537 38.364 1.00 99.64 C ATOM 1384 CE2 PHE B 36 63.035 33.626 37.183 1.00 99.86 C ATOM 1385 CZ PHE B 36 62.995 32.915 38.377 1.00 99.54 C ATOM 1386 N LYS B 37 64.600 28.089 33.319 1.00111.94 N ATOM 1387 CA LYS B 37 64.443 27.210 32.163 1.00113.55 C ATOM 1388 C LYS B 37 62.943 26.973 32.157 1.00115.25 C ATOM 1389 O LYS B 37 62.390 26.451 33.129 1.00114.21 O ATOM 1390 CB LYS B 37 65.174 25.876 32.352 1.00114.03 C ATOM 1391 CG LYS B 37 66.612 25.851 31.840 1.00114.35 C ATOM 1392 CD LYS B 37 67.212 24.456 32.005 1.00114.05 C ATOM 1393 CE LYS B 37 68.703 24.425 31.691 1.00112.21 C ATOM 1394 NZ LYS B 37 69.299 23.082 31.974 1.00109.34 N ATOM 1395 N VAL B 38 62.275 27.366 31.080 1.00117.18 N ATOM 1396 CA VAL B 38 60.835 27.202 31.040 1.00120.42 C ATOM 1397 C VAL B 38 60.287 26.546 29.788 1.00124.51 C ATOM 1398 O VAL B 38 60.840 26.688 28.695 1.00123.47 O ATOM 1399 CB VAL B 38 60.132 28.553 31.207 1.00118.74 C ATOM 1400 CG1 VAL B 38 58.659 28.335 31.448 1.00119.02 C ATOM 1401 CG2 VAL B 38 60.749 29.322 32.350 1.00119.18 C ATOM 1402 N LYS B 39 59.183 25.825 29.971 1.00129.95 N ATOM 1403 CA LYS B 39 58.498 25.151 28.879 1.00134.80 C ATOM 1404 C LYS B 39 57.634 26.191 28.172 1.00135.00 C ATOM 1405 O LYS B 39 56.808 26.861 28.797 1.00135.09 O ATOM 1406 CB LYS B 39 57.624 24.013 29.415 1.00138.94 C ATOM 1407 CG LYS B 39 58.413 22.857 30.026 1.00142.83 C ATOM 1408 CD LYS B 39 57.489 21.744 30.513 1.00145.43 C ATOM 1409 CE LYS B 39 58.278 20.555 31.050 1.00146.23 C ATOM 1410 NZ LYS B 39 57.396 19.456 31.546 1.00145.42 N ATOM 1411 N MET B 40 57.833 26.319 26.866 1.00133.96 N ATOM 1412 CA MET B 40 57.108 27.292 26.066 1.00132.37 C ATOM 1413 C MET B 40 55.621 26.988 25.921 1.00133.20 C ATOM 1414 O MET B 40 54.970 27.445 24.983 1.00131.50 O ATOM 1415 CB MET B 40 57.783 27.395 24.705 1.00128.82 C ATOM 1416 CG MET B 40 59.276 27.587 24.853 1.00126.43 C ATOM 1417 SD MET B 40 60.154 27.678 23.308 1.00128.56 S ATOM 1418 CE MET B 40 60.588 25.958 23.054 1.00128.03 C ATOM 1419 N THR B 41 55.094 26.219 26.869 1.00135.90 N ATOM 1420 CA THR B 41 53.681 25.848 26.894 1.00138.28 C ATOM 1421 C THR B 41 53.123 26.257 28.253 1.00139.09 C ATOM 1422 O THR B 41 51.924 26.150 28.510 1.00138.98 O ATOM 1423 CB THR B 41 53.486 24.324 26.741 1.00138.35 C ATOM 1424 OG1 THR B 41 54.183 23.866 25.576 1.00140.68 O ATOM 1425 CG2 THR B 41 52.003 23.984 26.605 1.00135.49 C ATOM 1426 N THR B 42 54.015 26.727 29.119 1.00139.33 N ATOM 1427 CA THR B 42 53.641 27.143 30.462 1.00137.29 C ATOM 1428 C THR B 42 53.364 28.641 30.529 1.00134.35 C ATOM 1429 O THR B 42 54.054 29.442 29.893 1.00132.10 O ATOM 1430 CB THR B 42 54.757 26.791 31.475 1.00137.92 C ATOM 1431 OG1 THR B 42 55.946 27.518 31.148 1.00138.06 O ATOM 1432 CG2 THR B 42 55.070 25.299 31.433 1.00137.04 C ATOM 1433 N HIS B 43 52.343 29.004 31.301 1.00132.89 N ATOM 1434 CA HIS B 43 51.956 30.400 31.480 1.00131.83 C ATOM 1435 C HIS B 43 53.081 31.133 32.193 1.00128.30 C ATOM 1436 O HIS B 43 53.564 30.675 33.233 1.00128.83 O ATOM 1437 CB HIS B 43 50.693 30.508 32.340 1.00134.44 C ATOM 1438 CG HIS B 43 49.571 29.630 31.890 1.00136.21 C ATOM 1439 ND1 HIS B 43 48.407 29.486 32.616 1.00136.48 N ATOM 1440 CD2 HIS B 43 49.433 28.841 30.798 1.00136.53 C ATOM 1441 CE1 HIS B 43 47.603 28.646 31.991 1.00137.21 C ATOM 1442 NE2 HIS B 43 48.201 28.240 30.886 1.00137.29 N ATOM 1443 N LEU B 44 53.491 32.273 31.650 1.00121.77 N ATOM 1444 CA LEU B 44 54.556 33.040 32.269 1.00114.70 C ATOM 1445 C LEU B 44 54.264 33.342 33.727 1.00113.03 