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 52 52 ILE A 4 ASP A 19 1 16 HELIX 53 53 LEU A 94 GLU A 98 1 5 HELIX 54 54 THR A 108 GLU A 122 1 15 HELIX 55 55 GLN A 130 LYS A 154 1 25 HELIX 56 56 HIS B 43 ARG B 54 1 12 HELIX 57 57 THR B 76 GLY B 81 1 6 HELIX 58 58 ALA C 432 PHE C 440 1 9 HELIX 59 59 LEU C 446 SER C 454 1 9 HELIX 60 60 LEU C 456 THR C 461 1 6 HELIX 61 61 ASP C 465 SER C 478 1 14 HELIX 62 62 ALA C 484 PHE C 502 1 19 HELIX 63 63 ASN C 508 MET C 520 1 13 HELIX 64 64 LEU C 535 VAL C 546 1 12 HELIX 65 65 LEU C 555 LYS C 565 1 11 HELIX 66 66 SER C 568 VAL C 587 1 20 HELIX 67 67 THR D 2641 LEU D 2651 1 11 HELIX 68 68 ASP D 2676 LEU D 2684 1 9 SHEET 31 31 1 VAL A 25 LYS A 30 0 SHEET 32 32 1 MET A 36 PRO A 46 0 SHEET 33 33 1 LEU A 57 LEU A 63 0 SHEET 34 34 1 LYS A 74 PHE A 77 0 SHEET 35 35 1 ILE B 22 ILE B 27 0 SHEET 36 36 1 GLU B 33 VAL B 38 0 SHEET 37 37 1 PHE B 64 PHE B 66 0 SHEET 38 38 1 GLN B 69 ARG B 70 0 SHEET 39 39 1 VAL B 87 VAL B 90 0 SHEET 40 40 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 60.960 25.770 44.445 1.00140.94 N ATOM 3304 CA SER D2629 60.050 26.607 43.609 1.00141.66 C ATOM 3305 C SER D2629 60.834 27.442 42.599 1.00143.21 C ATOM 3306 O SER D2629 61.116 26.991 41.485 1.00143.40 O ATOM 3307 CB SER D2629 59.208 27.528 44.505 1.00140.69 C ATOM 3308 OG SER D2629 60.021 28.374 45.302 1.00137.83 O ATOM 3309 N LEU D2630 61.181 28.663 42.996 1.00143.79 N ATOM 3310 CA LEU D2630 61.935 29.574 42.140 1.00142.41 C ATOM 3311 C LEU D2630 63.342 29.758 42.710 1.00138.81 C ATOM 3312 O LEU D2630 63.521 30.411 43.741 1.00138.86 O ATOM 3313 CB LEU D2630 61.206 30.921 42.059 1.00144.17 C ATOM 3314 CG LEU D2630 59.755 30.845 41.561 1.00144.40 C ATOM 3315 CD1 LEU D2630 59.108 32.222 41.607 1.00143.95 C ATOM 3316 CD2 LEU D2630 59.731 30.288 40.141 1.00145.04 C ATOM 3317 N ASP D2631 64.338 29.177 42.044 1.00133.75 N ATOM 3318 CA ASP D2631 65.717 29.269 42.517 1.00127.91 C ATOM 3319 C ASP D2631 66.436 30.583 42.224 1.00123.50 C ATOM 3320 O ASP D2631 66.466 31.080 41.094 1.00122.22 O ATOM 3321 CB ASP D2631 66.557 28.094 41.992 1.00126.19 C ATOM 3322 CG ASP D2631 66.575 26.911 42.955 1.00124.03 C ATOM 3323 OD1 ASP D2631 66.991 27.091 44.119 1.00119.77 O ATOM 3324 OD2 ASP D2631 66.178 25.797 42.549 1.00125.49 O ATOM 3325 N VAL D2632 67.010 31.125 43.289 1.00117.76 N ATOM 3326 CA VAL D2632 67.761 32.364 43.272 1.00111.41 C ATOM 3327 C VAL D2632 68.753 32.180 44.405 1.00107.81 C ATOM 3328 O VAL D2632 68.380 32.235 45.577 1.00106.15 O ATOM 3329 CB VAL D2632 66.858 33.558 43.591 1.00112.06 C ATOM 3330 CG1 VAL D2632 67.677 34.828 43.654 1.00112.51 C ATOM 3331 CG2 VAL D2632 65.775 33.675 42.541 1.00115.30 C ATOM 3332 N LEU D2633 70.012 31.942 44.058 1.00104.39 N ATOM 3333 CA LEU D2633 71.034 31.725 45.070 1.00102.46 C ATOM 3334 C LEU D2633 72.088 32.829 45.086 1.00101.16 C ATOM 3335 O LEU D2633 72.627 33.204 44.040 1.00 99.30 O ATOM 3336 CB LEU D2633 71.696 30.351 44.841 1.00102.18 C ATOM 3337 CG LEU D2633 72.679 29.768 45.871 1.00102.04 C ATOM 3338 CD1 LEU D2633 72.611 28.250 45.833 1.00100.09 C ATOM 3339 CD2 LEU D2633 74.100 30.253 45.601 1.00100.48 C ATOM 3340 N ILE D2634 72.363 33.355 46.282 1.00 99.38 N ATOM 3341 CA ILE D2634 73.374 34.396 46.456 1.00 96.60 C ATOM 3342 C ILE D2634 74.717 33.710 46.245 1.00 94.81 C ATOM 3343 O ILE D2634 75.101 32.841 47.027 1.00 95.81 O ATOM 3344 CB ILE D2634 73.354 34.986 47.881 1.00 94.80 C ATOM 3345 CG1 ILE D2634 71.921 35.310 48.300 1.00 95.20 C ATOM 3346 CG2 ILE D2634 74.204 36.246 47.926 1.00 92.37 C ATOM 3347 CD1 ILE D2634 71.799 35.859 49.707 1.00 93.88 C ATOM 3348 N VAL D2635 75.432 34.094 45.195 1.00 92.00 N ATOM 3349 CA VAL D2635 76.711 33.471 44.900 1.00 90.27 C ATOM 3350 C VAL D2635 77.928 34.235 45.405 