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 86 86 ILE A 4 ASP A 19 1 16 HELIX 87 87 LEU A 94 GLU A 98 1 5 HELIX 88 88 THR A 108 GLU A 122 1 15 HELIX 89 89 GLN A 130 LYS A 154 1 25 HELIX 90 90 HIS B 43 ARG B 54 1 12 HELIX 91 91 THR B 76 GLY B 81 1 6 HELIX 92 92 ALA C 432 PHE C 440 1 9 HELIX 93 93 LEU C 446 SER C 454 1 9 HELIX 94 94 LEU C 456 THR C 461 1 6 HELIX 95 95 ASP C 465 SER C 478 1 14 HELIX 96 96 ALA C 484 PHE C 502 1 19 HELIX 97 97 ASN C 508 MET C 520 1 13 HELIX 98 98 LEU C 535 VAL C 546 1 12 HELIX 99 99 LEU C 555 LYS C 565 1 11 HELIX 100 100 SER C 568 VAL C 587 1 20 HELIX 101 101 THR D 2641 LEU D 2651 1 11 HELIX 102 102 ASP D 2676 LEU D 2684 1 9 SHEET 51 51 1 VAL A 25 LYS A 30 0 SHEET 52 52 1 MET A 36 PRO A 46 0 SHEET 53 53 1 LEU A 57 LEU A 63 0 SHEET 54 54 1 LYS A 74 PHE A 77 0 SHEET 55 55 1 ILE B 22 ILE B 27 0 SHEET 56 56 1 GLU B 33 VAL B 38 0 SHEET 57 57 1 PHE B 64 PHE B 66 0 SHEET 58 58 1 GLN B 69 ARG B 70 0 SHEET 59 59 1 VAL B 87 VAL B 90 0 SHEET 60 60 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 3302 VAL C 587 ATOM 3303 N SER D2629 85.071 25.596 -57.432 1.00140.94 N ATOM 3304 CA SER D2629 84.159 26.429 -58.270 1.00141.66 C ATOM 3305 C SER D2629 84.942 27.263 -59.283 1.00143.21 C ATOM 3306 O SER D2629 85.225 26.809 -60.395 1.00143.40 O ATOM 3307 CB SER D2629 83.316 27.352 -57.377 1.00140.69 C ATOM 3308 OG SER D2629 84.128 28.201 -56.582 1.00137.83 O ATOM 3309 N LEU D2630 85.287 28.485 -58.889 1.00143.79 N ATOM 3310 CA LEU D2630 86.040 29.395 -59.748 1.00142.41 C ATOM 3311 C LEU D2630 87.447 29.583 -59.178 1.00138.81 C ATOM 3312 O LEU D2630 87.625 30.239 -58.149 1.00138.86 O ATOM 3313 CB LEU D2630 85.309 30.741 -59.833 1.00144.17 C ATOM 3314 CG LEU D2630 83.858 30.661 -60.331 1.00144.40 C ATOM 3315 CD1 LEU D2630 83.209 32.037 -60.289 1.00143.95 C ATOM 3316 CD2 LEU D2630 83.835 30.100 -61.749 1.00145.04 C ATOM 3317 N ASP D2631 88.444 29.001 -59.843 1.00133.75 N ATOM 3318 CA ASP D2631 89.822 29.097 -59.370 1.00127.91 C ATOM 3319 C ASP D2631 90.539 30.411 -59.667 1.00123.50 C ATOM 3320 O ASP D2631 90.569 30.905 -60.798 1.00122.22 O ATOM 3321 CB ASP D2631 90.664 27.921 -59.891 1.00126.19 C ATOM 3322 CG ASP D2631 90.684 26.741 -58.925 1.00124.03 C ATOM 3323 OD1 ASP D2631 91.100 26.925 -57.761 1.00119.77 O ATOM 3324 OD2 ASP D2631 90.289 25.626 -59.328 1.00125.49 O ATOM 3325 N VAL D2632 91.113 30.957 -58.603 1.00117.76 N ATOM 3326 CA VAL D2632 91.862 32.197 -58.624 1.00111.41 C ATOM 3327 C VAL D2632 92.854 32.018 -57.490 1.00107.81 C ATOM 3328 O VAL D2632 92.481 32.076 -56.318 1.00106.15 O ATOM 3329 CB VAL D2632 90.957 33.391 -58.308 1.00112.06 C ATOM 3330 CG1 VAL D2632 91.774 34.662 -58.249 1.00112.51 C ATOM 3331 CG2 VAL D2632 89.874 33.503 -59.359 1.00115.30 C ATOM 3332 N LEU D2633 94.113 31.781 -57.836 1.00104.39 N ATOM 3333 CA LEU D2633 95.136 31.568 -56.824 1.00102.46 C ATOM 3334 C LEU D2633 96.188 32.674 -56.811 1.00101.16 C ATOM 3335 O LEU D2633 96.726 33.047 -57.858 1.00 99.30 O ATOM 3336 CB LEU D2633 95.800 30.195 -57.049 1.00102.18 C ATOM 3337 CG LEU D2633 96.784 29.616 -56.017 1.00102.04 C ATOM 3338 CD1 LEU D2633 96.718 28.098 -56.051 1.00100.09 C ATOM 3339 CD2 LEU D2633 98.204 30.102 -56.288 1.00100.48 C ATOM 3340 N ILE D2634 96.462 33.204 -55.617 1.00 99.38 N ATOM 3341 CA ILE D2634 97.471 34.247 -55.446 1.00 96.60 C ATOM 3342 C ILE D2634 98.816 33.562 -55.655 1.00 94.81 C ATOM 3343 O ILE D2634 99.201 32.696 -54.870 1.00 95.81 O ATOM 3344 CB ILE D2634 97.451 34.841 -54.022 1.00 94.80 C ATOM 3345 CG1 ILE D2634 96.017 35.164 -53.604 1.00 95.20 C ATOM 3346 CG2 ILE D2634 98.299 36.102 -53.981 1.00 92.37 C ATOM 3347 CD1 ILE D2634 95.894 35.717 -52.199 1.00 93.88 C ATOM 3348 N VAL D2635 99.530 33.944 -56.706 1.00 92.00 N ATOM 3349 CA VAL D2635 100.810 33.322 -56.999 1.00 90.27 C ATOM 3350 C VAL D2635 102.026 34.090 -56.496 1.00 92.54 C ATOM 3351 O VAL