C ATOM 1446 O LEU B 44 55.186 33.597 34.496 1.00115.59 O ATOM 1447 CB LEU B 44 54.800 34.342 31.508 1.00109.75 C ATOM 1448 CG LEU B 44 55.676 34.194 30.263 1.00107.57 C ATOM 1449 CD1 LEU B 44 55.901 35.551 29.633 1.00108.52 C ATOM 1450 CD2 LEU B 44 57.005 33.576 30.644 1.00105.38 C ATOM 1451 N LYS B 45 52.994 33.306 34.122 1.00109.37 N ATOM 1452 CA LYS B 45 52.673 33.582 35.516 1.00108.03 C ATOM 1453 C LYS B 45 53.512 32.695 36.420 1.00108.20 C ATOM 1454 O LYS B 45 54.013 33.145 37.449 1.00108.14 O ATOM 1455 CB LYS B 45 51.198 33.337 35.823 1.00107.46 C ATOM 1456 CG LYS B 45 50.877 33.610 37.291 1.00107.36 C ATOM 1457 CD LYS B 45 49.423 33.363 37.648 1.00108.78 C ATOM 1458 CE LYS B 45 49.166 33.705 39.114 1.00108.17 C ATOM 1459 NZ LYS B 45 47.749 33.479 39.515 1.00108.76 N ATOM 1460 N LYS B 46 53.663 31.433 36.029 1.00109.39 N ATOM 1461 CA LYS B 46 54.449 30.485 36.811 1.00110.15 C ATOM 1462 C LYS B 46 55.840 31.058 37.053 1.00107.75 C ATOM 1463 O LYS B 46 56.376 30.965 38.161 1.00107.32 O ATOM 1464 CB LYS B 46 54.553 29.145 36.073 1.00112.35 C ATOM 1465 CG LYS B 46 53.208 28.545 35.697 1.00115.86 C ATOM 1466 CD LYS B 46 52.307 28.357 36.918 1.00118.25 C ATOM 1467 CE LYS B 46 50.905 27.900 36.508 1.00120.04 C ATOM 1468 NZ LYS B 46 49.978 27.724 37.664 1.00119.97 N ATOM 1469 N LEU B 47 56.416 31.653 36.011 1.00104.16 N ATOM 1470 CA LEU B 47 57.736 32.264 36.110 1.00100.75 C ATOM 1471 C LEU B 47 57.616 33.416 37.104 1.00102.12 C ATOM 1472 O LEU B 47 58.345 33.480 38.097 1.00103.68 O ATOM 1473 CB LEU B 47 58.184 32.789 34.740 1.00 93.49 C ATOM 1474 CG LEU B 47 59.638 33.257 34.614 1.00 90.12 C ATOM 1475 CD1 LEU B 47 59.980 33.525 33.160 1.00 90.67 C ATOM 1476 CD2 LEU B 47 59.845 34.499 35.440 1.00 88.97 C ATOM 1477 N LYS B 48 56.682 34.318 36.827 1.00101.13 N ATOM 1478 CA LYS B 48 56.432 35.460 37.690 1.00100.45 C ATOM 1479 C LYS B 48 56.417 35.005 39.147 1.00 99.23 C ATOM 1480 O LYS B 48 57.303 35.356 39.923 1.00 99.23 O ATOM 1481 CB LYS B 48 55.088 36.090 37.322 1.00103.00 C ATOM 1482 CG LYS B 48 54.651 37.217 38.231 1.00108.56 C ATOM 1483 CD LYS B 48 53.327 37.807 37.775 1.00112.75 C ATOM 1484 CE LYS B 48 52.873 38.925 38.705 1.00116.89 C ATOM 1485 NZ LYS B 48 51.578 39.520 38.268 1.00119.49 N ATOM 1486 N GLU B 49 55.414 34.207 39.500 1.00 98.70 N ATOM 1487 CA GLU B 49 55.256 33.692 40.861 1.00 99.08 C ATOM 1488 C GLU B 49 56.555 33.208 41.500 1.00 95.59 C ATOM 1489 O GLU B 49 56.907 33.624 42.605 1.00 93.96 O ATOM 1490 CB GLU B 49 54.262 32.534 40.873 1.00103.46 C ATOM 1491 CG GLU B 49 52.928 32.826 40.231 1.00107.76 C ATOM 1492 CD GLU B 49 51.987 31.649 40.342 1.00111.19 C ATOM 1493 OE1 GLU B 49 51.576 31.325 41.478 1.00112.65 O ATOM 1494 OE2 GLU B 49 51.670 31.042 39.297 1.00112.86 O ATOM 1495 N SER B 50 57.245 32.305 40.811 1.00 92.32 N ATOM 1496 CA SER B 50 58.499 31.755 41.311 1.00 91.43 C ATOM 1497 C SER B 50 59.412 32.865 41.806 1.00 91.14 C ATOM 1498 O SER B 50 59.881 32.845 42.947 1.00 90.39 O ATOM 1499 CB SER B 50 59.211 30.972 40.207 1.00 91.53 C ATOM 1500 OG SER B 50 60.458 30.471 40.665 1.00 92.02 O ATOM 1501 N TYR B 51 59.659 33.830 40.926 1.00 89.24 N ATOM 1502 CA TYR B 51 60.513 34.965 41.236 1.00 86.14 C ATOM 1503 C TYR B 51 60.180 35.485 42.627 1.00 84.08 C ATOM 1504 O TYR B 51 60.979 35.402 43.557 1.00 82.62 O ATOM 1505 CB TYR B 51 60.284 36.077 40.212 1.00 86.46 C ATOM 1506 CG TYR B 51 61.383 37.110 40.183 1.00 87.59 C ATOM 1507 CD1 TYR B 51 62.549 36.894 39.450 1.00 88.34 C ATOM 1508 CD2 TYR B 