1.00 92.54 C ATOM 3351 O VAL D2635 78.958 33.632 45.698 1.00 94.74 O ATOM 3352 CB VAL D2635 76.857 33.247 43.397 1.00 87.22 C ATOM 3353 CG1 VAL D2635 78.145 32.512 43.100 1.00 87.62 C ATOM 3354 CG2 VAL D2635 75.673 32.459 42.894 1.00 86.94 C ATOM 3355 N TYR D2636 77.816 35.554 45.513 1.00 92.71 N ATOM 3356 CA TYR D2636 78.936 36.363 45.984 1.00 91.74 C ATOM 3357 C TYR D2636 78.504 37.650 46.672 1.00 91.44 C ATOM 3358 O TYR D2636 77.535 38.286 46.263 1.00 94.91 O ATOM 3359 CB TYR D2636 79.850 36.712 44.812 1.00 93.05 C ATOM 3360 CG TYR D2636 80.874 37.781 45.128 1.00 97.23 C ATOM 3361 CD1 TYR D2636 81.908 37.541 46.035 1.00 98.69 C ATOM 3362 CD2 TYR D2636 80.804 39.038 44.525 1.00 97.91 C ATOM 3363 CE1 TYR D2636 82.849 38.531 46.333 1.00 98.92 C ATOM 3364 CE2 TYR D2636 81.736 40.033 44.816 1.00 97.98 C ATOM 3365 CZ TYR D2636 82.754 39.773 45.719 1.00 99.03 C ATOM 3366 OH TYR D2636 83.666 40.760 46.014 1.00100.19 O ATOM 3367 N GLU D2637 79.226 38.028 47.721 1.00 87.90 N ATOM 3368 CA GLU D2637 78.936 39.265 48.438 1.00 86.42 C ATOM 3369 C GLU D2637 80.251 39.936 48.836 1.00 84.85 C ATOM 3370 O GLU D2637 81.070 39.350 49.544 1.00 85.08 O ATOM 3371 CB GLU D2637 78.074 38.997 49.679 1.00 87.16 C ATOM 3372 CG GLU D2637 78.680 38.033 50.689 1.00 91.72 C ATOM 3373 CD GLU D2637 78.106 38.201 52.092 1.00 92.71 C ATOM 3374 OE1 GLU D2637 76.869 38.348 52.223 1.00 93.69 O ATOM 3375 OE2 GLU D2637 78.895 38.172 53.064 1.00 90.44 O ATOM 3376 N LEU D2638 80.450 41.164 48.368 1.00 82.36 N ATOM 3377 CA LEU D2638 81.667 41.919 48.656 1.00 78.42 C ATOM 3378 C LEU D2638 81.924 42.027 50.159 1.00 76.33 C ATOM 3379 O LEU D2638 81.105 42.559 50.904 1.00 74.22 O ATOM 3380 CB LEU D2638 81.558 43.321 48.045 1.00 76.30 C ATOM 3381 CG LEU D2638 82.843 44.111 47.776 1.00 73.34 C ATOM 3382 CD1 LEU D2638 82.482 45.503 47.271 1.00 71.68 C ATOM 3383 CD2 LEU D2638 83.676 44.205 49.040 1.00 73.99 C ATOM 3384 N THR D2639 83.072 41.526 50.595 1.00 75.83 N ATOM 3385 CA THR D2639 83.435 41.574 52.005 1.00 79.30 C ATOM 3386 C THR D2639 84.739 42.335 52.212 1.00 79.11 C ATOM 3387 O THR D2639 85.642 42.273 51.380 1.00 79.86 O ATOM 3388 CB THR D2639 83.604 40.154 52.589 1.00 81.61 C ATOM 3389 OG1 THR D2639 82.346 39.466 52.539 1.00 84.13 O ATOM 3390 CG2 THR D2639 84.094 40.220 54.038 1.00 79.64 C ATOM 3391 N PRO D2640 84.847 43.069 53.328 1.00 78.30 N ATOM 3392 CA PRO D2640 86.051 43.840 53.634 1.00 77.86 C ATOM 3393 C PRO D2640 87.001 43.133 54.607 1.00 78.72 C ATOM 3394 O PRO D2640 86.726 42.035 55.089 1.00 79.95 O ATOM 3395 CB PRO D2640 85.479 45.107 54.234 1.00 77.18 C ATOM 3396 CG PRO D2640 84.377 44.554 55.079 1.00 76.74 C ATOM 3397 CD PRO D2640 83.720 43.524 54.164 1.00 77.92 C ATOM 3398 N THR D2641 88.119 43.796 54.881 1.00 78.10 N ATOM 3399 CA THR D2641 89.152 43.320 55.793 1.00 74.79 C ATOM 3400 C THR D2641 88.605 43.326 57.192 1.00 72.19 C ATOM 3401 O THR D2641 87.631 44.009 57.472 1.00 72.20 O ATOM 3402 CB THR D2641 90.360 44.272 55.782 1.00 77.54 C ATOM 3403 OG1 THR D2641 91.071 44.118 54.549 1.00 85.04 O ATOM 3404 CG2 THR D2641 91.284 44.020 56.968 1.00 73.90 C ATOM 3405 N ALA D2642 89.237 42.574 58.078 1.00 74.93 N ATOM 3406 CA ALA D2642 88.810 42.551 59.467 1.00 78.87 C ATOM 3407 C ALA D2642 88.946 43.970 60.022 1.00 79.82 C ATOM 3408 O ALA D2642 88.034 44.483 60.674 1.00 76.63 O ATOM 3409 CB ALA D2642 89.678 41.584 60.271 1.00 79.59 C ATOM 3410 N GLU D2643 90.083 44.603 59.745 1.00 83.51 N ATOM 3411 CA GLU D2643 90.332 45.957 60.220 1.00 87.57 C ATOM 3412 C GLU D2643 89.417 46.995 59.547 1.00 88.00 C ATOM 3413 O GLU D2643 89.023 47.979 60.179 1.00 88.67 O ATOM 3414 CB GLU D2643 91.803 46.328 60.004 1.00 91.99 C ATOM 3415 CG GLU D2643 92.186 47.694 60.583 1.00 98.80 C ATOM 3416 CD GLU