HEADER LIGASE/PROTEIN BINDING 23-SEP-14 4WHV
TITLE E3 UBIQUITIN-PROTEIN LIGASE RNF8 IN COMPLEX WITH UBIQUITIN-CONJUGATING
TITLE 2 ENZYME E2 N AND POLYUBIQUITIN-B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;
COMPND 3 CHAIN: B, E, H, K;
COMPND 4 FRAGMENT: UNP RESIDUES 1-152;
COMPND 5 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME,UBC13,UBCH13,
COMPND 6 UBIQUITIN CARRIER PROTEIN N,UBIQUITIN-PROTEIN LIGASE N;
COMPND 7 EC: 6.3.2.19;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF8;
COMPND 12 CHAIN: C, D, I, J;
COMPND 13 FRAGMENT: UNP RESIDUES 345-485;
COMPND 14 SYNONYM: HRNF8,RING FINGER PROTEIN 8;
COMPND 15 EC: 6.3.2.-;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: POLYUBIQUITIN-B;
COMPND 19 CHAIN: A, F, G, L;
COMPND 20 FRAGMENT: UNP RESIDUES 1-76;
COMPND 21 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: UBE2N, BLU;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RNF8, KIAA0646;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: UBB;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PET47B+
KEYWDS E3 LIGASE, E2 CONJUGATING ENZYME, UBIQUITINATION, COILED COIL,
KEYWDS 2 LIGASE-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.HODGE,R.A.EDWARDS,J.N.M.GLOVER
REVDAT 5 27-SEP-23 4WHV 1 REMARK
REVDAT 4 22-NOV-17 4WHV 1 REMARK
REVDAT 3 11-MAY-16 4WHV 1 TITLE JRNL
REVDAT 2 09-MAR-16 4WHV 1 JRNL
REVDAT 1 30-SEP-15 4WHV 0
JRNL AUTH C.D.HODGE,I.H.ISMAIL,R.A.EDWARDS,G.L.HURA,A.T.XIAO,
JRNL AUTH 2 J.A.TAINER,M.J.HENDZEL,J.N.GLOVER
JRNL TITL RNF8 E3 UBIQUITIN LIGASE STIMULATES UBC13 E2 CONJUGATING
JRNL TITL 2 ACTIVITY THAT IS ESSENTIAL FOR DNA DOUBLE STRAND BREAK
JRNL TITL 3 SIGNALING AND BRCA1 TUMOR SUPPRESSOR RECRUITMENT.
JRNL REF J.BIOL.CHEM. V. 291 9396 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 26903517
JRNL DOI 10.1074/JBC.M116.715698
REMARK 2
REMARK 2 RESOLUTION. 8.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 8.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 4072
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.330
REMARK 3 R VALUE (WORKING SET) : 0.329
REMARK 3 FREE R VALUE : 0.337
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 189
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.2747 - 8.2056 0.99 3883 189 0.3293 0.3374
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.580
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 468.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 522.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 9764
REMARK 3 ANGLE : 1.089 13345
REMARK 3 CHIRALITY : 0.057 1640
REMARK 3 PLANARITY : 0.004 1733
REMARK 3 DIHEDRAL : 12.976 3377
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 4 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.6348-116.0961 0.2947
REMARK 3 T TENSOR
REMARK 3 T11: 5.8592 T22: 6.1400
REMARK 3 T33: 5.7536 T12: 0.3197
REMARK 3 T13: -1.4056 T23: -0.0871
REMARK 3 L TENSOR
REMARK 3 L11: 0.0832 L22: 0.2806
REMARK 3 L33: 0.0054 L12: 0.0448
REMARK 3 L13: -0.0395 L23: -0.0490
REMARK 3 S TENSOR
REMARK 3 S11: -1.7433 S12: -0.3495 S13: -1.0245
REMARK 3 S21: 0.5046 S22: 0.6452 S23: 0.1535
REMARK 3 S31: 0.9220 S32: 2.5514 S33: 0.2712
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 345 THROUGH 480)
REMARK 3 ORIGIN FOR THE GROUP (A): -90.3906-109.3493 1.6418
REMARK 3 T TENSOR
REMARK 3 T11: 5.7974 T22: 4.3496
REMARK 3 T33: 5.1482 T12: -0.2662
REMARK 3 T13: 0.0762 T23: 0.3601
REMARK 3 L TENSOR
REMARK 3 L11: -0.0466 L22: 0.2274
REMARK 3 L33: 1.4391 L12: 0.1198
REMARK 3 L13: -0.0027 L23: 0.6861
REMARK 3 S TENSOR
REMARK 3 S11: 1.2304 S12: -0.4749 S13: -1.4477
REMARK 3 S21: 1.4608 S22: -0.5541 S23: 0.5705
REMARK 3 S31: -1.3437 S32: -0.8917 S33: 0.4562
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 342 THROUGH 480)
REMARK 3 ORIGIN FOR THE GROUP (A): -99.2962-104.8491 -7.9739
REMARK 3 T TENSOR
REMARK 3 T11: 5.4427 T22: 5.8910
REMARK 3 T33: 7.5364 T12: 0.5045
REMARK 3 T13: -0.1450 T23: 0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 1.4811 L22: 1.2880
REMARK 3 L33: 0.5387 L12: -1.4650
REMARK 3 L13: -0.0324 L23: 0.4569
REMARK 3 S TENSOR
REMARK 3 S11: -0.6274 S12: 0.3230 S13: -4.7742
REMARK 3 S21: -0.1718 S22: 0.4576 S23: 1.4985
REMARK 3 S31: 0.1697 S32: -0.4897 S33: -1.9186
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 4 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A):-115.0228 -72.9423 -9.4638
REMARK 3 T TENSOR
REMARK 3 T11: 5.7150 T22: 5.3792
REMARK 3 T33: 7.1025 T12: 0.4943
REMARK 3 T13: -0.1758 T23: 1.1630
REMARK 3 L TENSOR
REMARK 3 L11: 0.6958 L22: 0.1466
REMARK 3 L33: 0.0408 L12: -0.2780
REMARK 3 L13: -0.2369 L23: 0.0343
REMARK 3 S TENSOR
REMARK 3 S11: 0.2408 S12: 0.6909 S13: -0.0274
REMARK 3 S21: 1.6138 S22: 0.1172 S23: -0.5093
REMARK 3 S31: -0.2063 S32: -0.2150 S33: 2.8275
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 4 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A): -62.5250 -73.1881 31.5667
REMARK 3 T TENSOR
REMARK 3 T11: 6.6795 T22: 6.8424
REMARK 3 T33: 5.3549 T12: 0.0196
REMARK 3 T13: -0.5920 T23: 0.4653
REMARK 3 L TENSOR
REMARK 3 L11: 0.0258 L22: 0.1964
REMARK 3 L33: 0.8359 L12: -0.0296
REMARK 3 L13: -0.0394 L23: 0.4054
REMARK 3 S TENSOR
REMARK 3 S11: 0.8326 S12: -1.4725 S13: -0.2779
REMARK 3 S21: 0.8728 S22: -0.4791 S23: 0.3103
REMARK 3 S31: -0.3282 S32: 0.2210 S33: 1.1470
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'I' AND RESID 380 THROUGH 480)
REMARK 3 ORIGIN FOR THE GROUP (A): -59.1374 -70.8919 1.0045
REMARK 3 T TENSOR
REMARK 3 T11: 5.1759 T22: 6.1314
REMARK 3 T33: 4.7387 T12: 0.9532
REMARK 3 T13: 0.5342 T23: -1.0489
REMARK 3 L TENSOR
REMARK 3 L11: 0.5465 L22: 1.2764
REMARK 3 L33: 1.2715 L12: -0.8362
REMARK 3 L13: 0.6401 L23: -0.9550
REMARK 3 S TENSOR
REMARK 3 S11: -0.6600 S12: -0.5532 S13: -0.6091
REMARK 3 S21: -0.0551 S22: -0.6709 S23: -2.4614
REMARK 3 S31: -0.5907 S32: 0.6320 S33: -0.4312
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'J' AND RESID 380 THROUGH 480)
REMARK 3 ORIGIN FOR THE GROUP (A): -71.3089 -63.0116 -10.9716
REMARK 3 T TENSOR
REMARK 3 T11: 5.4012 T22: 5.1416
REMARK 3 T33: 5.3009 T12: 0.9267
REMARK 3 T13: 1.5444 T23: 0.2063
REMARK 3 L TENSOR
REMARK 3 L11: 0.3258 L22: 0.4206
REMARK 3 L33: 0.9658 L12: -0.3634
REMARK 3 L13: 0.3844 L23: -0.4178
REMARK 3 S TENSOR
REMARK 3 S11: -0.1378 S12: -0.4336 S13: 0.6990
REMARK 3 S21: -0.3076 S22: -0.2801 S23: 0.3944
REMARK 3 S31: -0.0959 S32: -1.0325 S33: 0.4657
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'K' AND RESID 4 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A): -71.5807 -66.3725 -42.2015
REMARK 3 T TENSOR