51 61.281 38.281 40.930 1.00 87.81 C ATOM 1509 CE1 TYR B 51 63.590 37.817 39.466 1.00 91.12 C ATOM 1510 CE2 TYR B 51 62.315 39.210 40.954 1.00 90.14 C ATOM 1511 CZ TYR B 51 63.468 38.973 40.223 1.00 92.11 C ATOM 1512 OH TYR B 51 64.505 39.882 40.267 1.00 92.89 O ATOM 1513 N CYS B 52 58.968 36.003 42.748 1.00 83.69 N ATOM 1514 CA CYS B 52 58.460 36.571 43.983 1.00 85.14 C ATOM 1515 C CYS B 52 58.716 35.777 45.259 1.00 83.93 C ATOM 1516 O CYS B 52 59.221 36.328 46.232 1.00 82.84 O ATOM 1517 CB CYS B 52 56.968 36.821 43.823 1.00 88.25 C ATOM 1518 SG CYS B 52 56.607 37.793 42.351 1.00 94.15 S ATOM 1519 N GLN B 53 58.366 34.495 45.266 1.00 85.39 N ATOM 1520 CA GLN B 53 58.571 33.672 46.456 1.00 86.42 C ATOM 1521 C GLN B 53 60.041 33.318 46.678 1.00 84.41 C ATOM 1522 O GLN B 53 60.492 33.193 47.818 1.00 81.66 O ATOM 1523 CB GLN B 53 57.710 32.403 46.378 1.00 90.66 C ATOM 1524 CG GLN B 53 57.948 31.525 45.161 1.00 95.08 C ATOM 1525 CD GLN B 53 58.977 30.446 45.422 1.00 99.56 C ATOM 1526 OE1 GLN B 53 58.859 29.680 46.383 1.00101.22 O ATOM 1527 NE2 GLN B 53 59.993 30.370 44.562 1.00101.75 N ATOM 1528 N ARG B 54 60.787 33.161 45.589 1.00 83.91 N ATOM 1529 CA ARG B 54 62.207 32.852 45.689 1.00 83.87 C ATOM 1530 C ARG B 54 62.926 34.173 45.906 1.00 82.95 C ATOM 1531 O ARG B 54 64.138 34.276 45.732 1.00 82.79 O ATOM 1532 CB ARG B 54 62.701 32.172 44.404 1.00 87.44 C ATOM 1533 CG ARG B 54 64.225 32.099 44.252 1.00 91.81 C ATOM 1534 CD ARG B 54 64.910 31.406 45.423 1.00 97.29 C ATOM 1535 NE ARG B 54 65.072 29.967 45.220 1.00104.04 N ATOM 1536 CZ ARG B 54 65.903 29.424 44.334 1.00105.16 C ATOM 1537 NH1 ARG B 54 66.654 30.200 43.562 1.00104.58 N ATOM 1538 NH2 ARG B 54 65.991 28.104 44.224 1.00104.24 N ATOM 1539 N GLN B 55 62.164 35.187 46.296 1.00 83.44 N ATOM 1540 CA GLN B 55 62.727 36.508 46.536 1.00 83.74 C ATOM 1541 C GLN B 55 62.018 37.209 47.695 1.00 84.06 C ATOM 1542 O GLN B 55 62.422 38.293 48.113 1.00 84.62 O ATOM 1543 CB GLN B 55 62.614 37.355 45.268 1.00 82.88 C ATOM 1544 CG GLN B 55 63.598 38.506 45.212 1.00 86.84 C ATOM 1545 CD GLN B 55 65.044 38.039 45.139 1.00 90.06 C ATOM 1546 OE1 GLN B 55 65.482 37.481 44.128 1.00 88.09 O ATOM 1547 NE2 GLN B 55 65.793 38.262 46.219 1.00 91.86 N ATOM 1548 N GLY B 56 60.963 36.582 48.208 1.00 84.66 N ATOM 1549 CA GLY B 56 60.208 37.148 49.315 1.00 84.15 C ATOM 1550 C GLY B 56 59.544 38.474 48.998 1.00 83.88 C ATOM 1551 O GLY B 56 59.778 39.465 49.681 1.00 84.37 O ATOM 1552 N VAL B 57 58.702 38.489 47.972 1.00 85.02 N ATOM 1553 CA VAL B 57 58.018 39.708 47.552 1.00 87.68 C ATOM 1554 C VAL B 57 56.654 39.380 46.951 1.00 90.25 C ATOM 1555 O VAL B 57 56.568 38.623 45.991 1.00 93.20 O ATOM 1556 CB VAL B 57 58.844 40.450 46.484 1.00 88.15 C ATOM 1557 CG1 VAL B 57 58.078 41.645 45.967 1.00 88.73 C ATOM 1558 CG2 VAL B 57 60.176 40.882 47.067 1.00 89.76 C ATOM 1559 N PRO B 58 55.572 39.964 47.494 1.00 90.88 N ATOM 1560 CA PRO B 58 54.218 39.710 46.987 1.00 92.54 C ATOM 1561 C PRO B 58 54.062 39.806 45.468 1.00 94.72 C ATOM 1562 O PRO B 58 54.606 40.705 44.830 1.00 92.83 O ATOM 1563 CB PRO B 58 53.368 40.737 47.737 1.00 91.15 C ATOM 1564 CG PRO B 58 54.338 41.828 48.052 1.00 89.63 C ATOM 1565 CD PRO B 58 55.553 41.053 48.481 1.00 90.54 C ATOM 1566 N MET B 59 53.307 38.862 44.911 1.00 98.17 N ATOM 1567 CA MET B 59 53.049 38.773 43.473 1.00102.39 C ATOM 1568 C MET B 59 52.829 40.129 42.794 1.00103.95 C ATOM 1569 O MET B 59 53.202 40.326 41.632 1.00101.59 O ATOM 1570 CB MET B 59 51.821 37.887 43.236 