D2643 93.682 47.995 60.504 1.00102.01 C ATOM 3417 OE1 GLU D2643 94.258 47.889 59.397 1.00104.77 O ATOM 3418 OE2 GLU D2643 94.279 48.350 61.546 1.00100.80 O ATOM 3419 N GLN D2644 89.077 46.774 58.275 1.00 85.10 N ATOM 3420 CA GLN D2644 88.201 47.698 57.547 1.00 81.31 C ATOM 3421 C GLN D2644 86.795 47.734 58.145 1.00 78.64 C ATOM 3422 O GLN D2644 86.306 48.787 58.560 1.00 77.29 O ATOM 3423 CB GLN D2644 88.106 47.294 56.077 1.00 82.31 C ATOM 3424 CG GLN D2644 89.432 47.299 55.352 1.00 86.95 C ATOM 3425 CD GLN D2644 89.299 46.951 53.878 1.00 90.19 C ATOM 3426 OE1 GLN D2644 88.812 45.877 53.514 1.00 88.99 O ATOM 3427 NE2 GLN D2644 89.739 47.863 53.020 1.00 94.16 N ATOM 3428 N LYS D2645 86.148 46.572 58.172 1.00 75.52 N ATOM 3429 CA LYS D2645 84.806 46.441 58.722 1.00 71.77 C ATOM 3430 C LYS D2645 84.776 46.998 60.136 1.00 71.17 C ATOM 3431 O LYS D2645 83.845 47.701 60.514 1.00 72.08 O ATOM 3432 CB LYS D2645 84.397 44.971 58.736 1.00 70.45 C ATOM 3433 CG LYS D2645 83.078 44.670 59.435 1.00 72.06 C ATOM 3434 CD LYS D2645 82.761 43.167 59.377 1.00 73.17 C ATOM 3435 CE LYS D2645 81.468 42.821 60.107 1.00 74.56 C ATOM 3436 NZ LYS D2645 81.173 41.362 60.072 1.00 71.93 N ATOM 3437 N ALA D2646 85.807 46.685 60.912 1.00 70.43 N ATOM 3438 CA ALA D2646 85.899 47.156 62.288 1.00 69.87 C ATOM 3439 C ALA D2646 86.018 48.681 62.376 1.00 67.31 C ATOM 3440 O ALA D2646 85.548 49.291 63.339 1.00 69.36 O ATOM 3441 CB ALA D2646 87.084 46.491 62.984 1.00 71.62 C ATOM 3442 N LEU D2647 86.658 49.293 61.386 1.00 61.29 N ATOM 3443 CA LEU D2647 86.795 50.746 61.379 1.00 59.81 C ATOM 3444 C LEU D2647 85.421 51.354 61.149 1.00 59.55 C ATOM 3445 O LEU D2647 84.965 52.212 61.912 1.00 56.83 O ATOM 3446 CB LEU D2647 87.728 51.195 60.253 1.00 60.00 C ATOM 3447 CG LEU D2647 87.674 52.683 59.868 1.00 54.22 C ATOM 3448 CD1 LEU D2647 88.130 53.551 61.032 1.00 46.34 C ATOM 3449 CD2 LEU D2647 88.552 52.916 58.654 1.00 51.17 C ATOM 3450 N ALA D2648 84.780 50.897 60.074 1.00 58.69 N ATOM 3451 CA ALA D2648 83.450 51.351 59.688 1.00 60.98 C ATOM 3452 C ALA D2648 82.455 51.149 60.830 1.00 62.47 C ATOM 3453 O ALA D2648 81.536 51.947 61.032 1.00 60.09 O ATOM 3454 CB ALA D2648 82.993 50.587 58.455 1.00 60.70 C ATOM 3455 N THR D2649 82.642 50.057 61.562 1.00 64.66 N ATOM 3456 CA THR D2649 81.793 49.732 62.696 1.00 65.82 C ATOM 3457 C THR D2649 81.934 50.822 63.753 1.00 67.77 C ATOM 3458 O THR D2649 80.986 51.133 64.475 1.00 69.51 O ATOM 3459 CB THR D2649 82.210 48.400 63.315 1.00 66.85 C ATOM 3460 OG1 THR D2649 82.001 47.348 62.364 1.00 69.30 O ATOM 3461 CG2 THR D2649 81.408 48.129 64.576 1.00 69.28 C ATOM 3462 N LYS D2650 83.130 51.393 63.845 1.00 68.03 N ATOM 3463 CA LYS D2650 83.394 52.450 64.806 1.00 65.06 C ATOM 3464 C LYS D2650 82.747 53.738 64.312 1.00 65.35 C ATOM 3465 O LYS D2650 82.219 54.525 65.099 1.00 64.78 O ATOM 3466 CB LYS D2650 84.902 52.647 64.963 1.00 61.22 C ATOM 3467 CG LYS D2650 85.278 53.680 66.012 1.00 60.04 C ATOM 3468 N LEU D2651 82.769 53.928 62.996 1.00 64.72 N ATOM 3469 CA LEU D2651 82.212 55.124 62.377 1.00 63.51 C ATOM 3470 C LEU D2651 80.756 55.021 61.943 1.00 61.56 C ATOM 3471 O LEU D2651 80.230 55.921 61.286 1.00 60.77 O ATOM 3472 CB LEU D2651 83.069 55.516 61.179 1.00 62.94 C ATOM 3473 CG LEU D2651 84.554 55.605 61.514 1.00 60.32 C ATOM 3474 CD1 LEU D2651 85.272 56.240 60.345 1.00 62.38 C ATOM 3475 CD2 LEU D2651 84.767 56.429 62.779 1.00 56.70 C ATOM 3476 N LYS D2652 80.108 53.923 62.308 1.00 59.31 N ATOM 3477 CA LYS D2652 78.706 53.719 61.976 1.00 57.12 C ATOM 3478 C LYS D2652 78.469 53.828 60.479 1.00 56.89 C ATOM 3479 O LYS D2652 77.403 54.270 60.049 1.00 58.37 O ATOM 3480 CB LYS D2652 77.850 54.760 62.699 1.00 55.63 C ATOM 3481 CG LYS D2652 78.490 55.294 63.959 1.00 54.82 C