D2635 103.057 33.489 -56.201 1.00 94.74 O ATOM 3352 CB VAL D2635 100.956 33.094 -58.501 1.00 87.22 C ATOM 3353 CG1 VAL D2635 102.245 32.360 -58.796 1.00 87.62 C ATOM 3354 CG2 VAL D2635 99.774 32.303 -59.002 1.00 86.94 C ATOM 3355 N TYR D2636 101.912 35.409 -56.392 1.00 92.71 N ATOM 3356 CA TYR D2636 103.030 36.221 -55.923 1.00 91.74 C ATOM 3357 C TYR D2636 102.597 37.509 -55.239 1.00 91.44 C ATOM 3358 O TYR D2636 101.627 38.143 -55.650 1.00 94.91 O ATOM 3359 CB TYR D2636 103.944 36.568 -57.096 1.00 93.05 C ATOM 3360 CG TYR D2636 104.966 37.639 -56.783 1.00 97.23 C ATOM 3361 CD1 TYR D2636 106.001 37.404 -55.875 1.00 98.69 C ATOM 3362 CD2 TYR D2636 104.894 38.895 -57.390 1.00 97.91 C ATOM 3363 CE1 TYR D2636 106.940 38.396 -55.580 1.00 98.92 C ATOM 3364 CE2 TYR D2636 105.825 39.892 -57.102 1.00 97.98 C ATOM 3365 CZ TYR D2636 106.843 39.636 -56.198 1.00 99.03 C ATOM 3366 OH TYR D2636 107.754 40.625 -55.906 1.00100.19 O ATOM 3367 N GLU D2637 103.318 37.891 -54.191 1.00 87.90 N ATOM 3368 CA GLU D2637 103.026 39.130 -53.478 1.00 86.42 C ATOM 3369 C GLU D2637 104.340 39.804 -53.081 1.00 84.85 C ATOM 3370 O GLU D2637 105.160 39.222 -52.372 1.00 85.08 O ATOM 3371 CB GLU D2637 102.164 38.864 -52.236 1.00 87.16 C ATOM 3372 CG GLU D2637 102.772 37.904 -51.223 1.00 91.72 C ATOM 3373 CD GLU D2637 102.197 38.075 -49.821 1.00 92.71 C ATOM 3374 OE1 GLU D2637 100.960 38.221 -49.690 1.00 93.69 O ATOM 3375 OE2 GLU D2637 102.986 38.050 -48.848 1.00 90.44 O ATOM 3376 N LEU D2638 104.537 41.031 -53.553 1.00 82.36 N ATOM 3377 CA LEU D2638 105.753 41.789 -53.267 1.00 78.42 C ATOM 3378 C LEU D2638 106.010 41.902 -51.765 1.00 76.33 C ATOM 3379 O LEU D2638 105.190 42.435 -51.021 1.00 74.22 O ATOM 3380 CB LEU D2638 105.642 43.189 -53.882 1.00 76.30 C ATOM 3381 CG LEU D2638 106.926 43.980 -54.154 1.00 73.34 C ATOM 3382 CD1 LEU D2638 106.563 45.370 -54.663 1.00 71.68 C ATOM 3383 CD2 LEU D2638 107.758 44.079 -52.890 1.00 73.99 C ATOM 3384 N THR D2639 107.158 41.404 -51.327 1.00 75.83 N ATOM 3385 CA THR D2639 107.521 41.456 -49.917 1.00 79.30 C ATOM 3386 C THR D2639 108.824 42.220 -49.712 1.00 79.11 C ATOM 3387 O THR D2639 109.727 42.157 -50.544 1.00 79.86 O ATOM 3388 CB THR D2639 107.692 40.038 -49.329 1.00 81.61 C ATOM 3389 OG1 THR D2639 106.436 39.348 -49.377 1.00 84.13 O ATOM 3390 CG2 THR D2639 108.182 40.109 -47.880 1.00 79.64 C ATOM 3391 N PRO D2640 108.931 42.957 -48.598 1.00 78.30 N ATOM 3392 CA PRO D2640 110.134 43.731 -48.295 1.00 77.86 C ATOM 3393 C PRO D2640 111.085 43.028 -47.320 1.00 78.72 C ATOM 3394 O PRO D2640 110.812 41.931 -46.834 1.00 79.95 O ATOM 3395 CB PRO D2640 109.560 44.999 -47.698 1.00 77.18 C ATOM 3396 CG PRO D2640 108.459 44.447 -46.852 1.00 76.74 C ATOM 3397 CD PRO D2640 107.803 43.413 -47.764 1.00 77.92 C ATOM 3398 N THR D2641 112.202 43.694 -47.048 1.00 78.10 N ATOM 3399 CA THR D2641 113.236 43.222 -46.134 1.00 74.79 C ATOM 3400 C THR D2641 112.688 43.231 -44.735 1.00 72.19 C ATOM 3401 O THR D2641 111.713 43.914 -44.457 1.00 72.20 O ATOM 3402 CB THR D2641 114.442 44.176 -46.148 1.00 77.54 C ATOM 3403 OG1 THR D2641 115.153 44.019 -47.380 1.00 85.04 O ATOM 3404 CG2 THR D2641 115.366 43.929 -44.961 1.00 73.90 C ATOM 3405 N ALA D2642 113.322 42.483 -43.847 1.00 74.93 N ATOM 3406 CA ALA D2642 112.895 42.463 -42.458 1.00 78.87 C ATOM 3407 C ALA D2642 113.028 43.884 -41.907 1.00 79.82 C ATOM 3408 O ALA D2642 112.116 44.398 -41.257 1.00 76.63 O ATOM 3409 CB ALA D2642 113.764 41.500 -41.651 1.00 79.59 C ATOM 3410 N GLU D2643 114.164 44.518 -42.186 1.00 83.51 N ATOM 3411 CA GLU D2643 114.411 45.874 -41.715 1.00 87.57 C ATOM 3412 C GLU D2643 113.495 46.908 -42.391 1.00 88.00 C ATOM 3413 O GLU D2643 113.099 47.894 -41.762 1.00 88.67 O ATOM 3414 CB GLU D2643 115.882 46.246 -41.932 1.00 91.99 C ATOM 3415 CG GLU D2643 116.263 47.615 -41.357 1.00 98.80 C ATOM 3416 CD GLU D2643 117.758 47.918 -41.437 