REMARK 3 T11: 7.0614 T22: 5.4310
REMARK 3 T33: 5.7511 T12: 0.1107
REMARK 3 T13: -0.7167 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 0.2622 L22: 0.1560
REMARK 3 L33: 0.2408 L12: -0.2141
REMARK 3 L13: 0.2447 L23: -0.1773
REMARK 3 S TENSOR
REMARK 3 S11: 0.6618 S12: -0.0875 S13: -0.2368
REMARK 3 S21: -0.3948 S22: -0.6739 S23: -0.1980
REMARK 3 S31: -0.7362 S32: -0.3072 S33: -0.4257
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 71)
REMARK 3 ORIGIN FOR THE GROUP (A): -69.1139-110.6676 -19.3505
REMARK 3 T TENSOR
REMARK 3 T11: 7.3310 T22: 5.5186
REMARK 3 T33: 7.0914 T12: 0.7852
REMARK 3 T13: 0.1323 T23: 0.1186
REMARK 3 L TENSOR
REMARK 3 L11: -0.0024 L22: 0.0069
REMARK 3 L33: 0.0087 L12: -0.0139
REMARK 3 L13: -0.0098 L23: -0.0051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0832 S12: 0.5960 S13: -0.1094
REMARK 3 S21: 0.0129 S22: 0.1142 S23: 0.0432
REMARK 3 S31: -0.0559 S32: 0.6498 S33: -0.1237
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 71)
REMARK 3 ORIGIN FOR THE GROUP (A):-104.4062 -83.0631 8.8897
REMARK 3 T TENSOR
REMARK 3 T11: 6.5257 T22: 6.0166
REMARK 3 T33: 5.9082 T12: 0.0939
REMARK 3 T13: 0.7955 T23: -0.8385
REMARK 3 L TENSOR
REMARK 3 L11: 0.0584 L22: 0.0080
REMARK 3 L33: 0.0084 L12: 0.0363
REMARK 3 L13: 0.0241 L23: 0.0245
REMARK 3 S TENSOR
REMARK 3 S11: -0.6557 S12: -0.2605 S13: 0.4425
REMARK 3 S21: 0.6171 S22: -0.0196 S23: -0.2317
REMARK 3 S31: -0.6515 S32: 0.2918 S33: -0.3997
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 1 THROUGH 71)
REMARK 3 ORIGIN FOR THE GROUP (A): -77.9775 -59.0264 17.6071
REMARK 3 T TENSOR
REMARK 3 T11: 7.2864 T22: 5.9258
REMARK 3 T33: 5.8237 T12: 0.2900
REMARK 3 T13: -0.4699 T23: -0.9449
REMARK 3 L TENSOR
REMARK 3 L11: 0.2365 L22: 0.0796
REMARK 3 L33: 0.0136 L12: -0.0565
REMARK 3 L13: -0.0041 L23: 0.0514
REMARK 3 S TENSOR
REMARK 3 S11: 0.3522 S12: -0.5761 S13: -0.0566
REMARK 3 S21: -0.0072 S22: 0.2481 S23: -0.0716
REMARK 3 S31: -0.1674 S32: -0.7038 S33: 0.4946
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 71)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.2023 -75.5734 -28.2982
REMARK 3 T TENSOR
REMARK 3 T11: 6.6847 T22: 6.9134
REMARK 3 T33: 7.2149 T12: 0.6900
REMARK 3 T13: 1.1679 T23: -0.1215
REMARK 3 L TENSOR
REMARK 3 L11: 0.0702 L22: 0.0611
REMARK 3 L33: 0.0917 L12: 0.0429
REMARK 3 L13: -0.0940 L23: -0.0811
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: 0.1793 S13: -0.1948
REMARK 3 S21: -0.4431 S22: 0.2625 S23: 0.0821
REMARK 3 S31: -0.0184 S32: 0.1796 S33: 1.5121
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WHV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03321
REMARK 200 MONOCHROMATOR : UNK
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4094
REMARK 200 RESOLUTION RANGE HIGH (A) : 8.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.80
REMARK 200 R MERGE (I) : 0.19100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 8.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 24.20
REMARK 200 R MERGE FOR SHELL (I) : 0.90100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4ORH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.04 M (NH4)2HPO4, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 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 37.81567
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 75.63133
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.81567
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 75.63133
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 37.81567
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 75.63133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.81567
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 75.63133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER SET (2RNF8 PROTOMERS, 2UBC13~
REMARK 300 UB). THERE ARE 2 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS A,
REMARK 300 B, C, D, E, F AND CHAINS G, H, I, J, K, L
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, E, A, F
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J, K, G, L
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 GLY B -7
REMARK 465 PRO B -6
REMARK 465 LEU B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 PRO B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 ASN B 151
REMARK 465 ILE B 152
REMARK 465 GLY C 337
REMARK 465 PRO C 338
REMARK 465 LEU C 339
REMARK 465 GLY C 340
REMARK 465 SER C 341
REMARK 465 PRO C 342
REMARK 465 GLU C 343
REMARK 465 PHE C 344
REMARK 465 ALA C 481
REMARK 465 LYS C 482
REMARK 465 ARG C 483
REMARK 465 LEU C 484
REMARK 465 PHE C 485
REMARK 465 GLY D 337
REMARK 465 PRO D 338
REMARK 465 LEU D 339
REMARK 465 GLY D 340
REMARK 465 SER D 341
REMARK 465 ALA D 481
REMARK 465 LYS D 482
REMARK 465 ARG D 483
REMARK 465 LEU D 484
REMARK 465 PHE D 485
REMARK 465 GLY E -7
REMARK 465 PRO E -6
REMARK 465 LEU E -5
REMARK 465 GLY E -4
REMARK 465 SER E -3
REMARK 465 PRO E -2
REMARK 465 GLU E -1
REMARK 465 PHE E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLY E 3
REMARK 465 ASN E 151
REMARK 465 ILE E 152
REMARK 465 GLY H -7
REMARK 465 PRO H -6
REMARK 465 LEU H -5
REMARK 465 GLY H -4
REMARK 465 SER H -3
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PHE H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLY H 3
REMARK 465 ASN H 151
REMARK 465 ILE H 152
REMARK 465 GLY I 337
REMARK 465 PRO I 338
REMARK 465 LEU I 339
REMARK 465 GLY I 340
REMARK 465 SER I 341
REMARK 465 PRO I 342
REMARK 465 GLU I 343
REMARK 465 PHE I 344
REMARK 465 GLN I 345
REMARK 465 GLU I 346
REMARK 465 HIS I 347
REMARK 465 TRP I 348
REMARK 465 ALA I 349
REMARK 465 LEU I 350
REMARK 465 MET I 351
REMARK 465 GLU I 352
REMARK 465 GLU I 353
REMARK 465 LEU I 354
REMARK 465 ASN I 355
REMARK 465 ARG I 356
REMARK 465 SER I 357
REMARK 465 LYS I 358
REMARK 465 LYS I 359
REMARK 465 ASP I 360
REMARK 465 PHE I 361
REMARK 465 GLU I 362
REMARK 465 ALA I 363
REMARK 465 ILE I 364
REMARK 465 ILE I 365
REMARK 465 GLN I 366
REMARK 465 ALA I 367
REMARK 465 LYS I 368
REMARK 465 ASN I 369
REMARK 465 LYS I 370
REMARK 465 GLU I 371
REMARK 465 LEU I 372
REMARK 465 GLU I 373
REMARK 465 GLN I 374
REMARK 465 THR I 375
REMARK 465 LYS I 376
REMARK 465 GLU I 377
REMARK 465 GLU I 378
REMARK 465 LYS I 379
REMARK 465 ALA I 481
REMARK 465 LYS I 482
REMARK 465 ARG I 483
REMARK 465 LEU I 484
REMARK 465 PHE I 485
REMARK 465 GLY J 337
REMARK 465 PRO J 338
REMARK 465 LEU J 339
REMARK 465 GLY J 340
REMARK 465 SER J 341
REMARK 465 PRO J 342
REMARK 465 GLU J 343
REMARK 465 PHE J 344
REMARK 465 GLN J 345
REMARK 465 GLU J 346
REMARK 465 HIS J 347
REMARK 465 TRP J 348
REMARK 465 ALA J 349