ATOM 3482 CD LYS D2652 78.622 54.228 65.018 1.00 58.17 C ATOM 3483 CE LYS D2652 77.305 54.042 65.734 1.00 63.23 C ATOM 3484 NZ LYS D2652 76.877 55.331 66.360 1.00 68.37 N ATOM 3485 N LEU D2653 79.465 53.432 59.692 1.00 56.44 N ATOM 3486 CA LEU D2653 79.373 53.474 58.230 1.00 55.99 C ATOM 3487 C LEU D2653 79.059 52.087 57.679 1.00 56.98 C ATOM 3488 O LEU D2653 79.255 51.078 58.359 1.00 56.41 O ATOM 3489 CB LEU D2653 80.698 53.944 57.632 1.00 55.63 C ATOM 3490 CG LEU D2653 81.175 55.357 57.942 1.00 56.26 C ATOM 3491 CD1 LEU D2653 82.667 55.484 57.661 1.00 54.16 C ATOM 3492 CD2 LEU D2653 80.379 56.329 57.101 1.00 58.73 C ATOM 3493 N PRO D2654 78.572 52.016 56.431 1.00 58.72 N ATOM 3494 CA PRO D2654 78.247 50.722 55.820 1.00 62.70 C ATOM 3495 C PRO D2654 79.507 49.863 55.670 1.00 66.46 C ATOM 3496 O PRO D2654 80.454 50.254 54.992 1.00 69.57 O ATOM 3497 CB PRO D2654 77.645 51.118 54.476 1.00 61.45 C ATOM 3498 CG PRO D2654 78.371 52.381 54.150 1.00 60.57 C ATOM 3499 CD PRO D2654 78.374 53.115 55.473 1.00 57.68 C ATOM 3500 N PRO D2655 79.532 48.681 56.309 1.00 67.71 N ATOM 3501 CA PRO D2655 80.656 47.745 56.278 1.00 68.73 C ATOM 3502 C PRO D2655 81.484 47.705 55.000 1.00 70.55 C ATOM 3503 O PRO D2655 82.695 47.514 55.046 1.00 71.00 O ATOM 3504 CB PRO D2655 79.986 46.425 56.596 1.00 67.99 C ATOM 3505 CG PRO D2655 79.030 46.844 57.661 1.00 66.95 C ATOM 3506 CD PRO D2655 78.409 48.097 57.061 1.00 68.01 C ATOM 3507 N THR D2656 80.841 47.885 53.859 1.00 73.06 N ATOM 3508 CA THR D2656 81.566 47.876 52.598 1.00 76.90 C ATOM 3509 C THR D2656 81.926 49.301 52.209 1.00 77.24 C ATOM 3510 O THR D2656 81.643 49.718 51.089 1.00 80.65 O ATOM 3511 CB THR D2656 80.700 47.293 51.475 1.00 81.61 C ATOM 3512 OG1 THR D2656 79.458 48.009 51.413 1.00 82.91 O ATOM 3513 CG2 THR D2656 80.420 45.824 51.726 1.00 87.92 C ATOM 3514 N PHE D2657 82.556 50.054 53.106 1.00 74.73 N ATOM 3515 CA PHE D2657 82.872 51.443 52.782 1.00 73.93 C ATOM 3516 C PHE D2657 84.267 51.679 52.207 1.00 76.82 C ATOM 3517 O PHE D2657 84.414 52.251 51.119 1.00 74.06 O ATOM 3518 CB PHE D2657 82.647 52.335 54.015 1.00 66.80 C ATOM 3519 CG PHE D2657 82.597 53.808 53.699 1.00 60.23 C ATOM 3520 CD1 PHE D2657 81.792 54.285 52.673 1.00 56.55 C ATOM 3521 CD2 PHE D2657 83.355 54.718 54.423 1.00 55.94 C ATOM 3522 CE1 PHE D2657 81.748 55.641 52.373 1.00 52.81 C ATOM 3523 CE2 PHE D2657 83.311 56.076 54.125 1.00 52.43 C ATOM 3524 CZ PHE D2657 82.508 56.535 53.099 1.00 48.91 C ATOM 3525 N PHE D2658 85.289 51.234 52.928 1.00 79.36 N ATOM 3526 CA PHE D2658 86.659 51.422 52.477 1.00 80.39 C ATOM 3527 C PHE D2658 87.063 50.399 51.429 1.00 82.82 C ATOM 3528 O PHE D2658 88.246 50.110 51.250 1.00 81.59 O ATOM 3529 CB PHE D2658 87.602 51.361 53.668 1.00 78.78 C ATOM 3530 CG PHE D2658 87.126 52.156 54.835 1.00 78.54 C ATOM 3531 CD1 PHE D2658 86.411 51.548 55.856 1.00 80.31 C ATOM 3532 CD2 PHE D2658 87.349 53.522 54.894 1.00 78.70 C ATOM 3533 CE1 PHE D2658 85.924 52.293 56.920 1.00 82.42 C ATOM 3534 CE2 PHE D2658 86.866 54.276 55.952 1.00 80.52 C ATOM 3535 CZ PHE D2658 86.151 53.662 56.967 1.00 82.26 C ATOM 3536 N CYS D2659 86.071 49.855 50.735 1.00 86.92 N ATOM 3537 CA CYS D2659 86.326 48.878 49.692 1.00 91.80 C ATOM 3538 C CYS D2659 86.740 49.645 48.448 1.00 95.04 C ATOM 3539 O CYS D2659 87.306 49.077 47.514 1.00 95.41 O ATOM 3540 CB CYS D2659 85.065 48.060 49.415 1.00 94.65 C ATOM 3541 SG CYS D2659 84.441 47.171 50.862 1.00103.42 S ATOM 3542 N TYR D2660 86.452 50.946 48.448 1.00 97.96 N ATOM 3543 CA TYR D2660 86.800 51.817 47.333 1.00 99.45 C ATOM 3544 C TYR D2660 88.316 51.769 47.143 1.00105.36 C ATOM 3545 O TYR D2660 88.810 51.774 46.011 1.00106.33 O ATOM 3546 CB TYR D2660 86.356 53.255 47.628 1.00 92.67 C ATOM 3547 CG TYR D2660 87.215 53.970 