1.00104.38 C ATOM 1571 CG MET B 59 51.596 37.454 41.790 1.00106.07 C ATOM 1572 SD MET B 59 52.789 36.211 41.253 1.00109.24 S ATOM 1573 CE MET B 59 52.601 34.988 42.576 1.00109.82 C ATOM 1574 N ASN B 60 52.218 41.056 43.525 1.00105.96 N ATOM 1575 CA ASN B 60 51.922 42.385 43.001 1.00107.32 C ATOM 1576 C ASN B 60 53.119 43.323 43.053 1.00106.77 C ATOM 1577 O ASN B 60 53.529 43.874 42.036 1.00107.19 O ATOM 1578 CB ASN B 60 50.766 43.014 43.785 1.00108.99 C ATOM 1579 CG ASN B 60 51.089 43.195 45.261 1.00109.90 C ATOM 1580 OD1 ASN B 60 51.273 42.221 45.992 1.00110.89 O ATOM 1581 ND2 ASN B 60 51.166 44.448 45.702 1.00108.80 N ATOM 1582 N SER B 61 53.660 43.498 44.253 1.00105.11 N ATOM 1583 CA SER B 61 54.797 44.373 44.503 1.00103.26 C ATOM 1584 C SER B 61 55.647 44.702 43.277 1.00100.04 C ATOM 1585 O SER B 61 56.046 45.848 43.097 1.00101.63 O ATOM 1586 CB SER B 61 55.679 43.767 45.600 1.00105.92 C ATOM 1587 OG SER B 61 56.716 44.653 46.003 1.00108.14 O ATOM 1588 N LEU B 62 55.916 43.717 42.430 1.00 96.52 N ATOM 1589 CA LEU B 62 56.744 43.960 41.253 1.00 96.90 C ATOM 1590 C LEU B 62 55.958 44.167 39.959 1.00 98.84 C ATOM 1591 O LEU B 62 54.772 44.484 39.976 1.00 99.71 O ATOM 1592 CB LEU B 62 57.718 42.799 41.055 1.00 95.39 C ATOM 1593 CG LEU B 62 58.401 42.238 42.301 1.00 93.30 C ATOM 1594 CD1 LEU B 62 59.344 41.130 41.877 1.00 92.00 C ATOM 1595 CD2 LEU B 62 59.151 43.335 43.041 1.00 93.63 C ATOM 1596 N ARG B 63 56.657 43.992 38.840 1.00100.55 N ATOM 1597 CA ARG B 63 56.097 44.122 37.495 1.00102.07 C ATOM 1598 C ARG B 63 57.177 43.628 36.535 1.00101.66 C ATOM 1599 O ARG B 63 58.342 44.005 36.672 1.00102.86 O ATOM 1600 CB ARG B 63 55.756 45.580 37.179 1.00105.13 C ATOM 1601 CG ARG B 63 55.330 45.809 35.736 1.00108.71 C ATOM 1602 CD ARG B 63 55.304 47.291 35.372 1.00113.29 C ATOM 1603 NE ARG B 63 54.134 47.998 35.891 1.00115.43 N ATOM 1604 CZ ARG B 63 53.899 49.293 35.690 1.00115.94 C ATOM 1605 NH1 ARG B 63 54.756 50.022 34.985 1.00114.96 N ATOM 1606 NH2 ARG B 63 52.803 49.858 36.181 1.00116.32 N ATOM 1607 N PHE B 64 56.799 42.787 35.575 1.00 99.51 N ATOM 1608 CA PHE B 64 57.762 42.236 34.623 1.00 97.92 C ATOM 1609 C PHE B 64 57.510 42.743 33.210 1.00100.47 C ATOM 1610 O PHE B 64 56.362 42.890 32.796 1.00102.03 O ATOM 1611 CB PHE B 64 57.700 40.706 34.646 1.00 93.20 C ATOM 1612 CG PHE B 64 57.817 40.115 36.023 1.00 89.08 C ATOM 1613 CD1 PHE B 64 56.820 40.322 36.973 1.00 89.23 C ATOM 1614 CD2 PHE B 64 58.933 39.374 36.382 1.00 87.73 C ATOM 1615 CE1 PHE B 64 56.933 39.803 38.262 1.00 86.69 C ATOM 1616 CE2 PHE B 64 59.057 38.850 37.668 1.00 88.60 C ATOM 1617 CZ PHE B 64 58.053 39.067 38.610 1.00 87.63 C ATOM 1618 N LEU B 65 58.584 42.998 32.468 1.00103.33 N ATOM 1619 CA LEU B 65 58.460 43.507 31.107 1.00107.48 C ATOM 1620 C LEU B 65 59.280 42.734 30.076 1.00110.46 C ATOM 1621 O LEU B 65 60.232 42.027 30.415 1.00110.78 O ATOM 1622 CB LEU B 65 58.889 44.975 31.059 1.00109.58 C ATOM 1623 CG LEU B 65 58.345 45.928 32.124 1.00111.80 C ATOM 1624 CD1 LEU B 65 58.931 47.309 31.884 1.00113.23 C ATOM 1625 CD2 LEU B 65 56.824 45.969 32.077 1.00112.65 C ATOM 1626 N PHE B 66 58.899 42.892 28.812 1.00111.89 N ATOM 1627 CA PHE B 66 59.583 42.256 27.692 1.00111.36 C ATOM 1628 C PHE B 66 59.408 43.144 26.460 1.00112.80 C ATOM 1629 O PHE B 66 58.350 43.750 26.272 1.00112.03 O ATOM 1630 CB PHE B 66 59.007 40.865 27.426 1.00109.17 C ATOM 1631 CG PHE B 66 59.661 40.159 26.277 1.00108.88 C ATOM 1632 CD1 PHE B 66 61.035 39.959 26.261 1.00109.04 C