REMARK 465 LEU J 350
REMARK 465 MET J 351
REMARK 465 GLU J 352
REMARK 465 GLU J 353
REMARK 465 LEU J 354
REMARK 465 ASN J 355
REMARK 465 ARG J 356
REMARK 465 SER J 357
REMARK 465 LYS J 358
REMARK 465 LYS J 359
REMARK 465 ASP J 360
REMARK 465 PHE J 361
REMARK 465 GLU J 362
REMARK 465 ALA J 363
REMARK 465 ILE J 364
REMARK 465 ILE J 365
REMARK 465 GLN J 366
REMARK 465 ALA J 367
REMARK 465 LYS J 368
REMARK 465 ASN J 369
REMARK 465 LYS J 370
REMARK 465 GLU J 371
REMARK 465 LEU J 372
REMARK 465 GLU J 373
REMARK 465 GLN J 374
REMARK 465 THR J 375
REMARK 465 LYS J 376
REMARK 465 GLU J 377
REMARK 465 GLU J 378
REMARK 465 LYS J 379
REMARK 465 ALA J 481
REMARK 465 LYS J 482
REMARK 465 ARG J 483
REMARK 465 LEU J 484
REMARK 465 PHE J 485
REMARK 465 GLY K -7
REMARK 465 PRO K -6
REMARK 465 LEU K -5
REMARK 465 GLY K -4
REMARK 465 SER K -3
REMARK 465 PRO K -2
REMARK 465 GLU K -1
REMARK 465 PHE K 0
REMARK 465 MET K 1
REMARK 465 ALA K 2
REMARK 465 GLY K 3
REMARK 465 ASN K 151
REMARK 465 ILE K 152
REMARK 465 GLY A -6
REMARK 465 PRO A -5
REMARK 465 GLY A -4
REMARK 465 TYR A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 ARG A 72
REMARK 465 LEU A 73
REMARK 465 ARG A 74
REMARK 465 GLY A 75
REMARK 465 GLY A 76
REMARK 465 GLY F -6
REMARK 465 PRO F -5
REMARK 465 GLY F -4
REMARK 465 TYR F -3
REMARK 465 GLN F -2
REMARK 465 ASP F -1
REMARK 465 PRO F 0
REMARK 465 ARG F 72
REMARK 465 LEU F 73
REMARK 465 ARG F 74
REMARK 465 GLY F 75
REMARK 465 GLY F 76
REMARK 465 GLY G -6
REMARK 465 PRO G -5
REMARK 465 GLY G -4
REMARK 465 TYR G -3
REMARK 465 GLN G -2
REMARK 465 ASP G -1
REMARK 465 PRO G 0
REMARK 465 ARG G 72
REMARK 465 LEU G 73
REMARK 465 ARG G 74
REMARK 465 GLY G 75
REMARK 465 GLY G 76
REMARK 465 GLY L -6
REMARK 465 PRO L -5
REMARK 465 GLY L -4
REMARK 465 TYR L -3
REMARK 465 GLN L -2
REMARK 465 ASP L -1
REMARK 465 PRO L 0
REMARK 465 ARG L 72
REMARK 465 LEU L 73
REMARK 465 ARG L 74
REMARK 465 GLY L 75
REMARK 465 GLY L 76
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 ARG B 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 10 CG CD CE NZ
REMARK 470 PHE B 57 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 64 CG SD CE
REMARK 470 ARG B 70 CG CD NE CZ NH1 NH2
REMARK 470 SER B 96 OG
REMARK 470 PRO B 97 CG CD
REMARK 470 LEU B 99 CG CD1 CD2
REMARK 470 GLN B 100 CG CD OE1 NE2
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 470 ARG B 145 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 146 CG CD1 CD2
REMARK 470 GLN C 345 CG CD OE1 NE2
REMARK 470 GLU C 346 CG CD OE1 OE2
REMARK 470 HIS C 347 CG ND1 CD2 CE1 NE2
REMARK 470 TRP C 348 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 348 CZ3 CH2
REMARK 470 LEU C 350 CG CD1 CD2
REMARK 470 MET C 351 CG SD CE
REMARK 470 GLU C 352 CG CD OE1 OE2
REMARK 470 GLU C 353 CG CD OE1 OE2
REMARK 470 LEU C 354 CG CD1 CD2
REMARK 470 ASN C 355 CG OD1 ND2
REMARK 470 ARG C 356 CG CD NE CZ NH1 NH2
REMARK 470 SER C 357 OG
REMARK 470 LYS C 358 CG CD CE NZ
REMARK 470 LYS C 359 CG CD CE NZ
REMARK 470 ASP C 360 CG OD1 OD2
REMARK 470 PHE C 361 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 362 CG CD OE1 OE2
REMARK 470 ILE C 364 CG1 CG2 CD1
REMARK 470 ILE C 365 CG1 CG2 CD1
REMARK 470 GLN C 366 CG CD OE1 NE2
REMARK 470 LYS C 368 CG CD CE NZ
REMARK 470 ASN C 369 CG OD1 ND2
REMARK 470 LYS C 370 CG CD CE NZ
REMARK 470 GLU C 371 CG CD OE1 OE2
REMARK 470 LEU C 372 CG CD1 CD2
REMARK 470 GLU C 373 CG CD OE1 OE2
REMARK 470 GLN C 374 CG CD OE1 NE2
REMARK 470 THR C 375 OG1 CG2
REMARK 470 LYS C 376 CG CD CE NZ
REMARK 470 GLU C 377 CG CD OE1 OE2
REMARK 470 GLU C 378 CG CD OE1 OE2
REMARK 470 LYS C 379 CG CD CE NZ
REMARK 470 GLU C 380 CG CD OE1 OE2
REMARK 470 LYS C 381 CG CD CE NZ
REMARK 470 MET C 382 CG SD CE
REMARK 470 GLN C 383 CG CD OE1 NE2
REMARK 470 GLN C 385 CG CD OE1 NE2
REMARK 470 LYS C 386 CG CD CE NZ
REMARK 470 GLU C 387 CG CD OE1 OE2
REMARK 470 GLU C 388 CG CD OE1 OE2
REMARK 470 VAL C 389 CG1 CG2
REMARK 470 LEU C 390 CG CD1 CD2
REMARK 470 SER C 391 OG
REMARK 470 HIS C 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET C 393 CG SD CE
REMARK 470 ASN C 394 CG OD1 ND2
REMARK 470 ASP C 395 CG OD1 OD2
REMARK 470 VAL C 396 CG1 CG2
REMARK 470 LEU C 397 CG CD1 CD2
REMARK 470 ILE C 404 CG1 CG2 CD1
REMARK 470 TRP C 430 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 430 CZ3 CH2
REMARK 470 LYS C 432 CG CD CE NZ
REMARK 470 ARG C 433 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 442 CG CD CE NZ
REMARK 470 SER C 446 OG
REMARK 470 LYS C 480 CG CD CE NZ
REMARK 470 PRO D 342 CG CD
REMARK 470 GLU D 343 CB CG CD OE1 OE2
REMARK 470 PHE D 344 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN D 345 CG CD OE1 NE2
REMARK 470 GLU D 346 CG CD OE1 OE2
REMARK 470 HIS D 347 CG ND1 CD2 CE1 NE2
REMARK 470 TRP D 348 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 348 CZ3 CH2
REMARK 470 LEU D 350 CG CD1 CD2
REMARK 470 MET D 351 CG SD CE
REMARK 470 GLU D 352 CG CD OE1 OE2
REMARK 470 GLU D 353 CG CD OE1 OE2
REMARK 470 LEU D 354 CG CD1 CD2
REMARK 470 ASN D 355 CG OD1 ND2
REMARK 470 ARG D 356 CG CD NE CZ NH1 NH2
REMARK 470 SER D 357 OG
REMARK 470 LYS D 358 CG CD CE NZ
REMARK 470 LYS D 359 CG CD CE NZ
REMARK 470 ASP D 360 CG OD1 OD2
REMARK 470 PHE D 361 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 362 CG CD OE1 OE2
REMARK 470 ILE D 364 CG1 CG2 CD1
REMARK 470 ILE D 365 CG1 CG2 CD1
REMARK 470 GLN D 366 CG CD OE1 NE2
REMARK 470 LYS D 368 CG CD CE NZ
REMARK 470 ASN D 369 CG OD1 ND2
REMARK 470 LYS D 370 CG CD CE NZ
REMARK 470 GLU D 371 CG CD OE1 OE2
REMARK 470 LEU D 372 CG CD1 CD2
REMARK 470 GLU D 373 CG CD OE1 OE2
REMARK 470 GLN D 374 CG CD OE1 NE2
REMARK 470 THR D 375 OG1 CG2
REMARK 470 LYS D 376 CG CD CE NZ
REMARK 470 GLU D 377 CG CD OE1 OE2
REMARK 470 GLU D 378 CG CD OE1 OE2
REMARK 470 LYS D 379 CG CD CE NZ
REMARK 470 GLU D 380 CG CD OE1 OE2
REMARK 470 LYS D 381 CG CD CE NZ
REMARK 470 MET D 382 CG SD CE
REMARK 470 GLN D 383 CG CD OE1 NE2
REMARK 470 GLN D 385 CG CD OE1 NE2
REMARK 470 LYS D 386 CG CD CE NZ
REMARK 470 GLU D 387 CG CD OE1 OE2
REMARK 470 GLU D 388 CG CD OE1 OE2
REMARK 470 VAL D 389 CG1 CG2
REMARK 470 LEU D 390 CG CD1 CD2
REMARK 470 SER D 391 OG
REMARK 470 HIS D 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET D 393 CG SD CE
REMARK 470 ASN D 394 CG OD1 ND2
REMARK 470 ASP D 395 CG OD1 OD2
REMARK 470 VAL D 396 CG1 CG2
REMARK 470 LEU D 397 CG CD1 CD2
REMARK 470 ILE D 404 CG1 CG2 CD1
REMARK 470 TRP D 430 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 430 CZ3 CH2
REMARK 470 LYS D 432 CG CD CE NZ
REMARK 470 ARG D 433 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 442 CG CD CE NZ