1.00102.01 C ATOM 3417 OE1 GLU D2643 118.334 47.809 -42.543 1.00104.77 O ATOM 3418 OE2 GLU D2643 118.355 48.277 -40.396 1.00100.80 O ATOM 3419 N GLN D2644 113.155 46.683 -43.662 1.00 85.10 N ATOM 3420 CA GLN D2644 112.278 47.604 -44.393 1.00 81.31 C ATOM 3421 C GLN D2644 110.872 47.639 -43.795 1.00 78.64 C ATOM 3422 O GLN D2644 110.381 48.693 -43.383 1.00 77.29 O ATOM 3423 CB GLN D2644 112.183 47.195 -45.862 1.00 82.31 C ATOM 3424 CG GLN D2644 113.509 47.200 -46.587 1.00 86.95 C ATOM 3425 CD GLN D2644 113.377 46.848 -48.060 1.00 90.19 C ATOM 3426 OE1 GLN D2644 112.892 45.772 -48.421 1.00 88.99 O ATOM 3427 NE2 GLN D2644 113.816 47.758 -48.920 1.00 94.16 N ATOM 3428 N LYS D2645 110.226 46.476 -43.765 1.00 75.52 N ATOM 3429 CA LYS D2645 108.885 46.345 -43.214 1.00 71.77 C ATOM 3430 C LYS D2645 108.854 46.906 -41.802 1.00 71.17 C ATOM 3431 O LYS D2645 107.922 47.609 -41.426 1.00 72.08 O ATOM 3432 CB LYS D2645 108.478 44.874 -43.196 1.00 70.45 C ATOM 3433 CG LYS D2645 107.159 44.573 -42.496 1.00 72.06 C ATOM 3434 CD LYS D2645 106.845 43.070 -42.550 1.00 73.17 C ATOM 3435 CE LYS D2645 105.552 42.724 -41.819 1.00 74.56 C ATOM 3436 NZ LYS D2645 105.259 41.264 -41.850 1.00 71.93 N ATOM 3437 N ALA D2646 109.885 46.597 -41.025 1.00 70.43 N ATOM 3438 CA ALA D2646 109.976 47.072 -39.650 1.00 69.87 C ATOM 3439 C ALA D2646 110.093 48.597 -39.567 1.00 67.31 C ATOM 3440 O ALA D2646 109.622 49.210 -38.606 1.00 69.36 O ATOM 3441 CB ALA D2646 111.162 46.411 -38.952 1.00 71.62 C ATOM 3442 N LEU D2647 110.732 49.208 -40.559 1.00 61.29 N ATOM 3443 CA LEU D2647 110.867 50.661 -40.570 1.00 59.81 C ATOM 3444 C LEU D2647 109.492 51.266 -40.802 1.00 59.55 C ATOM 3445 O LEU D2647 109.035 52.125 -40.041 1.00 56.83 O ATOM 3446 CB LEU D2647 111.799 51.108 -41.697 1.00 60.00 C ATOM 3447 CG LEU D2647 111.743 52.595 -42.086 1.00 54.22 C ATOM 3448 CD1 LEU D2647 112.198 53.467 -40.925 1.00 46.34 C ATOM 3449 CD2 LEU D2647 112.621 52.825 -43.301 1.00 51.17 C ATOM 3450 N ALA D2648 108.852 50.805 -41.875 1.00 58.69 N ATOM 3451 CA ALA D2648 107.521 51.256 -42.263 1.00 60.98 C ATOM 3452 C ALA D2648 106.526 51.055 -41.120 1.00 62.47 C ATOM 3453 O ALA D2648 105.606 51.853 -40.920 1.00 60.09 O ATOM 3454 CB ALA D2648 107.065 50.487 -43.493 1.00 60.70 C ATOM 3455 N THR D2649 106.715 49.966 -40.385 1.00 64.66 N ATOM 3456 CA THR D2649 105.867 49.643 -39.250 1.00 65.82 C ATOM 3457 C THR D2649 106.006 50.736 -38.196 1.00 67.77 C ATOM 3458 O THR D2649 105.057 51.048 -37.475 1.00 69.51 O ATOM 3459 CB THR D2649 106.286 48.313 -38.627 1.00 66.85 C ATOM 3460 OG1 THR D2649 106.078 47.258 -39.575 1.00 69.30 O ATOM 3461 CG2 THR D2649 105.484 48.045 -37.365 1.00 69.28 C ATOM 3462 N LYS D2650 107.201 51.309 -38.106 1.00 68.03 N ATOM 3463 CA LYS D2650 107.463 52.369 -37.148 1.00 65.06 C ATOM 3464 C LYS D2650 106.814 53.655 -37.646 1.00 65.35 C ATOM 3465 O LYS D2650 106.285 54.444 -36.861 1.00 64.78 O ATOM 3466 CB LYS D2650 108.971 52.569 -36.991 1.00 61.22 C ATOM 3467 CG LYS D2650 109.345 53.606 -35.945 1.00 60.04 C ATOM 3468 N LEU D2651 106.836 53.841 -38.962 1.00 64.72 N ATOM 3469 CA LEU D2651 106.277 55.035 -39.585 1.00 63.51 C ATOM 3470 C LEU D2651 104.821 54.928 -40.018 1.00 61.56 C ATOM 3471 O LEU D2651 104.294 55.825 -40.678 1.00 60.77 O ATOM 3472 CB LEU D2651 107.134 55.424 -40.784 1.00 62.94 C ATOM 3473 CG LEU D2651 108.619 55.517 -40.449 1.00 60.32 C ATOM 3474 CD1 LEU D2651 109.336 56.149 -41.620 1.00 62.38 C ATOM 3475 CD2 LEU D2651 108.830 56.345 -39.186 1.00 56.70 C ATOM 3476 N LYS D2652 104.175 53.830 -39.650 1.00 59.31 N ATOM 3477 CA LYS D2652 102.773 53.623 -39.982 1.00 57.12 C ATOM 3478 C LYS D2652 102.536 53.727 -41.479 1.00 56.89 C ATOM 3479 O LYS D2652 101.470 54.166 -41.910 1.00 58.37 O ATOM 3480 CB LYS D2652 101.916 54.665 -39.262 1.00 55.63 C ATOM 3481 CG LYS D2652 102.555 55.204 -38.003 1.00 54.82 C ATOM 3482 CD LYS