48.654 1.00 88.84 C ATOM 3548 CD1 TYR D2660 88.413 54.583 48.288 1.00 84.88 C ATOM 3549 CD2 TYR D2660 86.848 54.002 50.000 1.00 89.48 C ATOM 3550 CE1 TYR D2660 89.225 55.207 49.231 1.00 83.08 C ATOM 3551 CE2 TYR D2660 87.658 54.627 50.956 1.00 86.95 C ATOM 3552 CZ TYR D2660 88.844 55.224 50.562 1.00 84.80 C ATOM 3553 OH TYR D2660 89.656 55.822 51.498 1.00 83.35 O ATOM 3554 N LYS D2661 89.038 51.719 48.265 1.00110.66 N ATOM 3555 CA LYS D2661 90.501 51.671 48.274 1.00114.67 C ATOM 3556 C LYS D2661 90.995 50.229 48.340 1.00118.71 C ATOM 3557 O LYS D2661 92.195 49.970 48.264 1.00121.56 O ATOM 3558 CB LYS D2661 91.062 52.458 49.469 1.00112.65 C ATOM 3559 CG LYS D2661 90.710 51.881 50.842 1.00110.95 C ATOM 3560 CD LYS D2661 91.372 52.675 51.979 1.00109.08 C ATOM 3561 CE LYS D2661 91.072 52.064 53.351 1.00106.34 C ATOM 3562 NZ LYS D2661 91.808 52.726 54.467 1.00101.43 N ATOM 3563 N ASN D2662 90.062 49.295 48.486 1.00121.06 N ATOM 3564 CA ASN D2662 90.401 47.880 48.547 1.00123.82 C ATOM 3565 C ASN D2662 90.536 47.373 47.108 1.00126.16 C ATOM 3566 O ASN D2662 91.066 46.291 46.862 1.00124.81 O ATOM 3567 CB ASN D2662 89.293 47.116 49.279 1.00123.87 C ATOM 3568 CG ASN D2662 89.782 45.817 49.896 1.00122.94 C ATOM 3569 OD1 ASN D2662 90.636 45.820 50.783 1.00120.69 O ATOM 3570 ND2 ASN D2662 89.236 44.698 49.431 1.00123.61 N ATOM 3571 N ARG D2663 90.056 48.180 46.163 1.00130.74 N ATOM 3572 CA ARG D2663 90.100 47.852 44.737 1.00134.00 C ATOM 3573 C ARG D2663 91.537 47.760 44.211 1.00136.26 C ATOM 3574 O ARG D2663 92.485 48.158 44.895 1.00136.05 O ATOM 3575 CB ARG D2663 89.326 48.907 43.931 1.00132.67 C ATOM 3576 CG ARG D2663 87.848 48.995 44.267 1.00130.83 C ATOM 3577 N PRO D2664 91.712 47.230 42.984 1.00137.51 N ATOM 3578 CA PRO D2664 93.038 47.089 42.373 1.00137.40 C ATOM 3579 C PRO D2664 93.623 48.376 41.777 1.00137.84 C ATOM 3580 O PRO D2664 94.801 48.666 41.972 1.00138.00 O ATOM 3581 CB PRO D2664 92.808 46.014 41.314 1.00135.85 C ATOM 3582 CG PRO D2664 91.423 46.308 40.860 1.00136.01 C ATOM 3583 CD PRO D2664 90.692 46.542 42.168 1.00136.95 C ATOM 3584 N ASP D2665 92.803 49.144 41.062 1.00138.21 N ATOM 3585 CA ASP D2665 93.261 50.382 40.427 1.00137.89 C ATOM 3586 C ASP D2665 93.808 51.438 41.393 1.00139.25 C ATOM 3587 O ASP D2665 94.430 51.110 42.406 1.00140.01 O ATOM 3588 CB ASP D2665 92.136 50.995 39.579 1.00136.53 C ATOM 3589 CG ASP D2665 90.929 51.393 40.404 1.00135.73 C ATOM 3590 N TYR D2666 93.570 52.705 41.063 1.00140.29 N ATOM 3591 CA TYR D2666 94.045 53.843 41.855 1.00141.22 C ATOM 3592 C TYR D2666 93.849 53.788 43.376 1.00140.77 C ATOM 3593 O TYR D2666 92.766 54.088 43.888 1.00140.83 O ATOM 3594 CB TYR D2666 93.427 55.142 41.313 1.00141.57 C ATOM 3595 CG TYR D2666 91.914 55.152 41.290 1.00140.56 C ATOM 3596 N VAL D2667 94.911 53.418 44.091 1.00138.78 N ATOM 3597 CA VAL D2667 94.885 53.350 45.550 1.00136.80 C ATOM 3598 C VAL D2667 96.300 53.296 46.114 1.00136.31 C ATOM 3599 O VAL D2667 97.200 52.725 45.501 1.00134.02 O ATOM 3600 CB VAL D2667 94.108 52.119 46.062 1.00134.87 C ATOM 3601 CG1 VAL D2667 94.788 50.840 45.602 1.00133.20 C ATOM 3602 CG2 VAL D2667 94.012 52.167 47.581 1.00131.26 C ATOM 3603 N SER D2668 96.486 53.902 47.284 1.00137.22 N ATOM 3604 CA SER D2668 97.787 53.934 47.946 1.00138.34 C ATOM 3605 C SER D2668 97.623 54.311 49.416 1.00140.25 C ATOM 3606 O SER D2668 96.878 53.663 50.149 1.00141.70 O ATOM 3607 CB SER D2668 98.706 54.942 47.252 1.00137.09 C ATOM 3608 OG SER D2668 98.162 56.249 47.310 1.00135.94 O ATOM 3609 N GLU D2669 98.324 55.356 49.845 1.00141.39 N ATOM 3610 CA GLU D2669 98.244 55.823 51.225 1.00143.09 C ATOM 3611 C GLU D2669 98.974 57.154 51.406 1.00145.03 C ATOM 3612 O GLU D2669 99.788 57.312 52.320 1.00145.31 O ATOM 3613 CB GLU D2669 