REMARK 470 SER D 446 OG
REMARK 470 LYS D 480 CG CD CE NZ
REMARK 470 ARG E 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 10 CG CD CE NZ
REMARK 470 PHE E 57 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET E 64 CG SD CE
REMARK 470 ARG E 70 CG CD NE CZ NH1 NH2
REMARK 470 SER E 96 OG
REMARK 470 PRO E 97 CG CD
REMARK 470 LEU E 99 CG CD1 CD2
REMARK 470 GLN E 100 CG CD OE1 NE2
REMARK 470 GLU E 138 CG CD OE1 OE2
REMARK 470 ARG E 145 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 146 CG CD1 CD2
REMARK 470 ARG H 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 10 CG CD CE NZ
REMARK 470 PHE H 57 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET H 64 CG SD CE
REMARK 470 ARG H 70 CG CD NE CZ NH1 NH2
REMARK 470 SER H 96 OG
REMARK 470 PRO H 97 CG CD
REMARK 470 LEU H 99 CG CD1 CD2
REMARK 470 GLN H 100 CG CD OE1 NE2
REMARK 470 GLU H 138 CG CD OE1 OE2
REMARK 470 ARG H 145 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 146 CG CD1 CD2
REMARK 470 GLU I 380 CG CD OE1 OE2
REMARK 470 LYS I 381 CG CD CE NZ
REMARK 470 MET I 382 CG SD CE
REMARK 470 GLN I 383 CG CD OE1 NE2
REMARK 470 GLN I 385 CG CD OE1 NE2
REMARK 470 LYS I 386 CG CD CE NZ
REMARK 470 GLU I 387 CG CD OE1 OE2
REMARK 470 GLU I 388 CG CD OE1 OE2
REMARK 470 VAL I 389 CG1 CG2
REMARK 470 LEU I 390 CG CD1 CD2
REMARK 470 SER I 391 OG
REMARK 470 HIS I 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET I 393 CG SD CE
REMARK 470 ASN I 394 CG OD1 ND2
REMARK 470 ASP I 395 CG OD1 OD2
REMARK 470 VAL I 396 CG1 CG2
REMARK 470 LEU I 397 CG CD1 CD2
REMARK 470 ILE I 404 CG1 CG2 CD1
REMARK 470 TRP I 430 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP I 430 CZ3 CH2
REMARK 470 LYS I 432 CG CD CE NZ
REMARK 470 ARG I 433 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 442 CG CD CE NZ
REMARK 470 SER I 446 OG
REMARK 470 LYS I 480 CG CD CE NZ
REMARK 470 GLU J 380 CG CD OE1 OE2
REMARK 470 LYS J 381 CG CD CE NZ
REMARK 470 MET J 382 CG SD CE
REMARK 470 GLN J 383 CG CD OE1 NE2
REMARK 470 GLN J 385 CG CD OE1 NE2
REMARK 470 LYS J 386 CG CD CE NZ
REMARK 470 GLU J 387 CG CD OE1 OE2
REMARK 470 GLU J 388 CG CD OE1 OE2
REMARK 470 VAL J 389 CG1 CG2
REMARK 470 LEU J 390 CG CD1 CD2
REMARK 470 SER J 391 OG
REMARK 470 HIS J 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET J 393 CG SD CE
REMARK 470 ASN J 394 CG OD1 ND2
REMARK 470 ASP J 395 CG OD1 OD2
REMARK 470 VAL J 396 CG1 CG2
REMARK 470 LEU J 397 CG CD1 CD2
REMARK 470 ILE J 404 CG1 CG2 CD1
REMARK 470 TRP J 430 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP J 430 CZ3 CH2
REMARK 470 LYS J 432 CG CD CE NZ
REMARK 470 ARG J 433 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 442 CG CD CE NZ
REMARK 470 SER J 446 OG
REMARK 470 LYS J 480 CG CD CE NZ
REMARK 470 ARG K 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG K 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 10 CG CD CE NZ
REMARK 470 PHE K 57 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET K 64 CG SD CE
REMARK 470 ARG K 70 CG CD NE CZ NH1 NH2
REMARK 470 SER K 96 OG
REMARK 470 PRO K 97 CG CD
REMARK 470 LEU K 99 CG CD1 CD2
REMARK 470 GLN K 100 CG CD OE1 NE2
REMARK 470 GLU K 138 CG CD OE1 OE2
REMARK 470 ARG K 145 CG CD NE CZ NH1 NH2
REMARK 470 LEU K 146 CG CD1 CD2
REMARK 470 GLN A 2 CG CD OE1 NE2
REMARK 470 PHE A 4 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 6 CG CD CE NZ
REMARK 470 THR A 9 OG1 CG2
REMARK 470 LYS A 11 CG CD CE NZ
REMARK 470 THR A 12 OG1 CG2
REMARK 470 GLU A 16 CG CD OE1 OE2
REMARK 470 GLU A 18 CG CD OE1 OE2
REMARK 470 SER A 20 OG
REMARK 470 ASP A 21 CG OD1 OD2
REMARK 470 THR A 22 OG1 CG2
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 ASN A 25 CG OD1 ND2
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 ASP A 32 CG OD1 OD2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 ASP A 39 CG OD1 OD2
REMARK 470 GLN A 40 CG CD OE1 NE2
REMARK 470 ARG A 42 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 GLN A 49 CG CD OE1 NE2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 ASP A 52 CG OD1 OD2
REMARK 470 ARG A 54 CG CD NE CZ NH1 NH2
REMARK 470 SER A 57 OG
REMARK 470 ASP A 58 CG OD1 OD2
REMARK 470 ASN A 60 CG OD1 ND2
REMARK 470 GLN A 62 CG CD OE1 NE2
REMARK 470 LYS A 63 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 HIS A 68 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 71 CG CD1 CD2
REMARK 470 GLN F 2 CG CD OE1 NE2
REMARK 470 PHE F 4 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS F 6 CG CD CE NZ
REMARK 470 THR F 9 OG1 CG2
REMARK 470 LYS F 11 CG CD CE NZ
REMARK 470 THR F 12 OG1 CG2
REMARK 470 GLU F 16 CG CD OE1 OE2
REMARK 470 GLU F 18 CG CD OE1 OE2
REMARK 470 SER F 20 OG
REMARK 470 ASP F 21 CG OD1 OD2
REMARK 470 THR F 22 OG1 CG2
REMARK 470 GLU F 24 CG CD OE1 OE2
REMARK 470 ASN F 25 CG OD1 ND2
REMARK 470 LYS F 29 CG CD CE NZ
REMARK 470 ASP F 32 CG OD1 OD2
REMARK 470 LYS F 33 CG CD CE NZ
REMARK 470 ASP F 39 CG OD1 OD2
REMARK 470 GLN F 40 CG CD OE1 NE2
REMARK 470 ARG F 42 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 GLN F 49 CG CD OE1 NE2
REMARK 470 GLU F 51 CG CD OE1 OE2
REMARK 470 ASP F 52 CG OD1 OD2
REMARK 470 ARG F 54 CG CD NE CZ NH1 NH2
REMARK 470 SER F 57 OG
REMARK 470 ASP F 58 CG OD1 OD2
REMARK 470 ASN F 60 CG OD1 ND2
REMARK 470 GLN F 62 CG CD OE1 NE2
REMARK 470 LYS F 63 CG CD CE NZ
REMARK 470 GLU F 64 CG CD OE1 OE2
REMARK 470 HIS F 68 CG ND1 CD2 CE1 NE2
REMARK 470 LEU F 71 CG CD1 CD2
REMARK 470 GLN G 2 CG CD OE1 NE2
REMARK 470 PHE G 4 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS G 6 CG CD CE NZ
REMARK 470 THR G 9 OG1 CG2
REMARK 470 LYS G 11 CG CD CE NZ
REMARK 470 THR G 12 OG1 CG2
REMARK 470 GLU G 16 CG CD OE1 OE2
REMARK 470 GLU G 18 CG CD OE1 OE2
REMARK 470 SER G 20 OG
REMARK 470 ASP G 21 CG OD1 OD2
REMARK 470 THR G 22 OG1 CG2
REMARK 470 GLU G 24 CG CD OE1 OE2
REMARK 470 ASN G 25 CG OD1 ND2
REMARK 470 LYS G 29 CG CD CE NZ
REMARK 470 ASP G 32 CG OD1 OD2
REMARK 470 LYS G 33 CG CD CE NZ
REMARK 470 ASP G 39 CG OD1 OD2
REMARK 470 GLN G 40 CG CD OE1 NE2
REMARK 470 ARG G 42 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 48 CG CD CE NZ
REMARK 470 GLN G 49 CG CD OE1 NE2
REMARK 470 GLU G 51 CG CD OE1 OE2
REMARK 470 ASP G 52 CG OD1 OD2
REMARK 470 ARG G 54 CG CD NE CZ NH1 NH2
REMARK 470 SER G 57 OG
REMARK 470 ASP G 58 CG OD1 OD2
REMARK 470 ASN G 60 CG OD1 ND2
REMARK 470 GLN G 62 CG CD OE1 NE2
REMARK 470 LYS G 63 CG CD CE NZ
REMARK 470 GLU G 64 CG CD OE1 OE2
REMARK 470 HIS G 68 CG ND1 CD2 CE1 NE2
REMARK 470 LEU G 71 CG CD1 CD2
REMARK 470 GLN L 2 CG CD OE1 NE2
REMARK 470 PHE L 4 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS L 6 CG CD CE NZ