D2652 102.689 54.141 -36.941 1.00 58.17 C ATOM 3483 CE LYS D2652 101.372 53.955 -36.225 1.00 63.23 C ATOM 3484 NZ LYS D2652 100.942 55.245 -35.603 1.00 68.37 N ATOM 3485 N LEU D2653 103.533 53.331 -42.265 1.00 56.44 N ATOM 3486 CA LEU D2653 103.441 53.368 -43.727 1.00 55.99 C ATOM 3487 C LEU D2653 103.129 51.979 -44.274 1.00 56.98 C ATOM 3488 O LEU D2653 103.327 50.972 -43.591 1.00 56.41 O ATOM 3489 CB LEU D2653 104.765 53.838 -44.326 1.00 55.63 C ATOM 3490 CG LEU D2653 105.240 55.253 -44.020 1.00 56.26 C ATOM 3491 CD1 LEU D2653 106.732 55.382 -44.302 1.00 54.16 C ATOM 3492 CD2 LEU D2653 104.443 56.221 -44.864 1.00 58.73 C ATOM 3493 N PRO D2654 102.642 51.904 -45.522 1.00 58.72 N ATOM 3494 CA PRO D2654 102.319 50.607 -46.129 1.00 62.70 C ATOM 3495 C PRO D2654 103.581 49.750 -46.276 1.00 66.46 C ATOM 3496 O PRO D2654 104.527 50.140 -46.956 1.00 69.57 O ATOM 3497 CB PRO D2654 101.717 50.999 -47.474 1.00 61.45 C ATOM 3498 CG PRO D2654 102.441 52.262 -47.804 1.00 60.57 C ATOM 3499 CD PRO D2654 102.443 53.000 -46.483 1.00 57.68 C ATOM 3500 N PRO D2655 103.607 48.570 -45.634 1.00 67.71 N ATOM 3501 CA PRO D2655 104.733 47.635 -45.662 1.00 68.73 C ATOM 3502 C PRO D2655 105.561 47.593 -46.940 1.00 70.55 C ATOM 3503 O PRO D2655 106.772 47.404 -46.894 1.00 71.00 O ATOM 3504 CB PRO D2655 104.065 46.315 -45.340 1.00 67.99 C ATOM 3505 CG PRO D2655 103.108 46.736 -44.277 1.00 66.95 C ATOM 3506 CD PRO D2655 102.485 47.986 -44.880 1.00 68.01 C ATOM 3507 N THR D2656 104.918 47.769 -48.082 1.00 73.06 N ATOM 3508 CA THR D2656 105.643 47.757 -49.343 1.00 76.90 C ATOM 3509 C THR D2656 106.001 49.182 -49.736 1.00 77.24 C ATOM 3510 O THR D2656 105.717 49.595 -50.857 1.00 80.65 O ATOM 3511 CB THR D2656 104.778 47.170 -50.464 1.00 81.61 C ATOM 3512 OG1 THR D2656 103.535 47.883 -50.528 1.00 82.91 O ATOM 3513 CG2 THR D2656 104.500 45.701 -50.209 1.00 87.92 C ATOM 3514 N PHE D2657 106.629 49.938 -48.841 1.00 74.73 N ATOM 3515 CA PHE D2657 106.943 51.327 -49.169 1.00 73.93 C ATOM 3516 C PHE D2657 108.338 51.563 -49.745 1.00 76.82 C ATOM 3517 O PHE D2657 108.484 52.132 -50.834 1.00 74.06 O ATOM 3518 CB PHE D2657 106.717 52.222 -47.939 1.00 66.80 C ATOM 3519 CG PHE D2657 106.665 53.694 -48.259 1.00 60.23 C ATOM 3520 CD1 PHE D2657 105.859 54.167 -49.286 1.00 56.55 C ATOM 3521 CD2 PHE D2657 107.421 54.607 -47.537 1.00 55.94 C ATOM 3522 CE1 PHE D2657 105.813 55.522 -49.590 1.00 52.81 C ATOM 3523 CE2 PHE D2657 107.375 55.964 -47.839 1.00 52.43 C ATOM 3524 CZ PHE D2657 106.571 56.419 -48.867 1.00 48.91 C ATOM 3525 N PHE D2658 109.361 51.122 -49.022 1.00 79.36 N ATOM 3526 CA PHE D2658 110.730 51.311 -49.474 1.00 80.39 C ATOM 3527 C PHE D2658 111.136 50.285 -50.519 1.00 82.82 C ATOM 3528 O PHE D2658 112.319 49.997 -50.697 1.00 81.59 O ATOM 3529 CB PHE D2658 111.673 51.254 -48.283 1.00 78.78 C ATOM 3530 CG PHE D2658 111.196 52.052 -47.118 1.00 78.54 C ATOM 3531 CD1 PHE D2658 110.482 51.446 -46.095 1.00 80.31 C ATOM 3532 CD2 PHE D2658 111.417 53.419 -47.063 1.00 78.70 C ATOM 3533 CE1 PHE D2658 109.994 52.193 -45.033 1.00 82.42 C ATOM 3534 CE2 PHE D2658 110.933 54.175 -46.007 1.00 80.52 C ATOM 3535 CZ PHE D2658 110.219 53.563 -44.990 1.00 82.26 C ATOM 3536 N CYS D2659 110.145 49.738 -51.211 1.00 86.92 N ATOM 3537 CA CYS D2659 110.401 48.758 -52.251 1.00 91.80 C ATOM 3538 C CYS D2659 110.814 49.522 -53.498 1.00 95.04 C ATOM 3539 O CYS D2659 111.381 48.952 -54.430 1.00 95.41 O ATOM 3540 CB CYS D2659 109.142 47.937 -52.526 1.00 94.65 C ATOM 3541 SG CYS D2659 108.519 47.051 -51.076 1.00103.42 S ATOM 3542 N TYR D2660 110.524 50.822 -53.501 1.00 97.96 N ATOM 3543 CA TYR D2660 110.871 51.691 -54.619 1.00 99.45 C ATOM 3544 C TYR D2660 112.387 51.645 -54.809 1.00105.36 C ATOM 3545 O TYR D2660 112.881 51.647 -55.941 1.00106.33 O ATOM 3546 CB TYR D2660 110.425 53.129 -54.328 1.00 92.67 C ATOM 3547 CG TYR D2660 111.283 53.848 -53.304 