98.819 54.767 52.181 1.00142.09 C ATOM 3614 CG GLU D2669 100.247 54.346 51.880 1.00141.30 C ATOM 3615 N GLU D2670 98.674 58.111 50.530 1.00147.07 N ATOM 3616 CA GLU D2670 99.299 59.431 50.583 1.00149.28 C ATOM 3617 C GLU D2670 98.667 60.434 49.606 1.00150.11 C ATOM 3618 O GLU D2670 98.571 60.167 48.407 1.00151.35 O ATOM 3619 CB GLU D2670 100.804 59.305 50.302 1.00149.28 C ATOM 3620 CG GLU D2670 101.149 58.597 48.998 1.00148.28 C ATOM 3621 N GLU D2671 98.243 61.583 50.137 1.00149.53 N ATOM 3622 CA GLU D2671 97.624 62.661 49.355 1.00148.23 C ATOM 3623 C GLU D2671 97.162 63.809 50.258 1.00147.84 C ATOM 3624 O GLU D2671 96.588 63.568 51.322 1.00148.56 O ATOM 3625 CB GLU D2671 96.420 62.139 48.561 1.00146.56 C ATOM 3626 CG GLU D2671 96.738 61.770 47.126 1.00145.18 C ATOM 3627 CD GLU D2671 97.506 62.865 46.414 1.00144.53 C ATOM 3628 OE1 GLU D2671 97.005 64.006 46.359 1.00144.10 O ATOM 3629 OE2 GLU D2671 98.614 62.586 45.913 1.00144.82 O ATOM 3630 N GLU D2672 97.405 65.051 49.836 1.00145.32 N ATOM 3631 CA GLU D2672 96.990 66.208 50.630 1.00142.32 C ATOM 3632 C GLU D2672 95.814 66.971 50.024 1.00140.64 C ATOM 3633 O GLU D2672 95.910 67.526 48.927 1.00139.72 O ATOM 3634 CB GLU D2672 98.158 67.172 50.850 1.00141.71 C ATOM 3635 CG GLU D2672 97.780 68.344 51.744 1.00142.10 C ATOM 3636 CD GLU D2672 98.977 69.137 52.221 1.00143.25 C ATOM 3637 OE1 GLU D2672 99.702 69.698 51.373 1.00144.25 O ATOM 3638 OE2 GLU D2672 99.189 69.197 53.450 1.00143.76 O ATOM 3639 N ASP D2673 94.712 66.997 50.770 1.00138.82 N ATOM 3640 CA ASP D2673 93.468 67.654 50.372 1.00135.05 C ATOM 3641 C ASP D2673 93.517 69.160 50.587 1.00133.22 C ATOM 3642 O ASP D2673 93.865 69.624 51.673 1.00131.86 O ATOM 3643 CB ASP D2673 92.309 67.069 51.186 1.00133.17 C ATOM 3644 CG ASP D2673 90.961 67.639 50.792 1.00131.52 C ATOM 3645 OD1 ASP D2673 90.808 68.876 50.766 1.00131.26 O ATOM 3646 OD2 ASP D2673 90.044 66.843 50.517 1.00131.34 O ATOM 3647 N ASP D2674 93.159 69.921 49.557 1.00131.96 N ATOM 3648 CA ASP D2674 93.149 71.371 49.687 1.00131.37 C ATOM 3649 C ASP D2674 92.329 72.125 48.649 1.00130.31 C ATOM 3650 O ASP D2674 91.795 73.192 48.953 1.00130.80 O ATOM 3651 CB ASP D2674 94.569 71.922 49.691 1.00132.58 C ATOM 3652 CG ASP D2674 94.594 73.426 49.830 1.00134.41 C ATOM 3653 OD1 ASP D2674 93.836 73.955 50.675 1.00132.32 O ATOM 3654 OD2 ASP D2674 95.368 74.075 49.097 1.00136.91 O ATOM 3655 N GLU D2675 92.237 71.585 47.435 1.00127.76 N ATOM 3656 CA GLU D2675 91.465 72.214 46.358 1.00125.35 C ATOM 3657 C GLU D2675 90.240 72.963 46.890 1.00124.38 C ATOM 3658 O GLU D2675 89.557 72.488 47.796 1.00124.55 O ATOM 3659 CB GLU D2675 91.006 71.154 45.352 1.00124.48 C ATOM 3660 CG GLU D2675 90.489 69.872 46.005 1.00125.39 C ATOM 3661 CD GLU D2675 89.651 69.018 45.067 1.00124.97 C ATOM 3662 OE1 GLU D2675 89.903 69.056 43.843 1.00124.19 O ATOM 3663 OE2 GLU D2675 88.750 68.299 45.556 1.00123.11 O ATOM 3664 N ASP D2676 89.969 74.139 46.332 1.00122.79 N ATOM 3665 CA ASP D2676 88.820 74.939 46.756 1.00120.45 C ATOM 3666 C ASP D2676 87.568 74.521 46.002 1.00115.69 C ATOM 3667 O ASP D2676 87.617 74.269 44.798 1.00115.72 O ATOM 3668 CB ASP D2676 89.079 76.428 46.512 1.00125.43 C ATOM 3669 CG ASP D2676 90.016 77.038 47.537 1.00129.83 C ATOM 3670 OD1 ASP D2676 89.668 77.042 48.737 1.00130.28 O ATOM 3671 OD2 ASP D2676 91.100 77.517 47.142 1.00133.56 O ATOM 3672 N PHE D2677 86.446 74.451 46.710 1.00109.34 N ATOM 3673 CA PHE D2677 85.190 74.062 46.084 1.00104.37 C ATOM 3674 C PHE D2677 85.096 74.651 44.675 1.00102.99 C ATOM 3675 O PHE D2677 85.118 73.919 43.686 1.00100.13 O ATOM 3676 CB PHE D2677 83.999 74.532 46.935 1.00 99.51 C ATOM 3677 CG PHE D2677 82.688 74.547 46.189 1.00 93.08 C ATOM 3678 CD1 PHE D2677 82.129 73.371 45.711 1.00 90.26 