HEADER PROTEIN BINDING/LIGASE 11-FEB-14 4ORH
TITLE CRYSTAL STRUCTURE OF RNF8 BOUND TO THE UBC13/MMS2 HETERODIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2;
COMPND 3 CHAIN: A, E, I;
COMPND 4 SYNONYM: DDVIT 1, ENTEROCYTE DIFFERENTIATION-ASSOCIATED FACTOR 1,
COMPND 5 EDAF-1, ENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1, EDPF-1, MMS2
COMPND 6 HOMOLOG, VITAMIN D3-INDUCIBLE PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;
COMPND 10 CHAIN: B, F, J;
COMPND 11 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME, UBC13, UBCH13,
COMPND 12 UBIQUITIN CARRIER PROTEIN N, UBIQUITIN-PROTEIN LIGASE N;
COMPND 13 EC: 6.3.2.19;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF8;
COMPND 17 CHAIN: C, G, H, K, L;
COMPND 18 SYNONYM: HRNF8, RING FINGER PROTEIN 8;
COMPND 19 EC: 6.3.2.-;
COMPND 20 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: MMS2, UBE2V2, UEV2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: UBE2N, BLU;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: RNF8, KIAA0646;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS COILED-COIL, E3 UBIQUITIN LIGASE, UBIQUITIN, PROTEIN BINDING-LIGASE,
KEYWDS 2 PROTEIN BINDING-LIGASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.CAMPBELL,R.A.EDWARDS,J.N.M.GLOVER
REVDAT 4 22-NOV-17 4ORH 1 REMARK
REVDAT 3 03-DEC-14 4ORH 1 AUTHOR
REVDAT 2 05-NOV-14 4ORH 1 AUTHOR
REVDAT 1 26-FEB-14 4ORH 0
SPRSDE 26-FEB-14 4ORH 4EPO
JRNL AUTH S.J.CAMPBELL,R.A.EDWARDS,C.C.LEUNG,D.NECULAI,C.D.HODGE,
JRNL AUTH 2 S.DHE-PAGANON,J.N.GLOVER
JRNL TITL MOLECULAR INSIGHTS INTO THE FUNCTION OF RING FINGER
JRNL TITL 2 (RNF)-CONTAINING PROTEINS HRNF8 AND HRNF168 IN
JRNL TITL 3 UBC13/MMS2-DEPENDENT UBIQUITYLATION.
JRNL REF J.BIOL.CHEM. V. 287 23900 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22589545
JRNL DOI 10.1074/JBC.M112.359653
REMARK 2
REMARK 2 RESOLUTION. 4.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.3_1479
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) : 4.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 123.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 45858
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.277
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1258
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1123.5808 - 12.3430 0.99 2618 119 0.2357 0.2137
REMARK 3 2 12.3430 - 9.7983 0.99 2595 146 0.1822 0.1893
REMARK 3 3 9.7983 - 8.5601 1.00 2615 144 0.2318 0.2340
REMARK 3 4 8.5601 - 7.7776 1.00 2615 151 0.2536 0.2607
REMARK 3 5 7.7776 - 7.2202 1.00 2665 108 0.2787 0.2956
REMARK 3 6 7.2202 - 6.7945 1.00 2618 124 0.3013 0.3661
REMARK 3 7 6.7945 - 6.4543 0.99 2594 124 0.3269 0.3760
REMARK 3 8 6.4543 - 6.1733 0.96 2515 176 0.3564 0.3533
REMARK 3 9 6.1733 - 5.9357 0.97 2543 114 0.3426 0.3246
REMARK 3 10 5.9357 - 5.7308 0.97 2546 118 0.3412 0.3312
REMARK 3 11 5.7308 - 5.5517 0.97 2515 180 0.3396 0.3623
REMARK 3 12 5.5517 - 5.3930 0.97 2525 131 0.3470 0.3622
REMARK 3 13 5.3930 - 5.2510 0.97 2553 146 0.3610 0.3694
REMARK 3 14 5.2510 - 5.1229 0.97 2536 147 0.3544 0.3796
REMARK 3 15 5.1229 - 5.0064 0.97 2532 143 0.3540 0.3101
REMARK 3 16 5.0064 - 4.8999 0.97 2566 129 0.3572 0.3652
REMARK 3 17 4.8999 - 4.8018 0.92 2377 130 0.3549 0.3655
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) : 0.740
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 175.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 258.4
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 11728
REMARK 3 ANGLE : 1.091 15931
REMARK 3 CHIRALITY : 0.058 1817
REMARK 3 PLANARITY : 0.004 2084
REMARK 3 DIHEDRAL : 12.361 4352
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 6 THROUGH 144)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.8753 33.1482 17.3940
REMARK 3 T TENSOR
REMARK 3 T11: 1.9041 T22: 2.7651
REMARK 3 T33: 2.4334 T12: 0.0882
REMARK 3 T13: -0.4148 T23: -0.0882
REMARK 3 L TENSOR
REMARK 3 L11: 8.8025 L22: 10.4676
REMARK 3 L33: 7.2046 L12: 1.5215
REMARK 3 L13: -1.0968 L23: -5.9856
REMARK 3 S TENSOR