1.00 88.84 C ATOM 3548 CD1 TYR D2660 112.480 54.462 -53.672 1.00 84.88 C ATOM 3549 CD2 TYR D2660 110.915 53.884 -51.958 1.00 89.48 C ATOM 3550 CE1 TYR D2660 113.291 55.090 -52.731 1.00 83.08 C ATOM 3551 CE2 TYR D2660 111.724 54.513 -51.004 1.00 86.95 C ATOM 3552 CZ TYR D2660 112.910 55.110 -51.400 1.00 84.80 C ATOM 3553 OH TYR D2660 113.721 55.712 -50.465 1.00 83.35 O ATOM 3554 N LYS D2661 113.109 51.599 -53.687 1.00110.66 N ATOM 3555 CA LYS D2661 114.572 51.553 -53.677 1.00114.67 C ATOM 3556 C LYS D2661 115.068 50.112 -53.607 1.00118.71 C ATOM 3557 O LYS D2661 116.269 49.855 -53.682 1.00121.56 O ATOM 3558 CB LYS D2661 115.132 52.344 -52.485 1.00112.65 C ATOM 3559 CG LYS D2661 114.781 51.771 -51.110 1.00110.95 C ATOM 3560 CD LYS D2661 115.441 52.569 -49.975 1.00109.08 C ATOM 3561 CE LYS D2661 115.142 51.962 -48.602 1.00106.34 C ATOM 3562 NZ LYS D2661 115.877 52.628 -47.487 1.00101.43 N ATOM 3563 N ASN D2662 114.137 49.177 -53.458 1.00121.06 N ATOM 3564 CA ASN D2662 114.478 47.763 -53.393 1.00123.82 C ATOM 3565 C ASN D2662 114.614 47.252 -54.831 1.00126.16 C ATOM 3566 O ASN D2662 115.145 46.170 -55.074 1.00124.81 O ATOM 3567 CB ASN D2662 113.371 46.999 -52.659 1.00123.87 C ATOM 3568 CG ASN D2662 113.862 45.703 -52.038 1.00122.94 C ATOM 3569 OD1 ASN D2662 114.716 45.710 -51.151 1.00120.69 O ATOM 3570 ND2 ASN D2662 113.318 44.582 -52.500 1.00123.61 N ATOM 3571 N ARG D2663 114.132 48.055 -55.778 1.00130.74 N ATOM 3572 CA ARG D2663 114.177 47.723 -57.203 1.00134.00 C ATOM 3573 C ARG D2663 115.614 47.632 -57.729 1.00136.26 C ATOM 3574 O ARG D2663 116.562 48.033 -57.046 1.00136.05 O ATOM 3575 CB ARG D2663 113.401 48.775 -58.012 1.00132.67 C ATOM 3576 CG ARG D2663 111.923 48.861 -57.677 1.00130.83 C ATOM 3577 N PRO D2664 115.790 47.099 -58.954 1.00137.51 N ATOM 3578 CA PRO D2664 117.116 46.958 -59.565 1.00137.40 C ATOM 3579 C PRO D2664 117.699 48.244 -60.165 1.00137.84 C ATOM 3580 O PRO D2664 118.877 48.536 -59.970 1.00138.00 O ATOM 3581 CB PRO D2664 116.888 45.879 -60.621 1.00135.85 C ATOM 3582 CG PRO D2664 115.502 46.170 -61.076 1.00136.01 C ATOM 3583 CD PRO D2664 114.771 46.407 -59.768 1.00136.95 C ATOM 3584 N ASP D2665 116.878 49.009 -60.882 1.00138.21 N ATOM 3585 CA ASP D2665 117.334 50.246 -61.520 1.00137.89 C ATOM 3586 C ASP D2665 117.880 51.305 -60.558 1.00139.25 C ATOM 3587 O ASP D2665 118.502 50.981 -59.544 1.00140.01 O ATOM 3588 CB ASP D2665 116.208 50.854 -62.370 1.00136.53 C ATOM 3589 CG ASP D2665 115.001 51.253 -61.546 1.00135.73 C ATOM 3590 N TYR D2666 117.640 52.571 -60.891 1.00140.29 N ATOM 3591 CA TYR D2666 118.113 53.712 -60.103 1.00141.22 C ATOM 3592 C TYR D2666 117.917 53.661 -58.581 1.00140.77 C ATOM 3593 O TYR D2666 116.834 53.961 -58.070 1.00140.83 O ATOM 3594 CB TYR D2666 117.493 55.008 -60.648 1.00141.57 C ATOM 3595 CG TYR D2666 115.980 55.016 -60.671 1.00140.56 C ATOM 3596 N VAL D2667 118.980 53.295 -57.865 1.00138.78 N ATOM 3597 CA VAL D2667 118.954 53.231 -56.406 1.00136.80 C ATOM 3598 C VAL D2667 120.369 53.181 -55.842 1.00136.31 C ATOM 3599 O VAL D2667 121.270 52.609 -56.453 1.00134.02 O ATOM 3600 CB VAL D2667 118.178 52.000 -55.891 1.00134.87 C ATOM 3601 CG1 VAL D2667 118.860 50.721 -56.347 1.00133.20 C ATOM 3602 CG2 VAL D2667 118.082 52.052 -54.372 1.00131.26 C ATOM 3603 N SER D2668 120.554 53.790 -54.674 1.00137.22 N ATOM 3604 CA SER D2668 121.855 53.826 -54.012 1.00138.34 C ATOM 3605 C SER D2668 121.690 54.207 -52.543 1.00140.25 C ATOM 3606 O SER D2668 120.946 53.560 -51.808 1.00141.70 O ATOM 3607 CB SER D2668 122.772 54.834 -54.709 1.00137.09 C ATOM 3608 OG SER D2668 122.226 56.140 -54.654 1.00135.94 O ATOM 3609 N GLU D2669 122.389 55.255 -52.117 1.00141.39 N ATOM 3610 CA GLU D2669 122.309 55.726 -50.738 1.00143.09 C ATOM 3611 C GLU D2669 123.037 57.058 -50.561 1.00145.03 C ATOM 3612 O GLU D2669 123.850 57.220 -49.648 1.00145.31 O ATOM 3613 CB GLU D2669 