REMARK 470 THR L 9 OG1 CG2
REMARK 470 LYS L 11 CG CD CE NZ
REMARK 470 THR L 12 OG1 CG2
REMARK 470 GLU L 16 CG CD OE1 OE2
REMARK 470 GLU L 18 CG CD OE1 OE2
REMARK 470 SER L 20 OG
REMARK 470 ASP L 21 CG OD1 OD2
REMARK 470 THR L 22 OG1 CG2
REMARK 470 GLU L 24 CG CD OE1 OE2
REMARK 470 ASN L 25 CG OD1 ND2
REMARK 470 LYS L 29 CG CD CE NZ
REMARK 470 ASP L 32 CG OD1 OD2
REMARK 470 LYS L 33 CG CD CE NZ
REMARK 470 ASP L 39 CG OD1 OD2
REMARK 470 GLN L 40 CG CD OE1 NE2
REMARK 470 ARG L 42 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 48 CG CD CE NZ
REMARK 470 GLN L 49 CG CD OE1 NE2
REMARK 470 GLU L 51 CG CD OE1 OE2
REMARK 470 ASP L 52 CG OD1 OD2
REMARK 470 ARG L 54 CG CD NE CZ NH1 NH2
REMARK 470 SER L 57 OG
REMARK 470 ASP L 58 CG OD1 OD2
REMARK 470 ASN L 60 CG OD1 ND2
REMARK 470 GLN L 62 CG CD OE1 NE2
REMARK 470 LYS L 63 CG CD CE NZ
REMARK 470 GLU L 64 CG CD OE1 OE2
REMARK 470 HIS L 68 CG ND1 CD2 CE1 NE2
REMARK 470 LEU L 71 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG D 441 CB SER E 96 1.64
REMARK 500 O LEU H 99 OG1 THR H 103 1.91
REMARK 500 O LEU B 99 OG1 THR B 103 1.91
REMARK 500 O LEU E 99 OG1 THR E 103 1.91
REMARK 500 O LEU K 99 OG1 THR K 103 1.91
REMARK 500 OE2 GLU D 408 CB ARG E 6 2.01
REMARK 500 O ALA K 98 CA THR L 9 2.03
REMARK 500 O LEU D 397 OH TYR D 409 2.05
REMARK 500 O LEU J 397 OH TYR J 409 2.05
REMARK 500 O GLU I 400 N GLN I 402 2.07
REMARK 500 O GLU C 400 N GLN C 402 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N LEU H 4 O SER H 30 7555 1.16
REMARK 500 CA ASP L 58 CA ASP L 58 7554 1.24
REMARK 500 CD2 TYR E 34 NZ LYS E 74 12554 1.31
REMARK 500 N LEU H 4 C SER H 30 7555 1.54
REMARK 500 O SER L 57 O SER L 57 7554 1.55
REMARK 500 OD2 ASP E 28 OH TYR E 147 12554 1.67
REMARK 500 CE2 TYR E 34 CD LYS E 74 12554 1.67
REMARK 500 CB ASP L 58 CB ASP L 58 7554 1.69
REMARK 500 O SER B 30 CB ALA B 32 7555 1.70
REMARK 500 CG GLU B 127 CG GLU H 127 7555 1.88
REMARK 500 CD ARG E 85 CD ARG E 85 12554 1.94
REMARK 500 N ASP L 58 O ASP L 58 7554 2.05
REMARK 500 CD2 LEU B 4 CB SER B 30 7555 2.08
REMARK 500 CA ASP L 58 CB ASP L 58 7554 2.10
REMARK 500 CE2 TYR E 34 NZ LYS E 74 12554 2.14
REMARK 500 CG ASP E 28 OH TYR E 147 12554 2.15
REMARK 500 CE2 TYR E 34 CE LYS E 74 12554 2.15
REMARK 500 CG TYR E 34 NZ LYS E 74 12554 2.16
REMARK 500 CA ASP L 58 C ASP L 58 7554 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 LYS B 92 -72.89 -145.49
REMARK 500 LYS B 94 40.43 -94.35
REMARK 500 PRO B 97 -7.23 -55.74
REMARK 500 GLN B 100 172.08 79.17
REMARK 500 ASN B 116 78.57 -119.15
REMARK 500 LEU B 121 36.66 -92.51
REMARK 500 ASN B 123 -100.22 -48.63
REMARK 500 ASP B 124 -25.40 177.91
REMARK 500 GLU C 400 -106.70 -84.53
REMARK 500 LEU C 401 41.47 -50.57
REMARK 500 ALA C 419 3.70 85.53
REMARK 500 ILE C 435 57.58 -98.45
REMARK 500 GLU D 398 -33.32 -179.33
REMARK 500 ALA D 419 1.87 83.69
REMARK 500 LYS E 92 -72.97 -145.55
REMARK 500 LYS E 94 40.53 -94.39
REMARK 500 PRO E 97 -7.42 -55.67
REMARK 500 GLN E 100 172.04 79.22
REMARK 500 ASN E 116 78.71 -119.12
REMARK 500 LEU E 121 36.79 -92.65
REMARK 500 ASN E 123 -100.27 -48.59
REMARK 500 ASP E 124 -25.40 177.87
REMARK 500 LYS H 92 -72.98 -145.51
REMARK 500 LYS H 94 40.62 -94.41
REMARK 500 PRO H 97 -7.30 -55.67
REMARK 500 GLN H 100 172.01 79.17
REMARK 500 ASN H 116 78.72 -119.09
REMARK 500 LEU H 121 36.74 -92.59
REMARK 500 ASN H 123 -100.27 -48.69
REMARK 500 ASP H 124 -25.40 177.94
REMARK 500 GLU I 400 -106.92 -84.45
REMARK 500 LEU I 401 41.36 -50.48
REMARK 500 ALA I 419 3.80 85.41
REMARK 500 ILE I 435 57.64 -98.50
REMARK 500 GLU J 398 -33.32 -179.33
REMARK 500 ALA J 419 1.89 83.66
REMARK 500 LYS K 92 -73.02 -145.50
REMARK 500 LYS K 94 40.44 -94.30
REMARK 500 PRO K 97 -7.38 -55.70
REMARK 500 GLN K 100 172.07 79.19
REMARK 500 ASN K 116 78.80 -119.07
REMARK 500 LEU K 121 36.79 -92.64
REMARK 500 ASN K 123 -100.30 -48.59
REMARK 500 ASP K 124 -25.40 177.88
REMARK 500 LYS A 63 111.79 -28.20
REMARK 500 LYS F 63 111.81 -28.20
REMARK 500 LYS G 63 111.88 -28.31
REMARK 500 LYS L 63 111.87 -28.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 403 SG
REMARK 620 2 CYS C 406 SG 112.1
REMARK 620 3 CYS C 423 SG 103.6 101.9
REMARK 620 4 CYS C 426 SG 117.8 108.6 111.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 418 SG
REMARK 620 2 HIS C 420 ND1 114.6
REMARK 620 3 CYS C 437 SG 105.8 104.0
REMARK 620 4 CYS C 440 SG 108.8 113.8 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 403 SG
REMARK 620 2 CYS D 406 SG 110.6
REMARK 620 3 CYS D 423 SG 103.6 101.3
REMARK 620 4 CYS D 426 SG 120.2 106.3 113.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 418 SG
REMARK 620 2 HIS D 420 ND1 112.0
REMARK 620 3 CYS D 437 SG 109.2 108.7
REMARK 620 4 CYS D 440 SG 107.9 109.5 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 403 SG
REMARK 620 2 CYS I 406 SG 112.1
REMARK 620 3 CYS I 423 SG 103.6 101.9
REMARK 620 4 CYS I 426 SG 117.8 108.6 111.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 418 SG
REMARK 620 2 HIS I 420 ND1 114.5
REMARK 620 3 CYS I 437 SG 105.9 104.0
REMARK 620 4 CYS I 440 SG 108.8 113.8 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 403 SG
REMARK 620 2 CYS J 406 SG 110.6
REMARK 620 3 CYS J 423 SG 103.6 101.3
REMARK 620 4 CYS J 426 SG 120.2 106.3 113.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 418 SG
REMARK 620 2 HIS J 420 ND1 112.0
REMARK 620 3 CYS J 437 SG 109.3 108.7
REMARK 620 4 CYS J 440 SG 107.9 109.5 109.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide TYR E 34 and LYS E
REMARK 800 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ORH RELATED DB: PDB
DBREF 4WHV B 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4WHV C 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4WHV D 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4WHV E 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4WHV H 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4WHV I 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4WHV J 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4WHV K 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4WHV A 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 4WHV F 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 4WHV G 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 4WHV L 1 76 UNP P0CG47 UBB_HUMAN 1 76
SEQADV 4WHV GLY B -7 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO B -6 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LEU B -5 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLY B -4 UNP P61088 EXPRESSION TAG