C ATOM 3679 CD2 PHE D2677 82.043 75.746 45.919 1.00 88.71 C ATOM 3680 CE1 PHE D2677 80.952 73.393 44.971 1.00 86.53 C ATOM 3681 CE2 PHE D2677 80.874 75.771 45.184 1.00 85.06 C ATOM 3682 CZ PHE D2677 80.326 74.595 44.706 1.00 84.91 C ATOM 3683 N GLU D2678 85.017 75.976 44.601 1.00103.96 N ATOM 3684 CA GLU D2678 84.903 76.690 43.335 1.00104.41 C ATOM 3685 C GLU D2678 85.835 76.148 42.267 1.00102.01 C ATOM 3686 O GLU D2678 85.442 75.956 41.114 1.00101.10 O ATOM 3687 CB GLU D2678 85.180 78.180 43.546 1.00108.95 C ATOM 3688 CG GLU D2678 85.091 78.993 42.266 1.00115.94 C ATOM 3689 CD GLU D2678 83.841 78.672 41.462 1.00119.78 C ATOM 3690 OE1 GLU D2678 82.721 78.907 41.975 1.00120.27 O ATOM 3691 OE2 GLU D2678 83.983 78.179 40.321 1.00122.31 O ATOM 3692 N THR D2679 87.081 75.916 42.653 1.00100.09 N ATOM 3693 CA THR D2679 88.070 75.383 41.729 1.00 98.36 C ATOM 3694 C THR D2679 87.500 74.105 41.109 1.00 95.70 C ATOM 3695 O THR D2679 87.291 74.021 39.894 1.00 90.89 O ATOM 3696 CB THR D2679 89.385 75.050 42.478 1.00 98.93 C ATOM 3697 OG1 THR D2679 89.873 76.226 43.140 1.00 98.91 O ATOM 3698 CG2 THR D2679 90.439 74.537 41.514 1.00 97.75 C ATOM 3699 N ALA D2680 87.233 73.132 41.981 1.00 94.08 N ATOM 3700 CA ALA D2680 86.699 71.824 41.617 1.00 89.32 C ATOM 3701 C ALA D2680 85.519 71.874 40.652 1.00 86.85 C ATOM 3702 O ALA D2680 85.476 71.121 39.680 1.00 85.18 O ATOM 3703 CB ALA D2680 86.303 71.076 42.879 1.00 86.21 C ATOM 3704 N VAL D2681 84.562 72.752 40.934 1.00 86.63 N ATOM 3705 CA VAL D2681 83.381 72.897 40.087 1.00 86.89 C ATOM 3706 C VAL D2681 83.833 73.179 38.664 1.00 89.65 C ATOM 3707 O VAL D2681 83.244 72.687 37.700 1.00 86.89 O ATOM 3708 CB VAL D2681 82.493 74.077 40.538 1.00 85.25 C ATOM 3709 CG1 VAL D2681 81.166 74.024 39.812 1.00 84.38 C ATOM 3710 CG2 VAL D2681 82.287 74.045 42.037 1.00 85.19 C ATOM 3711 N LYS D2682 84.889 73.982 38.550 1.00 93.54 N ATOM 3712 CA LYS D2682 85.438 74.355 37.257 1.00 93.82 C ATOM 3713 C LYS D2682 86.298 73.236 36.685 1.00 90.91 C ATOM 3714 O LYS D2682 86.273 72.989 35.485 1.00 89.62 O ATOM 3715 CB LYS D2682 86.264 75.636 37.377 1.00 95.89 C ATOM 3716 CG LYS D2682 86.787 76.148 36.043 1.00 99.62 C ATOM 3717 CD LYS D2682 87.654 77.381 36.227 1.00102.97 C ATOM 3718 CE LYS D2682 88.267 77.833 34.914 1.00104.31 C ATOM 3719 NZ LYS D2682 89.103 79.055 35.094 1.00105.76 N ATOM 3720 N LYS D2683 87.062 72.565 37.542 1.00 89.35 N ATOM 3721 CA LYS D2683 87.906 71.464 37.087 1.00 90.36 C ATOM 3722 C LYS D2683 86.998 70.495 36.340 1.00 93.16 C ATOM 3723 O LYS D2683 87.415 69.793 35.417 1.00 91.78 O ATOM 3724 CB LYS D2683 88.554 70.762 38.284 1.00 87.54 C ATOM 3725 N LEU D2684 85.740 70.482 36.757 1.00 98.90 N ATOM 3726 CA LEU D2684 84.718 69.633 36.167 1.00104.21 C ATOM 3727 C LEU D2684 84.347 70.175 34.784 1.00106.42 C ATOM 3728 O LEU D2684 83.864 69.436 33.923 1.00105.48 O ATOM 3729 CB LEU D2684 83.493 69.619 37.091 1.00104.18 C ATOM 3730 CG LEU D2684 82.186 68.950 36.667 1.00101.82 C ATOM 3731 CD1 LEU D2684 82.421 67.492 36.285 1.00102.33 C ATOM 3732 CD2 LEU D2684 81.200 69.067 37.820 1.00 98.53 C ATOM 3733 N ASN D2685 84.600 71.468 34.594 1.00109.54 N ATOM 3734 CA ASN D2685 84.325 72.193 33.352 1.00112.98 C ATOM 3735 C ASN D2685 83.345 71.543 32.380 1.00113.04 C ATOM 3736 O ASN D2685 82.201 71.989 32.262 1.00111.87 O ATOM 3737 CB ASN D2685 85.641 72.520 32.629 1.00115.81 C ATOM 3738 CG ASN D2685 86.539 71.306 32.443 1.00118.71 C ATOM 3739 OD1 ASN D2685 87.670 71.435 31.975 1.00120.63 O ATOM 3740 ND2 ASN D2685 86.044 70.129 32.802 1.00119.25 N ATOM 3741 N GLY D2686 83.795 70.507 31.677 1.00113.09 N ATOM 3742 CA GLY D2686 82.933 69.823 30.729 1.00113.04 C ATOM 3743 C GLY D2686 81.585 69.485 31.338 1.00113.02 C ATOM 3744 O GLY D2686 81.366 69.701 