REMARK 3 S11: 0.4646 S12: -0.1035 S13: 0.5232
REMARK 3 S21: -0.6378 S22: -0.1910 S23: -0.3261
REMARK 3 S31: -0.7873 S32: -0.1020 S33: -0.0009
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 3 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5562 5.3868 31.2266
REMARK 3 T TENSOR
REMARK 3 T11: 1.1307 T22: 3.1914
REMARK 3 T33: 1.7092 T12: -0.4525
REMARK 3 T13: -0.1205 T23: 0.2011
REMARK 3 L TENSOR
REMARK 3 L11: 14.3881 L22: 15.0554
REMARK 3 L33: 9.6163 L12: -4.7716
REMARK 3 L13: 2.8746 L23: -6.7414
REMARK 3 S TENSOR
REMARK 3 S11: 0.4506 S12: -0.4020 S13: -0.2486
REMARK 3 S21: -0.3177 S22: -0.6173 S23: 0.2458
REMARK 3 S31: 0.1400 S32: -0.5332 S33: 0.0048
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 392 THROUGH 483)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3656 8.3386 30.8612
REMARK 3 T TENSOR
REMARK 3 T11: 1.3826 T22: 3.5515
REMARK 3 T33: 3.1570 T12: -0.0142
REMARK 3 T13: -0.3525 T23: -0.2434
REMARK 3 L TENSOR
REMARK 3 L11: 4.6764 L22: 4.8112
REMARK 3 L33: 9.6901 L12: -1.2684
REMARK 3 L13: 1.9324 L23: -4.0872
REMARK 3 S TENSOR
REMARK 3 S11: 1.0492 S12: -0.6541 S13: 0.4414
REMARK 3 S21: 0.3805 S22: -0.6924 S23: 0.1681
REMARK 3 S31: -0.6138 S32: -0.2506 S33: -0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 7 THROUGH 144)
REMARK 3 ORIGIN FOR THE GROUP (A): 93.3840 -18.9786 44.8469
REMARK 3 T TENSOR
REMARK 3 T11: 1.4120 T22: 3.3593
REMARK 3 T33: 2.0662 T12: -0.0524
REMARK 3 T13: 0.0958 T23: 0.6246
REMARK 3 L TENSOR
REMARK 3 L11: 9.6165 L22: 8.0628
REMARK 3 L33: 9.3834 L12: -3.2907
REMARK 3 L13: -1.9392 L23: -0.1050
REMARK 3 S TENSOR
REMARK 3 S11: 0.3416 S12: -1.9560 S13: -0.5958
REMARK 3 S21: -0.2920 S22: -0.0248 S23: 0.6708
REMARK 3 S31: 0.4441 S32: 0.4392 S33: 0.0019
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 3 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A): 67.2221 -1.8946 34.6389
REMARK 3 T TENSOR
REMARK 3 T11: 1.2792 T22: 2.8140
REMARK 3 T33: 1.8845 T12: 0.0245
REMARK 3 T13: -0.0148 T23: 0.6316
REMARK 3 L TENSOR
REMARK 3 L11: 9.4580 L22: 13.1760
REMARK 3 L33: 10.3848 L12: -1.5730
REMARK 3 L13: 0.7145 L23: 10.9533
REMARK 3 S TENSOR
REMARK 3 S11: -0.6477 S12: -1.0270 S13: 0.2226
REMARK 3 S21: -0.0727 S22: -0.4587 S23: 0.4098
REMARK 3 S31: 0.3321 S32: 0.1613 S33: -0.0003
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 345 THROUGH 483)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0791 -14.1912 0.8909
REMARK 3 T TENSOR
REMARK 3 T11: 2.2474 T22: 2.5298
REMARK 3 T33: 2.3608 T12: -0.1172
REMARK 3 T13: 0.1694 T23: 0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 2.4507 L22: -1.2580
REMARK 3 L33: 8.1503 L12: 0.3963
REMARK 3 L13: -1.9616 L23: -0.5336
REMARK 3 S TENSOR
REMARK 3 S11: 0.5719 S12: -0.3301 S13: -0.1833
REMARK 3 S21: -0.1356 S22: 0.1764 S23: -0.1134
REMARK 3 S31: -0.0073 S32: 1.1898 S33: 0.0012
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 342 THROUGH 483)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1038 -16.1521 -5.3711
REMARK 3 T TENSOR
REMARK 3 T11: 2.2560 T22: 2.5434
REMARK 3 T33: 2.4203 T12: -0.3540
REMARK 3 T13: -0.3135 T23: 0.2938
REMARK 3 L TENSOR
REMARK 3 L11: -1.0815 L22: 9.3442
REMARK 3 L33: 5.1519 L12: 2.7267
REMARK 3 L13: 0.0972 L23: -7.3169
REMARK 3 S TENSOR
REMARK 3 S11: -0.4404 S12: -1.0275 S13: 0.1033
REMARK 3 S21: -0.8789 S22: -0.3728 S23: 0.2117
REMARK 3 S31: 1.3930 S32: 0.1065 S33: -0.0241
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'I' AND RESID 7 THROUGH 144)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3378 49.2326 71.3638
REMARK 3 T TENSOR
REMARK 3 T11: 5.0072 T22: 4.5660
REMARK 3 T33: 5.1996 T12: 0.5951
REMARK 3 T13: 0.7317 T23: -0.9877
REMARK 3 L TENSOR
REMARK 3 L11: -1.0254 L22: -0.2201
REMARK 3 L33: -0.9084 L12: 0.3791
REMARK 3 L13: 0.0780 L23: -2.7298
REMARK 3 S TENSOR
REMARK 3 S11: 0.4348 S12: -0.1408 S13: 2.4092
REMARK 3 S21: 2.9829 S22: 0.2521 S23: 2.5559
REMARK 3 S31: -2.3628 S32: 1.0700 S33: 0.2461
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'J' AND RESID 3 THROUGH 150)