ATOM 1633 CD2 PHE B 66 58.908 39.711 25.197 1.00109.11 C ATOM 1634 CE1 PHE B 66 61.653 39.326 25.183 1.00108.06 C ATOM 1635 CE2 PHE B 66 59.515 39.076 24.114 1.00107.87 C ATOM 1636 CZ PHE B 66 60.891 38.884 24.109 1.00106.51 C ATOM 1637 N GLU B 67 60.441 43.221 25.625 1.00114.44 N ATOM 1638 CA GLU B 67 60.394 44.060 24.431 1.00117.24 C ATOM 1639 C GLU B 67 59.889 45.443 24.828 1.00118.65 C ATOM 1640 O GLU B 67 59.247 46.138 24.041 1.00120.62 O ATOM 1641 CB GLU B 67 59.460 43.461 23.375 1.00120.96 C ATOM 1642 CG GLU B 67 59.990 42.220 22.664 1.00125.12 C ATOM 1643 CD GLU B 67 59.028 41.696 21.599 1.00127.52 C ATOM 1644 OE1 GLU B 67 57.886 41.325 21.951 1.00127.22 O ATOM 1645 OE2 GLU B 67 59.413 41.655 20.408 1.00127.81 O ATOM 1646 N GLY B 68 60.179 45.833 26.064 1.00118.79 N ATOM 1647 CA GLY B 68 59.738 47.125 26.546 1.00119.45 C ATOM 1648 C GLY B 68 58.331 47.068 27.105 1.00120.62 C ATOM 1649 O GLY B 68 58.068 47.607 28.180 1.00120.92 O ATOM 1650 N GLN B 69 57.423 46.408 26.390 1.00120.78 N ATOM 1651 CA GLN B 69 56.039 46.311 26.842 1.00121.40 C ATOM 1652 C GLN B 69 55.805 45.291 27.953 1.00120.80 C ATOM 1653 O GLN B 69 56.487 44.267 28.039 1.00119.77 O ATOM 1654 CB GLN B 69 55.107 46.024 25.658 1.00122.00 C ATOM 1655 CG GLN B 69 54.990 47.196 24.690 1.00122.38 C ATOM 1656 CD GLN B 69 53.802 47.078 23.752 1.00121.48 C ATOM 1657 OE1 GLN B 69 53.685 46.114 22.996 1.00122.01 O ATOM 1658 NE2 GLN B 69 52.916 48.068 23.795 1.00119.53 N ATOM 1659 N ARG B 70 54.825 45.593 28.799 1.00119.70 N ATOM 1660 CA ARG B 70 54.464 44.757 29.936 1.00118.23 C ATOM 1661 C ARG B 70 54.202 43.301 29.571 1.00119.24 C ATOM 1662 O ARG B 70 54.085 42.954 28.396 1.00118.96 O ATOM 1663 CB ARG B 70 53.238 45.350 30.629 1.00115.97 C ATOM 1664 CG ARG B 70 52.930 44.749 31.974 1.00115.74 C ATOM 1665 CD ARG B 70 52.055 45.686 32.776 1.00118.92 C ATOM 1666 NE ARG B 70 51.983 45.287 34.177 1.00123.64 N ATOM 1667 CZ ARG B 70 51.509 46.059 35.150 1.00126.18 C ATOM 1668 NH1 ARG B 70 51.062 47.277 34.871 1.00127.77 N ATOM 1669 NH2 ARG B 70 51.486 45.617 36.402 1.00126.21 N ATOM 1670 N ILE B 71 54.114 42.452 30.590 1.00121.20 N ATOM 1671 CA ILE B 71 53.871 41.028 30.390 1.00122.34 C ATOM 1672 C ILE B 71 52.561 40.561 31.016 1.00123.66 C ATOM 1673 O ILE B 71 52.317 40.760 32.210 1.00122.04 O ATOM 1674 CB ILE B 71 55.024 40.173 30.965 1.00120.83 C ATOM 1675 CG1 ILE B 71 56.271 40.339 30.095 1.00121.17 C ATOM 1676 CG2 ILE B 71 54.609 38.711 31.036 1.00118.50 C ATOM 1677 CD1 ILE B 71 57.466 39.533 30.567 1.00121.87 C ATOM 1678 N ALA B 72 51.730 39.930 30.188 1.00124.69 N ATOM 1679 CA ALA B 72 50.436 39.412 30.617 1.00123.31 C ATOM 1680 C ALA B 72 50.645 38.286 31.612 1.00121.97 C ATOM 1681 O ALA B 72 51.662 37.594 31.578 1.00121.55 O ATOM 1682 CB ALA B 72 49.638 38.906 29.414 1.00121.30 C ATOM 1683 N ASP B 73 49.672 38.104 32.493 1.00120.96 N ATOM 1684 CA ASP B 73 49.744 37.067 33.506 1.00121.43 C ATOM 1685 C ASP B 73 49.523 35.677 32.903 1.00122.56 C ATOM 1686 O ASP B 73 49.938 34.667 33.475 1.00121.24 O ATOM 1687 CB ASP B 73 48.702 37.348 34.584 1.00121.68 C ATOM 1688 CG ASP B 73 49.052 36.714 35.903 1.00122.33 C ATOM 1689 OD1 ASP B 73 50.145 37.015 36.431 1.00120.08 O ATOM 1690 OD2 ASP B 73 48.234 35.917 36.413 1.00124.11 O ATOM 1691 N ASN B 74 48.873 35.636 31.743 1.00125.07 N ATOM 1692 CA ASN B 74 48.591 34.383 31.044 1.00125.90 C ATOM 1693 C ASN B 74 49.528 34.202 29.862 1.00128.02 C ATOM 1694 O ASN B 74 49.465 33.198 29.155 1.00127.04 O ATOM 1695 CB ASN B 74 