SEQADV 4WHV SER B -3 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO B -2 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLU B -1 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PHE B 0 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LYS B 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 4WHV GLY C 337 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO C 338 UNP O76064 EXPRESSION TAG
SEQADV 4WHV LEU C 339 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY C 340 UNP O76064 EXPRESSION TAG
SEQADV 4WHV SER C 341 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO C 342 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLU C 343 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PHE C 344 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY D 337 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO D 338 UNP O76064 EXPRESSION TAG
SEQADV 4WHV LEU D 339 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY D 340 UNP O76064 EXPRESSION TAG
SEQADV 4WHV SER D 341 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO D 342 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLU D 343 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PHE D 344 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY E -7 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO E -6 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LEU E -5 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLY E -4 UNP P61088 EXPRESSION TAG
SEQADV 4WHV SER E -3 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO E -2 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLU E -1 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PHE E 0 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LYS E 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 4WHV GLY H -7 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO H -6 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LEU H -5 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLY H -4 UNP P61088 EXPRESSION TAG
SEQADV 4WHV SER H -3 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO H -2 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLU H -1 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PHE H 0 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LYS H 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 4WHV GLY I 337 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO I 338 UNP O76064 EXPRESSION TAG
SEQADV 4WHV LEU I 339 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY I 340 UNP O76064 EXPRESSION TAG
SEQADV 4WHV SER I 341 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO I 342 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLU I 343 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PHE I 344 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY J 337 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO J 338 UNP O76064 EXPRESSION TAG
SEQADV 4WHV LEU J 339 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY J 340 UNP O76064 EXPRESSION TAG
SEQADV 4WHV SER J 341 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PRO J 342 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLU J 343 UNP O76064 EXPRESSION TAG
SEQADV 4WHV PHE J 344 UNP O76064 EXPRESSION TAG
SEQADV 4WHV GLY K -7 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO K -6 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LEU K -5 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLY K -4 UNP P61088 EXPRESSION TAG
SEQADV 4WHV SER K -3 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PRO K -2 UNP P61088 EXPRESSION TAG
SEQADV 4WHV GLU K -1 UNP P61088 EXPRESSION TAG
SEQADV 4WHV PHE K 0 UNP P61088 EXPRESSION TAG
SEQADV 4WHV LYS K 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 4WHV GLY A -6 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO A -5 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY A -4 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV TYR A -3 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLN A -2 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV ASP A -1 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO A 0 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY F -6 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO F -5 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY F -4 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV TYR F -3 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLN F -2 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV ASP F -1 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO F 0 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY G -6 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO G -5 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY G -4 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV TYR G -3 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLN G -2 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV ASP G -1 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO G 0 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY L -6 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO L -5 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLY L -4 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV TYR L -3 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV GLN L -2 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV ASP L -1 UNP P0CG47 EXPRESSION TAG
SEQADV 4WHV PRO L 0 UNP P0CG47 EXPRESSION TAG
SEQRES 1 B 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 B 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 B 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 B 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 B 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 B 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 B 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 B 160 GLY ARG ILE LYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 B 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 B 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 B 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 B 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 B 160 MET ASN ASN ILE