122.885 54.673 -49.779 1.00142.09 C ATOM 3614 CG GLU D2669 124.314 54.254 -50.079 1.00141.30 C ATOM 3615 N GLU D2670 122.735 58.012 -51.440 1.00147.07 N ATOM 3616 CA GLU D2670 123.358 59.333 -51.391 1.00149.28 C ATOM 3617 C GLU D2670 122.725 60.332 -52.371 1.00150.11 C ATOM 3618 O GLU D2670 122.629 60.062 -53.569 1.00151.35 O ATOM 3619 CB GLU D2670 124.863 59.209 -51.671 1.00149.28 C ATOM 3620 CG GLU D2670 125.209 58.497 -52.973 1.00148.28 C ATOM 3621 N GLU D2671 122.299 61.482 -51.843 1.00149.53 N ATOM 3622 CA GLU D2671 121.678 62.557 -52.628 1.00148.23 C ATOM 3623 C GLU D2671 121.214 63.707 -51.729 1.00147.84 C ATOM 3624 O GLU D2671 120.641 63.468 -50.664 1.00148.56 O ATOM 3625 CB GLU D2671 120.475 62.031 -53.421 1.00146.56 C ATOM 3626 CG GLU D2671 120.794 61.658 -54.855 1.00145.18 C ATOM 3627 CD GLU D2671 121.560 62.752 -55.570 1.00144.53 C ATOM 3628 OE1 GLU D2671 121.057 63.892 -55.628 1.00144.10 O ATOM 3629 OE2 GLU D2671 122.668 62.474 -56.070 1.00144.82 O ATOM 3630 N GLU D2672 121.456 64.948 -52.154 1.00145.32 N ATOM 3631 CA GLU D2672 121.039 66.107 -51.364 1.00142.32 C ATOM 3632 C GLU D2672 119.862 66.866 -51.972 1.00140.64 C ATOM 3633 O GLU D2672 119.957 67.418 -53.070 1.00139.72 O ATOM 3634 CB GLU D2672 122.205 67.073 -51.146 1.00141.71 C ATOM 3635 CG GLU D2672 121.826 68.247 -50.256 1.00142.10 C ATOM 3636 CD GLU D2672 123.021 69.043 -49.781 1.00143.25 C ATOM 3637 OE1 GLU D2672 123.745 69.603 -50.631 1.00144.25 O ATOM 3638 OE2 GLU D2672 123.233 69.107 -48.552 1.00143.76 O ATOM 3639 N ASP D2673 118.760 66.893 -51.226 1.00138.82 N ATOM 3640 CA ASP D2673 117.515 67.547 -51.626 1.00135.05 C ATOM 3641 C ASP D2673 117.561 69.053 -51.415 1.00133.22 C ATOM 3642 O ASP D2673 117.909 69.521 -50.331 1.00131.86 O ATOM 3643 CB ASP D2673 116.356 66.962 -50.810 1.00133.17 C ATOM 3644 CG ASP D2673 115.008 67.529 -51.206 1.00131.52 C ATOM 3645 OD1 ASP D2673 114.853 68.766 -51.235 1.00131.26 O ATOM 3646 OD2 ASP D2673 114.092 66.731 -51.479 1.00131.34 O ATOM 3647 N ASP D2674 117.202 69.811 -52.447 1.00131.96 N ATOM 3648 CA ASP D2674 117.190 71.261 -52.322 1.00131.37 C ATOM 3649 C ASP D2674 116.369 72.011 -53.362 1.00130.31 C ATOM 3650 O ASP D2674 115.833 73.078 -53.061 1.00130.80 O ATOM 3651 CB ASP D2674 118.609 71.814 -52.319 1.00132.58 C ATOM 3652 CG ASP D2674 118.632 73.319 -52.185 1.00134.41 C ATOM 3653 OD1 ASP D2674 117.873 73.849 -51.341 1.00132.32 O ATOM 3654 OD2 ASP D2674 119.405 73.967 -52.919 1.00136.91 O ATOM 3655 N GLU D2675 116.278 71.467 -54.574 1.00127.76 N ATOM 3656 CA GLU D2675 115.505 72.092 -55.653 1.00125.35 C ATOM 3657 C GLU D2675 114.279 72.841 -55.123 1.00124.38 C ATOM 3658 O GLU D2675 113.596 72.367 -54.216 1.00124.55 O ATOM 3659 CB GLU D2675 115.047 71.028 -56.656 1.00124.48 C ATOM 3660 CG GLU D2675 114.532 69.747 -55.999 1.00125.39 C ATOM 3661 CD GLU D2675 113.696 68.889 -56.935 1.00124.97 C ATOM 3662 OE1 GLU D2675 113.948 68.924 -58.159 1.00124.19 O ATOM 3663 OE2 GLU D2675 112.796 68.170 -56.444 1.00123.11 O ATOM 3664 N ASP D2676 114.006 74.015 -55.685 1.00122.79 N ATOM 3665 CA ASP D2676 112.856 74.814 -55.263 1.00120.45 C ATOM 3666 C ASP D2676 111.604 74.392 -56.016 1.00115.69 C ATOM 3667 O ASP D2676 111.654 74.137 -57.219 1.00115.72 O ATOM 3668 CB ASP D2676 113.112 76.303 -55.512 1.00125.43 C ATOM 3669 CG ASP D2676 114.048 76.917 -54.488 1.00129.83 C ATOM 3670 OD1 ASP D2676 113.700 76.924 -53.288 1.00130.28 O ATOM 3671 OD2 ASP D2676 115.132 77.397 -54.885 1.00133.56 O ATOM 3672 N PHE D2677 110.482 74.322 -55.308 1.00109.34 N ATOM 3673 CA PHE D2677 109.227 73.930 -55.933 1.00104.37 C ATOM 3674 C PHE D2677 109.132 74.514 -57.343 1.00102.99 C ATOM 3675 O PHE D2677 109.155 73.779 -58.330 1.00100.13 O ATOM 3676 CB PHE D2677 108.035 74.400 -55.083 1.00 99.51 C ATOM 3677 CG PHE D2677 106.724 74.411 -55.829 1.00 93.08 C ATOM 3678 CD1 PHE D2677 106.167 73.233 -56.304 1.00 