47.144 34.367 30.553 1.00124.25 C ATOM 1696 CG ASN B 74 46.148 34.241 31.686 1.00124.47 C ATOM 1697 OD1 ASN B 74 44.945 34.419 31.493 1.00124.44 O ATOM 1698 ND2 ASN B 74 46.644 33.922 32.877 1.00124.64 N ATOM 1699 N HIS B 75 50.398 35.186 29.658 1.00132.15 N ATOM 1700 CA HIS B 75 51.369 35.164 28.569 1.00136.28 C ATOM 1701 C HIS B 75 52.201 33.879 28.571 1.00136.45 C ATOM 1702 O HIS B 75 52.161 33.103 29.527 1.00138.15 O ATOM 1703 CB HIS B 75 52.306 36.372 28.686 1.00139.50 C ATOM 1704 CG HIS B 75 52.337 37.236 27.464 1.00142.04 C ATOM 1705 ND1 HIS B 75 52.628 36.743 26.209 1.00142.47 N ATOM 1706 CD2 HIS B 75 52.111 38.562 27.304 1.00142.36 C ATOM 1707 CE1 HIS B 75 52.575 37.728 25.330 1.00142.60 C ATOM 1708 NE2 HIS B 75 52.264 38.841 25.969 1.00142.80 N ATOM 1709 N THR B 76 52.955 33.674 27.495 1.00133.74 N ATOM 1710 CA THR B 76 53.821 32.511 27.328 1.00132.45 C ATOM 1711 C THR B 76 54.504 32.709 25.990 1.00130.73 C ATOM 1712 O THR B 76 53.901 33.265 25.079 1.00129.04 O ATOM 1713 CB THR B 76 53.017 31.189 27.276 1.00134.70 C ATOM 1714 OG1 THR B 76 52.394 30.953 28.544 1.00137.57 O ATOM 1715 CG2 THR B 76 53.930 30.013 26.951 1.00134.69 C ATOM 1716 N PRO B 77 55.772 32.271 25.854 1.00131.67 N ATOM 1717 CA PRO B 77 56.504 32.420 24.590 1.00132.49 C ATOM 1718 C PRO B 77 55.638 32.000 23.407 1.00134.35 C ATOM 1719 O PRO B 77 55.967 32.258 22.247 1.00133.51 O ATOM 1720 CB PRO B 77 57.710 31.512 24.787 1.00130.98 C ATOM 1721 CG PRO B 77 58.002 31.700 26.232 1.00130.10 C ATOM 1722 CD PRO B 77 56.625 31.629 26.871 1.00131.07 C ATOM 1723 N LYS B 78 54.529 31.341 23.728 1.00136.34 N ATOM 1724 CA LYS B 78 53.561 30.890 22.742 1.00137.74 C ATOM 1725 C LYS B 78 53.025 32.142 22.055 1.00138.88 C ATOM 1726 O LYS B 78 52.525 32.090 20.931 1.00139.63 O ATOM 1727 CB LYS B 78 52.422 30.145 23.448 1.00137.27 C ATOM 1728 CG LYS B 78 51.291 29.676 22.542 1.00137.09 C ATOM 1729 CD LYS B 78 50.166 29.050 23.358 1.00136.51 C ATOM 1730 CE LYS B 78 48.977 28.678 22.485 1.00136.59 C ATOM 1731 NZ LYS B 78 47.837 28.153 23.292 1.00136.28 N ATOM 1732 N GLU B 79 53.152 33.269 22.748 1.00139.23 N ATOM 1733 CA GLU B 79 52.685 34.552 22.246 1.00139.27 C ATOM 1734 C GLU B 79 53.836 35.533 22.025 1.00139.93 C ATOM 1735 O GLU B 79 53.784 36.360 21.117 1.00141.81 O ATOM 1736 CB GLU B 79 51.694 35.164 23.237 1.00138.96 C ATOM 1737 CG GLU B 79 50.581 34.229 23.663 1.00140.83 C ATOM 1738 CD GLU B 79 49.729 33.773 22.499 1.00143.23 C ATOM 1739 OE1 GLU B 79 49.187 34.641 21.782 1.00145.11 O ATOM 1740 OE2 GLU B 79 49.598 32.546 22.301 1.00143.96 O ATOM 1741 N LEU B 80 54.872 35.435 22.858 1.00138.87 N ATOM 1742 CA LEU B 80 56.028 36.329 22.773 1.00136.13 C ATOM 1743 C LEU B 80 57.139 35.848 21.856 1.00135.52 C ATOM 1744 O LEU B 80 58.056 36.608 21.538 1.00133.21 O ATOM 1745 CB LEU B 80 56.606 36.569 24.165 1.00134.56 C ATOM 1746 CG LEU B 80 55.730 37.403 25.094 1.00133.54 C ATOM 1747 CD1 LEU B 80 56.348 37.486 26.479 1.00133.42 C ATOM 1748 CD2 LEU B 80 55.567 38.785 24.493 1.00134.44 C ATOM 1749 N GLY B 81 57.061 34.590 21.436 1.00136.64 N ATOM 1750 CA GLY B 81 58.082 34.046 20.560 1.00138.78 C ATOM 1751 C GLY B 81 59.475 34.289 21.108 1.00139.61 C ATOM 1752 O GLY B 81 60.441 34.425 20.359 1.00137.88 O ATOM 1753 N MET B 82 59.575 34.348 22.429 1.00141.93 N ATOM 1754 CA MET B 82 60.855 34.574 23.074 1.00144.62 C ATOM 1755 C MET B 82 61.810 33.427 22.767 1.00145.50 C ATOM 1756 O MET B 82 61.541 32.281 23.125 1.00146.03 O ATOM 1757 CB MET B 82 60.671 34.687 24.589 