SEQRES 1 C 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 C 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 C 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 C 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 C 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 C 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 C 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 C 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 C 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 C 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 C 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 C 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 D 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 D 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 D 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 D 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 D 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 D 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 D 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 D 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 D 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 D 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 D 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 D 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 E 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 E 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 E 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 E 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 E 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 E 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 E 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 E 160 GLY ARG ILE LYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 E 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 E 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 E 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 E 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 E 160 MET ASN ASN ILE
SEQRES 1 H 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 H 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 H 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 H 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 H 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 H 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 H 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 H 160 GLY ARG ILE LYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 H 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 H 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 H 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 H 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 H 160 MET ASN ASN ILE
SEQRES 1 I 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 I 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 I 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 I 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 I 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 I 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 I 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 I 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 I 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 I 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 I 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 I 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 J 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 J 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 J 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 J 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 J 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 J 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 J 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 J 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 J 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 J 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 J 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 J 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 K 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 K 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 K 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 K 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 K 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 K 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 K 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 K 160 GLY ARG ILE LYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 K 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 K 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 K 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 K 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 K 160 MET ASN ASN ILE
SEQRES 1 A 83 GLY PRO GLY TYR GLN ASP PRO MET GLN ILE PHE VAL LYS
SEQRES 2 A 83 THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO
SEQRES 3 A 83 SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP
SEQRES 4 A 83 LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 5 A 83 ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP
SEQRES 6 A 83 TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU
SEQRES 7 A 83 ARG LEU ARG GLY GLY
SEQRES 1 F 83 GLY PRO GLY TYR GLN ASP PRO MET GLN ILE PHE VAL LYS
SEQRES 2 F 83 THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO
SEQRES 3 F 83 SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP
SEQRES 4 F 83 LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 5 F 83 ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP
SEQRES 6 F 83 TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU
SEQRES 7 F 83 ARG LEU ARG GLY GLY
SEQRES 1 G 83 GLY PRO GLY TYR GLN ASP PRO MET GLN ILE PHE VAL LYS
SEQRES 2 G 83 THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO
SEQRES 3 G 83 SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP
SEQRES 4 G 83 LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 5 G 83 ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP
SEQRES 6 G 83 TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU
SEQRES 7 G 83 ARG LEU ARG GLY GLY
SEQRES 1 L 83 GLY PRO GLY TYR GLN ASP PRO MET GLN ILE PHE VAL LYS
SEQRES 2 L 83 THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO
SEQRES 3 L 83 SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP
SEQRES 4 L 83 LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 5 L 83 ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP
SEQRES 6 L 83 TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU
SEQRES 7 L 83 ARG LEU ARG GLY GLY
HET ZN C 501 1
HET ZN C 502 1
HET ZN D 501 1
HET ZN D 502 1
HET ZN I 501 1
HET ZN I 502 1
HET ZN J 501 1
HET ZN J 502 1
HETNAM ZN ZINC ION
FORMUL 13 ZN 8(ZN 2+)
HELIX 1 AA1 PRO B 5 GLU B 18 1 14
HELIX 2 AA2 LEU B 88 LYS B 92 5 5
HELIX 3 AA3 GLN B 100 ALA B 114 1 15
HELIX 4 AA4 ASP B 124 ASN B 132 1 9
HELIX 5 AA5 ASN B 132 ALA B 148 1 17