90.26 C ATOM 3679 CD2 PHE D2677 106.077 75.608 -56.103 1.00 88.71 C ATOM 3680 CE1 PHE D2677 104.990 73.251 -57.044 1.00 86.53 C ATOM 3681 CE2 PHE D2677 104.908 75.629 -56.838 1.00 85.06 C ATOM 3682 CZ PHE D2677 104.362 74.451 -57.312 1.00 84.91 C ATOM 3683 N GLU D2678 109.051 75.839 -57.421 1.00103.96 N ATOM 3684 CA GLU D2678 108.936 76.549 -58.689 1.00104.41 C ATOM 3685 C GLU D2678 109.869 76.005 -59.756 1.00102.01 C ATOM 3686 O GLU D2678 109.476 75.809 -60.908 1.00101.10 O ATOM 3687 CB GLU D2678 109.211 78.040 -58.483 1.00108.95 C ATOM 3688 CG GLU D2678 109.121 78.849 -59.765 1.00115.94 C ATOM 3689 CD GLU D2678 107.871 78.524 -60.568 1.00119.78 C ATOM 3690 OE1 GLU D2678 106.751 78.759 -60.056 1.00120.27 O ATOM 3691 OE2 GLU D2678 108.014 78.028 -61.708 1.00122.31 O ATOM 3692 N THR D2679 111.115 75.776 -59.369 1.00100.09 N ATOM 3693 CA THR D2679 112.105 75.242 -60.291 1.00 98.36 C ATOM 3694 C THR D2679 111.537 73.962 -60.908 1.00 95.70 C ATOM 3695 O THR D2679 111.328 73.874 -62.123 1.00 90.89 O ATOM 3696 CB THR D2679 113.421 74.913 -59.541 1.00 98.93 C ATOM 3697 OG1 THR D2679 113.907 76.092 -58.883 1.00 98.91 O ATOM 3698 CG2 THR D2679 114.475 74.399 -60.504 1.00 97.75 C ATOM 3699 N ALA D2680 111.272 72.991 -60.033 1.00 94.08 N ATOM 3700 CA ALA D2680 110.740 71.681 -60.393 1.00 89.32 C ATOM 3701 C ALA D2680 109.560 71.726 -61.358 1.00 86.85 C ATOM 3702 O ALA D2680 109.518 70.970 -62.328 1.00 85.18 O ATOM 3703 CB ALA D2680 110.345 70.936 -59.129 1.00 86.21 C ATOM 3704 N VAL D2681 108.601 72.604 -61.079 1.00 86.63 N ATOM 3705 CA VAL D2681 107.420 72.744 -61.926 1.00 86.89 C ATOM 3706 C VAL D2681 107.872 73.023 -63.350 1.00 89.65 C ATOM 3707 O VAL D2681 107.283 72.527 -64.313 1.00 86.89 O ATOM 3708 CB VAL D2681 106.530 73.924 -61.479 1.00 85.25 C ATOM 3709 CG1 VAL D2681 105.203 73.867 -62.205 1.00 84.38 C ATOM 3710 CG2 VAL D2681 106.324 73.896 -59.980 1.00 85.19 C ATOM 3711 N LYS D2682 108.926 73.827 -63.466 1.00 93.54 N ATOM 3712 CA LYS D2682 109.475 74.197 -64.761 1.00 93.82 C ATOM 3713 C LYS D2682 110.337 73.078 -65.329 1.00 90.91 C ATOM 3714 O LYS D2682 110.312 72.827 -66.529 1.00 89.62 O ATOM 3715 CB LYS D2682 110.299 75.480 -64.644 1.00 95.89 C ATOM 3716 CG LYS D2682 110.821 75.989 -65.980 1.00 99.62 C ATOM 3717 CD LYS D2682 111.686 77.224 -65.799 1.00102.97 C ATOM 3718 CE LYS D2682 112.299 77.673 -67.114 1.00104.31 C ATOM 3719 NZ LYS D2682 113.133 78.896 -66.937 1.00105.76 N ATOM 3720 N LYS D2683 111.102 72.411 -64.470 1.00 89.35 N ATOM 3721 CA LYS D2683 111.947 71.310 -64.922 1.00 90.36 C ATOM 3722 C LYS D2683 111.041 70.337 -65.666 1.00 93.16 C ATOM 3723 O LYS D2683 111.459 69.633 -66.587 1.00 91.78 O ATOM 3724 CB LYS D2683 112.596 70.612 -63.723 1.00 87.54 C ATOM 3725 N LEU D2684 109.783 70.323 -65.249 1.00 98.90 N ATOM 3726 CA LEU D2684 108.762 69.471 -65.837 1.00104.21 C ATOM 3727 C LEU D2684 108.390 70.008 -67.221 1.00106.42 C ATOM 3728 O LEU D2684 107.908 69.266 -68.080 1.00105.48 O ATOM 3729 CB LEU D2684 107.537 69.458 -64.913 1.00104.18 C ATOM 3730 CG LEU D2684 106.231 68.786 -65.335 1.00101.82 C ATOM 3731 CD1 LEU D2684 106.468 67.327 -65.713 1.00102.33 C ATOM 3732 CD2 LEU D2684 105.245 68.904 -64.182 1.00 98.53 C ATOM 3733 N ASN D2685 108.641 71.301 -67.415 1.00109.54 N ATOM 3734 CA ASN D2685 108.365 72.022 -68.659 1.00112.98 C ATOM 3735 C ASN D2685 107.386 71.368 -69.629 1.00113.04 C ATOM 3736 O ASN D2685 106.242 71.812 -69.749 1.00111.87 O ATOM 3737 CB ASN D2685 109.681 72.349 -69.383 1.00115.81 C ATOM 3738 CG ASN D2685 110.581 71.136 -69.566 1.00118.71 C ATOM 3739 OD1 ASN D2685 111.712 71.265 -70.034 1.00120.63 O ATOM 3740 ND2 ASN D2685 110.087 69.959 -69.203 1.00119.25 N ATOM 3741 N GLY D2686 107.838 70.330 -70.329 1.00113.09 N ATOM 3742 CA GLY D2686 106.977 69.642 -71.275 1.00113.04 C ATOM 3743 C GLY D2686 105.630 69.304 -70.665 1.00113.02 C ATOM 3744 O GLY D2686 