1.00147.33 C ATOM 1758 CG MET B 82 59.700 35.774 25.022 1.00151.33 C ATOM 1759 SD MET B 82 59.680 36.034 26.814 1.00154.69 S ATOM 1760 CE MET B 82 58.393 34.902 27.321 1.00154.31 C ATOM 1761 N GLU B 83 62.917 33.733 22.095 1.00146.38 N ATOM 1762 CA GLU B 83 63.913 32.716 21.771 1.00147.49 C ATOM 1763 C GLU B 83 64.655 32.368 23.060 1.00149.08 C ATOM 1764 O GLU B 83 64.101 32.489 24.152 1.00148.84 O ATOM 1765 CB GLU B 83 64.892 33.248 20.727 1.00144.99 C ATOM 1766 N GLU B 84 65.901 31.927 22.940 1.00151.53 N ATOM 1767 CA GLU B 84 66.680 31.601 24.127 1.00153.89 C ATOM 1768 C GLU B 84 67.511 32.834 24.441 1.00153.70 C ATOM 1769 O GLU B 84 67.593 33.752 23.622 1.00153.89 O ATOM 1770 CB GLU B 84 67.615 30.412 23.873 1.00157.34 C ATOM 1771 CG GLU B 84 66.974 29.200 23.202 1.00160.65 C ATOM 1772 CD GLU B 84 66.978 29.296 21.681 1.00161.12 C ATOM 1773 OE1 GLU B 84 68.076 29.402 21.093 1.00159.84 O ATOM 1774 OE2 GLU B 84 65.885 29.262 21.075 1.00161.97 O ATOM 1775 N GLU B 85 68.117 32.862 25.623 1.00153.07 N ATOM 1776 CA GLU B 85 68.961 33.985 26.030 1.00152.32 C ATOM 1777 C GLU B 85 68.180 35.283 26.239 1.00148.22 C ATOM 1778 O GLU B 85 68.757 36.310 26.596 1.00147.01 O ATOM 1779 CB GLU B 85 70.062 34.211 24.984 1.00156.35 C ATOM 1780 CG GLU B 85 71.096 35.260 25.363 1.00158.61 C ATOM 1781 CD GLU B 85 71.922 34.851 26.563 1.00159.19 C ATOM 1782 OE1 GLU B 85 72.647 33.839 26.463 1.00158.87 O ATOM 1783 OE2 GLU B 85 71.841 35.538 27.604 1.00159.78 O ATOM 1784 N ASP B 86 66.871 35.238 26.016 1.00144.48 N ATOM 1785 CA ASP B 86 66.034 36.420 26.189 1.00140.49 C ATOM 1786 C ASP B 86 66.277 37.094 27.526 1.00135.09 C ATOM 1787 O ASP B 86 67.018 36.586 28.369 1.00135.34 O ATOM 1788 CB ASP B 86 64.553 36.052 26.083 1.00144.55 C ATOM 1789 CG ASP B 86 63.982 36.351 24.719 1.00148.40 C ATOM 1790 OD1 ASP B 86 64.041 37.526 24.301 1.00150.84 O ATOM 1791 OD2 ASP B 86 63.472 35.417 24.066 1.00150.51 O ATOM 1792 N VAL B 87 65.640 38.244 27.717 1.00127.22 N ATOM 1793 CA VAL B 87 65.780 38.996 28.953 1.00118.79 C ATOM 1794 C VAL B 87 64.443 39.558 29.398 1.00113.49 C ATOM 1795 O VAL B 87 63.593 39.889 28.575 1.00112.63 O ATOM 1796 CB VAL B 87 66.770 40.171 28.782 1.00117.27 C ATOM 1797 CG1 VAL B 87 66.775 41.038 30.031 1.00115.77 C ATOM 1798 CG2 VAL B 87 68.165 39.639 28.503 1.00116.38 C ATOM 1799 N ILE B 88 64.256 39.638 30.710 1.00108.74 N ATOM 1800 CA ILE B 88 63.041 40.196 31.279 1.00106.10 C ATOM 1801 C ILE B 88 63.463 41.201 32.337 1.00105.23 C ATOM 1802 O ILE B 88 64.393 40.953 33.105 1.00102.95 O ATOM 1803 CB ILE B 88 62.141 39.130 31.949 1.00105.13 C ATOM 1804 CG1 ILE B 88 61.577 38.172 30.901 1.00105.16 C ATOM 1805 CG2 ILE B 88 60.979 39.810 32.660 1.00105.09 C ATOM 1806 CD1 ILE B 88 60.570 37.173 31.457 1.00101.73 C ATOM 1807 N GLU B 89 62.781 42.340 32.357 1.00105.16 N ATOM 1808 CA GLU B 89 63.070 43.388 33.323 1.00104.38 C ATOM 1809 C GLU B 89 61.977 43.392 34.379 1.00 99.74 C ATOM 1810 O GLU B 89 60.808 43.173 34.068 1.00 98.62 O ATOM 1811 CB GLU B 89 63.105 44.757 32.636 1.00109.87 C ATOM 1812 CG GLU B 89 64.454 45.459 32.685 1.00116.14 C ATOM 1813 CD GLU B 89 65.424 44.942 31.639 1.00119.54 C ATOM 1814 OE1 GLU B 89 65.122 45.091 30.433 1.00120.65 O ATOM 1815 OE2 GLU B 89 66.483 44.391 32.020 1.00120.27 O ATOM 1816 N VAL B 90 62.361 43.626 35.627 1.00 95.94 N ATOM 1817 CA VAL B 90 61.391 43.683 36.711 1.00 95.75 C ATOM 1818 C VAL B 90 61.534 45.059 37.335 1.00 97.13 C ATOM 1819 O VAL B 90 62.648 45.524 37.578 1.00 98.83 O ATOM 