32.531 1.00112.96 O ATOM 3745 N LYS D2687 80.679 68.950 30.527 1.00112.45 N ATOM 3746 CA LYS D2687 79.352 68.593 31.014 1.00111.96 C ATOM 3747 C LYS D2687 79.394 67.797 32.319 1.00109.37 C ATOM 3748 O LYS D2687 80.464 67.409 32.795 1.00108.47 O ATOM 3749 CB LYS D2687 78.575 67.822 29.940 1.00114.44 C ATOM 3750 CG LYS D2687 78.176 68.680 28.738 1.00115.45 C ATOM 3751 CD LYS D2687 77.079 68.017 27.917 1.00115.75 C ATOM 3752 CE LYS D2687 76.539 68.957 26.847 1.00115.13 C ATOM 3753 NZ LYS D2687 75.346 68.378 26.161 1.00114.91 N ATOM 3754 N LEU D2688 78.219 67.554 32.887 1.00105.74 N ATOM 3755 CA LEU D2688 78.109 66.848 34.155 1.00103.61 C ATOM 3756 C LEU D2688 77.686 65.397 33.993 1.00101.52 C ATOM 3757 O LEU D2688 77.689 64.631 34.957 1.00 98.19 O ATOM 3758 CB LEU D2688 77.093 67.572 35.034 1.00106.07 C ATOM 3759 CG LEU D2688 77.066 69.093 34.851 1.00107.25 C ATOM 3760 CD1 LEU D2688 75.831 69.679 35.511 1.00108.44 C ATOM 3761 CD2 LEU D2688 78.330 69.695 35.434 1.00109.10 C ATOM 3762 N TYR D2689 77.325 65.024 32.770 1.00102.09 N ATOM 3763 CA TYR D2689 76.875 63.667 32.492 1.00105.35 C ATOM 3764 C TYR D2689 77.869 62.930 31.603 1.00106.11 C ATOM 3765 O TYR D2689 78.011 63.249 30.427 1.00104.20 O ATOM 3766 CB TYR D2689 75.496 63.715 31.825 1.00107.81 C ATOM 3767 CG TYR D2689 74.559 64.728 32.457 1.00109.74 C ATOM 3768 CD1 TYR D2689 74.645 66.085 32.138 1.00109.79 C ATOM 3769 CD2 TYR D2689 73.627 64.339 33.421 1.00110.54 C ATOM 3770 CE1 TYR D2689 73.829 67.029 32.767 1.00109.18 C ATOM 3771 CE2 TYR D2689 72.808 65.275 34.056 1.00109.17 C ATOM 3772 CZ TYR D2689 72.916 66.615 33.725 1.00108.68 C ATOM 3773 OH TYR D2689 72.124 67.536 34.367 1.00108.76 O ATOM 3774 N LEU D2690 78.543 61.933 32.173 1.00109.71 N ATOM 3775 CA LEU D2690 79.548 61.158 31.448 1.00115.01 C ATOM 3776 C LEU D2690 79.051 60.479 30.178 1.00120.90 C ATOM 3777 O LEU D2690 79.851 60.056 29.341 1.00121.33 O ATOM 3778 CB LEU D2690 80.184 60.103 32.370 1.00112.10 C ATOM 3779 CG LEU D2690 79.341 58.997 33.020 1.00108.50 C ATOM 3780 CD1 LEU D2690 78.680 58.125 31.962 1.00105.59 C ATOM 3781 CD2 LEU D2690 80.242 58.153 33.917 1.00104.94 C ATOM 3782 N ASP D2691 77.735 60.368 30.035 1.00127.82 N ATOM 3783 CA ASP D2691 77.155 59.731 28.858 1.00134.10 C ATOM 3784 C ASP D2691 77.828 60.204 27.569 1.00136.17 C ATOM 3785 O ASP D2691 77.646 61.343 27.132 1.00136.39 O ATOM 3786 CB ASP D2691 75.648 60.002 28.798 1.00136.34 C ATOM 3787 CG ASP D2691 74.890 59.341 29.938 1.00137.66 C ATOM 3788 OD1 ASP D2691 74.925 58.093 30.032 1.00136.44 O ATOM 3789 OD2 ASP D2691 74.261 60.071 30.737 1.00138.87 O ATOM 3790 N GLY D2692 78.611 59.314 26.968 1.00137.27 N ATOM 3791 CA GLY D2692 79.310 59.650 25.745 1.00139.36 C ATOM 3792 C GLY D2692 80.809 59.629 25.962 1.00141.72 C ATOM 3793 O GLY D2692 81.557 60.258 25.213 1.00143.07 O ATOM 3794 N SER D2693 81.247 58.904 26.991 1.00142.80 N ATOM 3795 CA SER D2693 82.670 58.796 27.315 1.00142.38 C ATOM 3796 C SER D2693 83.284 57.508 26.766 1.00141.13 C ATOM 3797 O SER D2693 84.211 57.611 25.932 1.00138.97 O ATOM 3798 CB SER D2693 82.876 58.855 28.835 1.00141.63 C ATOM 3799 OG SER D2693 82.247 57.764 29.485 1.00140.90 O TER 3838 HOH C 28 HETATM 3839 O HOH D 2 79.909 71.869 31.060 1.00 47.45 O HETATM 3840 O HOH D 4 90.887 65.157 52.742 1.00 50.05 O HETATM 3841 O HOH D 11 85.406 50.609 44.816 1.00 65.38 O HETATM 3842 O HOH D 12 82.748 54.007 49.741 1.00 72.95 O HETATM 3843 O HOH D 14 89.823 39.267 57.541 1.00 53.69 O HETATM 3844 O HOH D 15 89.385 53.666 41.338 1.00 58.50 O HETATM 3845 O HOH D 19 77.889 49.851 60.133 1.00 52.49 O HETATM 3846 O HOH D 20 67.473 23.152 44.353 1.00 59.94 O HETATM 3847 O HOH D 22 84.851 41.233 48.917 1.00 63.00 O CONECT 1952 1951 1953 2753 CONECT 2753 1952 2752 END