105.410 69.523 -69.473 1.00112.96 O ATOM 3745 N LYS D2687 104.724 68.765 -71.475 1.00112.45 N ATOM 3746 CA LYS D2687 103.398 68.408 -70.987 1.00111.96 C ATOM 3747 C LYS D2687 103.441 67.616 -69.680 1.00109.37 C ATOM 3748 O LYS D2687 104.512 67.231 -69.202 1.00108.47 O ATOM 3749 CB LYS D2687 102.622 67.632 -72.059 1.00114.44 C ATOM 3750 CG LYS D2687 102.222 68.486 -73.263 1.00115.45 C ATOM 3751 CD LYS D2687 101.126 67.819 -74.082 1.00115.75 C ATOM 3752 CE LYS D2687 100.584 68.755 -75.155 1.00115.13 C ATOM 3753 NZ LYS D2687 99.392 68.173 -75.839 1.00114.91 N ATOM 3754 N LEU D2688 102.266 67.373 -69.111 1.00105.74 N ATOM 3755 CA LEU D2688 102.157 66.670 -67.841 1.00103.61 C ATOM 3756 C LEU D2688 101.737 65.218 -67.999 1.00101.52 C ATOM 3757 O LEU D2688 101.741 64.455 -67.032 1.00 98.19 O ATOM 3758 CB LEU D2688 101.140 67.395 -66.964 1.00106.07 C ATOM 3759 CG LEU D2688 101.111 68.915 -67.151 1.00107.25 C ATOM 3760 CD1 LEU D2688 99.875 69.502 -66.493 1.00108.44 C ATOM 3761 CD2 LEU D2688 102.374 69.521 -66.570 1.00109.10 C ATOM 3762 N TYR D2689 101.376 64.841 -69.221 1.00102.09 N ATOM 3763 CA TYR D2689 100.928 63.482 -69.495 1.00105.35 C ATOM 3764 C TYR D2689 101.923 62.744 -70.381 1.00106.11 C ATOM 3765 O TYR D2689 102.065 63.060 -71.558 1.00104.20 O ATOM 3766 CB TYR D2689 99.549 63.526 -70.162 1.00107.81 C ATOM 3767 CG TYR D2689 98.611 64.540 -69.533 1.00109.74 C ATOM 3768 CD1 TYR D2689 98.695 65.896 -69.856 1.00109.79 C ATOM 3769 CD2 TYR D2689 97.679 64.152 -68.568 1.00110.54 C ATOM 3770 CE1 TYR D2689 97.877 66.840 -69.230 1.00109.18 C ATOM 3771 CE2 TYR D2689 96.859 65.089 -67.935 1.00109.17 C ATOM 3772 CZ TYR D2689 96.965 66.428 -68.270 1.00108.68 C ATOM 3773 OH TYR D2689 96.171 67.350 -67.631 1.00108.76 O ATOM 3774 N LEU D2690 102.599 61.750 -69.809 1.00109.71 N ATOM 3775 CA LEU D2690 103.605 60.974 -70.531 1.00115.01 C ATOM 3776 C LEU D2690 103.109 60.291 -71.799 1.00120.90 C ATOM 3777 O LEU D2690 103.910 59.867 -72.635 1.00121.33 O ATOM 3778 CB LEU D2690 104.243 59.923 -69.606 1.00112.10 C ATOM 3779 CG LEU D2690 103.401 58.818 -68.953 1.00108.50 C ATOM 3780 CD1 LEU D2690 102.742 57.942 -70.008 1.00105.59 C ATOM 3781 CD2 LEU D2690 104.304 57.978 -68.053 1.00104.94 C ATOM 3782 N ASP D2691 101.793 60.178 -71.942 1.00127.82 N ATOM 3783 CA ASP D2691 101.214 59.536 -73.117 1.00134.10 C ATOM 3784 C ASP D2691 101.887 60.006 -74.408 1.00136.17 C ATOM 3785 O ASP D2691 101.703 61.144 -74.848 1.00136.39 O ATOM 3786 CB ASP D2691 99.707 59.805 -73.178 1.00136.34 C ATOM 3787 CG ASP D2691 98.950 59.146 -72.036 1.00137.66 C ATOM 3788 OD1 ASP D2691 98.987 57.898 -71.938 1.00136.44 O ATOM 3789 OD2 ASP D2691 98.320 59.877 -71.239 1.00138.87 O ATOM 3790 N GLY D2692 102.671 59.116 -75.006 1.00137.27 N ATOM 3791 CA GLY D2692 103.370 59.449 -76.230 1.00139.36 C ATOM 3792 C GLY D2692 104.869 59.431 -76.013 1.00141.72 C ATOM 3793 O GLY D2692 105.616 60.059 -76.764 1.00143.07 O ATOM 3794 N SER D2693 105.308 58.710 -74.982 1.00142.80 N ATOM 3795 CA SER D2693 106.731 58.605 -74.657 1.00142.38 C ATOM 3796 C SER D2693 107.347 57.316 -75.202 1.00141.13 C ATOM 3797 O SER D2693 108.274 57.418 -76.037 1.00138.97 O ATOM 3798 CB SER D2693 106.937 58.669 -73.137 1.00141.63 C ATOM 3799 OG SER D2693 106.309 57.579 -72.484 1.00140.90 O TER 3838 HOH C 28 HETATM 3839 O HOH D 2 103.950 71.685 -70.950 1.00 47.45 O HETATM 3840 O HOH D 4 114.937 65.053 -49.249 1.00 50.05 O HETATM 3841 O HOH D 11 109.479 50.473 -57.132 1.00 65.38 O HETATM 3842 O HOH D 12 106.815 53.882 -52.217 1.00 72.95 O HETATM 3843 O HOH D 14 113.913 39.175 -44.374 1.00 53.69 O HETATM 3844 O HOH D 15 113.453 53.526 -60.619 1.00 58.50 O HETATM 3845 O HOH D 19 101.962 49.748 -41.813 1.00 52.49 O HETATM 3846 O HOH D 20 91.588 22.988 -57.516 1.00 59.94 O HETATM 3847 O HOH D 22 108.938 41.108 -53.004 1.00 63.00 O CONECT 1952 1951 1953 2753 CONECT 2753 1952 2752 END