1820 CB VAL B 90 61.658 42.622 37.805 1.00 95.11 C ATOM 1821 CG1 VAL B 90 60.489 42.575 38.783 1.00 91.08 C ATOM 1822 CG2 VAL B 90 61.871 41.264 37.179 1.00 98.09 C ATOM 1823 N TYR B 91 60.410 45.717 37.577 1.00 96.26 N ATOM 1824 CA TYR B 91 60.448 47.033 38.183 1.00 95.88 C ATOM 1825 C TYR B 91 59.572 47.050 39.416 1.00 94.74 C ATOM 1826 O TYR B 91 58.478 46.493 39.414 1.00 92.95 O ATOM 1827 CB TYR B 91 59.961 48.096 37.202 1.00 99.87 C ATOM 1828 CG TYR B 91 60.835 48.265 35.983 1.00104.35 C ATOM 1829 CD1 TYR B 91 60.795 47.345 34.937 1.00105.14 C ATOM 1830 CD2 TYR B 91 61.703 49.352 35.874 1.00107.01 C ATOM 1831 CE1 TYR B 91 61.598 47.502 33.806 1.00107.43 C ATOM 1832 CE2 TYR B 91 62.510 49.520 34.747 1.00109.50 C ATOM 1833 CZ TYR B 91 62.453 48.592 33.716 1.00108.51 C ATOM 1834 OH TYR B 91 63.250 48.751 32.602 1.00107.29 O ATOM 1835 N GLN B 92 60.073 47.676 40.475 1.00 96.07 N ATOM 1836 CA GLN B 92 59.325 47.797 41.717 1.00 95.96 C ATOM 1837 C GLN B 92 58.048 48.539 41.335 1.00 96.08 C ATOM 1838 O GLN B 92 58.098 49.522 40.588 1.00 96.75 O ATOM 1839 CB GLN B 92 60.150 48.595 42.734 1.00 95.34 C ATOM 1840 CG GLN B 92 59.407 49.074 43.978 1.00 96.90 C ATOM 1841 CD GLN B 92 58.866 47.950 44.839 1.00 96.49 C ATOM 1842 OE1 GLN B 92 59.429 46.854 44.884 1.00 96.22 O ATOM 1843 NE2 GLN B 92 57.776 48.227 45.552 1.00 94.42 N ATOM 1844 N GLU B 93 56.904 48.062 41.814 1.00 94.82 N ATOM 1845 CA GLU B 93 55.649 48.714 41.475 1.00 93.56 C ATOM 1846 C GLU B 93 55.452 49.952 42.333 1.00 89.01 C ATOM 1847 O GLU B 93 55.790 49.970 43.520 1.00 87.41 O ATOM 1848 CB GLU B 93 54.466 47.756 41.641 1.00 99.05 C ATOM 1849 CG GLU B 93 53.220 48.220 40.890 1.00106.29 C ATOM 1850 CD GLU B 93 53.461 48.376 39.390 1.00109.61 C ATOM 1851 OE1 GLU B 93 53.432 47.353 38.667 1.00107.95 O ATOM 1852 OE2 GLU B 93 53.692 49.525 38.942 1.00110.99 O ATOM 1853 N GLN B 94 54.894 50.985 41.709 1.00 83.24 N ATOM 1854 CA GLN B 94 54.667 52.262 42.366 1.00 75.74 C ATOM 1855 C GLN B 94 53.483 52.961 41.718 1.00 75.28 C ATOM 1856 O GLN B 94 52.970 52.505 40.696 1.00 77.03 O ATOM 1857 CB GLN B 94 55.903 53.123 42.179 1.00 70.72 C ATOM 1858 CG GLN B 94 56.182 53.379 40.710 1.00 63.12 C ATOM 1859 CD GLN B 94 57.531 53.996 40.470 1.00 59.91 C ATOM 1860 OE1 GLN B 94 58.569 53.362 40.684 1.00 59.21 O ATOM 1861 NE2 GLN B 94 57.533 55.245 40.022 1.00 58.74 N ATOM 1862 N THR B 95 53.071 54.078 42.317 1.00 73.77 N ATOM 1863 CA THR B 95 51.960 54.889 41.824 1.00 72.52 C ATOM 1864 C THR B 95 52.271 56.352 42.127 1.00 71.82 C ATOM 1865 O THR B 95 53.177 56.649 42.908 1.00 71.54 O ATOM 1866 CB THR B 95 50.635 54.529 42.524 1.00 74.12 C ATOM 1867 OG1 THR B 95 50.741 54.817 43.925 1.00 77.88 O ATOM 1868 CG2 THR B 95 50.313 53.052 42.339 1.00 74.59 C ATOM 1869 N GLY B 96 51.521 57.264 41.515 1.00 71.42 N ATOM 1870 CA GLY B 96 51.749 58.679 41.758 1.00 70.51 C ATOM 1871 C GLY B 96 51.419 59.064 43.188 1.00 71.19 C ATOM 1872 O GLY B 96 51.219 58.200 44.043 1.00 73.22 O ATOM 1873 N GLY B 97 51.364 60.363 43.454 1.00 71.62 N ATOM 1874 CA GLY B 97 51.050 60.872 44.790 1.00 72.10 C ATOM 1875 C GLY B 97 50.449 62.271 44.675 1.00 73.30 C ATOM 1876 O GLY B 97 50.396 62.839 43.581 1.00 75.82 O TER 3801 HOH A 165 HETATM 3802 O HOH B 98 62.841 50.516 40.434 1.00 42.65 O HETATM 3803 O HOH B 99 69.098 37.614 44.143 1.00 33.02 O HETATM 3804 O HOH B 100 51.905 47.187 46.194 1.00 60.33 O HETATM 3805 O HOH B 101 68.054 36.896 47.112 1.00 49.30 O CONECT 1875 1874 1876 2676 CONECT 2676 1875 2675 END