HELIX 6 AA6 GLU C 346 ASN C 399 1 54
HELIX 7 AA7 SER C 424 MET C 431 1 8
HELIX 8 AA8 SER C 450 ASN C 462 1 13
HELIX 9 AA9 SER C 465 LYS C 480 1 16
HELIX 10 AB1 GLU D 343 LEU D 397 1 55
HELIX 11 AB2 SER D 424 LYS D 434 1 11
HELIX 12 AB3 SER D 450 ASN D 462 1 13
HELIX 13 AB4 SER D 465 LYS D 480 1 16
HELIX 14 AB5 PRO E 5 GLU E 18 1 14
HELIX 15 AB6 LEU E 88 LYS E 92 5 5
HELIX 16 AB7 GLN E 100 ALA E 114 1 15
HELIX 17 AB8 ASP E 124 ASN E 132 1 9
HELIX 18 AB9 ASN E 132 ALA E 148 1 17
HELIX 19 AC1 PRO H 5 GLU H 18 1 14
HELIX 20 AC2 LEU H 88 LYS H 92 5 5
HELIX 21 AC3 GLN H 100 ALA H 114 1 15
HELIX 22 AC4 ASP H 124 ASN H 132 1 9
HELIX 23 AC5 ASN H 132 ALA H 148 1 17
HELIX 24 AC6 LYS I 381 ASN I 399 1 19
HELIX 25 AC7 SER I 424 MET I 431 1 8
HELIX 26 AC8 SER I 450 ASN I 462 1 13
HELIX 27 AC9 SER I 465 LYS I 480 1 16
HELIX 28 AD1 LYS J 381 LEU J 397 1 17
HELIX 29 AD2 SER J 424 LYS J 434 1 11
HELIX 30 AD3 SER J 450 ASN J 462 1 13
HELIX 31 AD4 SER J 465 LYS J 480 1 16
HELIX 32 AD5 PRO K 5 GLU K 18 1 14
HELIX 33 AD6 LEU K 88 LYS K 92 5 5
HELIX 34 AD7 GLN K 100 ALA K 114 1 15
HELIX 35 AD8 ASP K 124 ASN K 132 1 9
HELIX 36 AD9 ASN K 132 ALA K 148 1 17
HELIX 37 AE1 THR A 22 GLY A 35 1 14
HELIX 38 AE2 PRO A 37 GLN A 41 5 5
HELIX 39 AE3 LEU A 56 ASN A 60 5 5
HELIX 40 AE4 THR F 22 GLY F 35 1 14
HELIX 41 AE5 PRO F 37 GLN F 41 5 5
HELIX 42 AE6 LEU F 56 ASN F 60 5 5
HELIX 43 AE7 THR G 22 GLY G 35 1 14
HELIX 44 AE8 PRO G 37 GLN G 41 5 5
HELIX 45 AE9 LEU G 56 ASN G 60 5 5
HELIX 46 AF1 THR L 22 GLY L 35 1 14
HELIX 47 AF2 PRO L 37 GLN L 41 5 5
HELIX 48 AF3 LEU L 56 ASN L 60 5 5
SHEET 1 AA1 4 ILE B 23 PRO B 27 0
SHEET 2 AA1 4 TYR B 34 ALA B 40 -1 O HIS B 36 N GLU B 26
SHEET 3 AA1 4 THR B 51 PHE B 57 -1 O LEU B 56 N PHE B 35
SHEET 4 AA1 4 LYS B 68 PHE B 71 -1 O LYS B 68 N PHE B 57
SHEET 1 AA2 3 SER C 421 CYS C 423 0
SHEET 2 AA2 3 ALA C 413 LEU C 416 -1 N VAL C 414 O PHE C 422
SHEET 3 AA2 3 LYS C 447 TYR C 449 -1 O THR C 448 N THR C 415
SHEET 1 AA3 3 SER D 421 CYS D 423 0
SHEET 2 AA3 3 ALA D 413 LEU D 416 -1 N VAL D 414 O PHE D 422
SHEET 3 AA3 3 LYS D 447 TYR D 449 -1 O THR D 448 N THR D 415
SHEET 1 AA4 4 ILE E 23 PRO E 27 0
SHEET 2 AA4 4 TYR E 34 ALA E 40 -1 O HIS E 36 N GLU E 26
SHEET 3 AA4 4 THR E 51 PHE E 57 -1 O LEU E 56 N PHE E 35
SHEET 4 AA4 4 LYS E 68 PHE E 71 -1 O LYS E 68 N PHE E 57
SHEET 1 AA5 4 ILE H 23 PRO H 27 0
SHEET 2 AA5 4 TYR H 34 ALA H 40 -1 O HIS H 36 N GLU H 26
SHEET 3 AA5 4 THR H 51 PHE H 57 -1 O LEU H 56 N PHE H 35
SHEET 4 AA5 4 LYS H 68 PHE H 71 -1 O LYS H 68 N PHE H 57
SHEET 1 AA6 3 SER I 421 CYS I 423 0
SHEET 2 AA6 3 ALA I 413 LEU I 416 -1 N VAL I 414 O PHE I 422
SHEET 3 AA6 3 LYS I 447 TYR I 449 -1 O THR I 448 N THR I 415
SHEET 1 AA7 3 SER J 421 CYS J 423 0
SHEET 2 AA7 3 ALA J 413 LEU J 416 -1 N VAL J 414 O PHE J 422
SHEET 3 AA7 3 LYS J 447 TYR J 449 -1 O THR J 448 N THR J 415
SHEET 1 AA8 4 ILE K 23 PRO K 27 0
SHEET 2 AA8 4 TYR K 34 ALA K 40 -1 O HIS K 36 N GLU K 26
SHEET 3 AA8 4 THR K 51 PHE K 57 -1 O LEU K 56 N PHE K 35
SHEET 4 AA8 4 LYS K 68 PHE K 71 -1 O LYS K 68 N PHE K 57
SHEET 1 AA9 5 THR A 12 GLU A 16 0
SHEET 2 AA9 5 GLN A 2 LYS A 6 -1 N ILE A 3 O LEU A 15
SHEET 3 AA9 5 THR A 66 VAL A 70 1 O LEU A 67 N PHE A 4
SHEET 4 AA9 5 ARG A 42 PHE A 45 -1 N ILE A 44 O HIS A 68
SHEET 5 AA9 5 LYS A 48 GLN A 49 -1 O LYS A 48 N PHE A 45
SHEET 1 AB1 5 THR F 12 GLU F 16 0
SHEET 2 AB1 5 GLN F 2 LYS F 6 -1 N ILE F 3 O LEU F 15
SHEET 3 AB1 5 THR F 66 VAL F 70 1 O LEU F 67 N PHE F 4
SHEET 4 AB1 5 ARG F 42 PHE F 45 -1 N ILE F 44 O HIS F 68
SHEET 5 AB1 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45
SHEET 1 AB2 5 THR G 12 GLU G 16 0
SHEET 2 AB2 5 GLN G 2 LYS G 6 -1 N ILE G 3 O LEU G 15
SHEET 3 AB2 5 THR G 66 VAL G 70 1 O LEU G 67 N PHE G 4
SHEET 4 AB2 5 ARG G 42 PHE G 45 -1 N ILE G 44 O HIS G 68
SHEET 5 AB2 5 LYS G 48 GLN G 49 -1 O LYS G 48 N PHE G 45
SHEET 1 AB3 5 THR L 12 GLU L 16 0
SHEET 2 AB3 5 GLN L 2 LYS L 6 -1 N ILE L 3 O LEU L 15
SHEET 3 AB3 5 THR L 66 VAL L 70 1 O LEU L 67 N PHE L 4
SHEET 4 AB3 5 ARG L 42 PHE L 45 -1 N ILE L 44 O HIS L 68
SHEET 5 AB3 5 LYS L 48 GLN L 49 -1 O LYS L 48 N PHE L 45
LINK SG CYS C 403 ZN ZN C 502 1555 1555 2.40
LINK SG CYS C 406 ZN ZN C 502 1555 1555 2.33
LINK SG CYS C 418 ZN ZN C 501 1555 1555 2.30
LINK ND1 HIS C 420 ZN ZN C 501 1555 1555 2.07
LINK SG CYS C 423 ZN ZN C 502 1555 1555 2.39
LINK SG CYS C 426 ZN ZN C 502 1555 1555 2.32
LINK SG CYS C 437 ZN ZN C 501 1555 1555 2.32
LINK SG CYS C 440 ZN ZN C 501 1555 1555 2.30
LINK SG CYS D 403 ZN ZN D 502 1555 1555 2.33
LINK SG CYS D 406 ZN ZN D 502 1555 1555 2.31
LINK SG CYS D 418 ZN ZN D 501 1555 1555 2.23
LINK ND1 HIS D 420 ZN ZN D 501 1555 1555 2.22
LINK SG CYS D 423 ZN ZN D 502 1555 1555 2.35
LINK SG CYS D 426 ZN ZN D 502 1555 1555 2.28
LINK SG CYS D 437 ZN ZN D 501 1555 1555 2.32
LINK SG CYS D 440 ZN ZN D 501 1555 1555 2.24
LINK SG CYS I 403 ZN ZN I 502 1555 1555 2.40
LINK SG CYS I 406 ZN ZN I 502 1555 1555 2.32
LINK SG CYS I 418 ZN ZN I 501 1555 1555 2.30
LINK ND1 HIS I 420 ZN ZN I 501 1555 1555 2.07
LINK SG CYS I 423 ZN ZN I 502 1555 1555 2.39
LINK SG CYS I 426 ZN ZN I 502 1555 1555 2.32
LINK SG CYS I 437 ZN ZN I 501 1555 1555 2.32
LINK SG CYS I 440 ZN ZN I 501 1555 1555 2.30
LINK SG CYS J 403 ZN ZN J 502 1555 1555 2.33
LINK SG CYS J 406 ZN ZN J 502 1555 1555 2.31
LINK SG CYS J 418 ZN ZN J 501 1555 1555 2.23
LINK ND1 HIS J 420 ZN ZN J 501 1555 1555 2.22
LINK SG CYS J 423 ZN ZN J 502 1555 1555 2.35
LINK SG CYS J 426 ZN ZN J 502 1555 1555 2.28
LINK SG CYS J 437 ZN ZN J 501 1555 1555 2.32
LINK SG CYS J 440 ZN ZN J 501 1555 1555 2.24
CISPEP 1 TYR B 62 PRO B 63 0 9.45
CISPEP 2 TYR E 62 PRO E 63 0 9.52
CISPEP 3 TYR H 62 PRO H 63 0 9.52
CISPEP 4 TYR K 62 PRO K 63 0 9.45
SITE 1 AC1 4 CYS C 418 HIS C 420 CYS C 437 CYS C 440
SITE 1 AC2 4 CYS C 403 CYS C 406 CYS C 423 CYS C 426
SITE 1 AC3 4 CYS D 418 HIS D 420 CYS D 437 CYS D 440
SITE 1 AC4 4 CYS D 403 CYS D 406 CYS D 423 CYS D 426
SITE 1 AC5 4 CYS I 418 HIS I 420 CYS I 437 CYS I 440
SITE 1 AC6 4 CYS I 403 CYS I 406 CYS I 423 CYS I 426
SITE 1 AC7 4 CYS J 418 HIS J 420 CYS J 437 CYS J 440
SITE 1 AC8 4 CYS J 403 CYS J 406 CYS J 423 CYS J 426
SITE 1 AC9 13 PRO E 27 ASP E 28 ASN E 31 ALA E 32
SITE 2 AC9 13 ARG E 33 PHE E 35 HIS E 36 GLU E 55
SITE 3 AC9 13 LEU E 56 THR E 73 ILE E 75 TRP E 143
SITE 4 AC9 13 TYR E 147
CRYST1 341.379 341.379 113.447 90.00 90.00 120.00 P 64 2 2 48
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 0.002929 0.001691 0.000000 0.00000
SCALE2 0.000000 0.003382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008815 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