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0702 20.7311 55.8294
REMARK 3 T TENSOR
REMARK 3 T11: 1.5447 T22: 3.5799
REMARK 3 T33: 2.3017 T12: 0.7107
REMARK 3 T13: -0.0098 T23: -0.3780
REMARK 3 L TENSOR
REMARK 3 L11: 10.6003 L22: 7.1057
REMARK 3 L33: 13.6605 L12: 4.0070
REMARK 3 L13: -4.9763 L23: -1.8651
REMARK 3 S TENSOR
REMARK 3 S11: -0.6813 S12: -0.5864 S13: 0.7787
REMARK 3 S21: 0.2224 S22: 0.3813 S23: -0.5626
REMARK 3 S31: -0.4983 S32: -1.6822 S33: -0.0006
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'K' AND RESID 345 THROUGH 483)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4199 -4.0385 75.0794
REMARK 3 T TENSOR
REMARK 3 T11: 2.2795 T22: 5.1505
REMARK 3 T33: 2.5161 T12: 0.2642
REMARK 3 T13: 0.3760 T23: 0.3753
REMARK 3 L TENSOR
REMARK 3 L11: -0.6745 L22: 6.5504
REMARK 3 L33: 1.3192 L12: 1.8203
REMARK 3 L13: -1.6447 L23: -2.2104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: -0.0832 S13: 0.8183
REMARK 3 S21: 2.7237 S22: -0.2701 S23: -0.2449
REMARK 3 S31: -0.4586 S32: -1.3820 S33: -0.0424
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'L' AND RESID 342 THROUGH 483)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9062 -15.2438 70.8316
REMARK 3 T TENSOR
REMARK 3 T11: 2.7828 T22: 5.1651
REMARK 3 T33: 3.0751 T12: -0.3380
REMARK 3 T13: 0.4676 T23: 0.6652
REMARK 3 L TENSOR
REMARK 3 L11: 0.2624 L22: 4.6303
REMARK 3 L33: -1.0143 L12: -1.3823
REMARK 3 L13: 0.3963 L23: -2.0967
REMARK 3 S TENSOR
REMARK 3 S11: -1.0282 S12: -0.9148 S13: -0.2838
REMARK 3 S21: -0.4893 S22: 1.9770 S23: -0.0583
REMARK 3 S31: 0.9064 S32: -3.3930 S33: 0.1133
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 4ORH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084858.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 4.5
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11435
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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45946
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.800
REMARK 200 RESOLUTION RANGE LOW (A) : 200.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.57300
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 75 MM SODIUM ACETATE, 1.0 M AMMONIUM
REMARK 280 PHOSPHATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 102.62900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 102.62900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 117.68600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 102.62900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 102.62900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.68600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 102.62900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 102.62900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 117.68600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 102.62900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 102.62900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.68600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: I, J, K, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 A -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 PRO A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 ASN A 145
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 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 GLN C 345
REMARK 465 GLU C 346
REMARK 465 HIS C 347
REMARK 465 TRP C 348
REMARK 465 ALA C 349
REMARK 465 LEU C 350
REMARK 465 MET C 351
REMARK 465 GLU C 352
REMARK 465 GLU C 353
REMARK 465 LEU C 354
REMARK 465 ASN C 355
REMARK 465 ARG C 356
REMARK 465 SER C 357
REMARK 465 LYS C 358
REMARK 465 LYS C 359
REMARK 465 ASP C 360
REMARK 465 PHE C 361
REMARK 465 GLU C 362
REMARK 465 ALA C 363
REMARK 465 ILE C 364
REMARK 465 ILE C 365
REMARK 465 GLN C 366
REMARK 465 ALA C 367
REMARK 465 LYS C 368
REMARK 465 ASN C 369
REMARK 465 LYS C 370
REMARK 465 GLU C 371
REMARK 465 LEU C 372
REMARK 465 GLU C 373
REMARK 465 GLN C 374
REMARK 465 THR C 375
REMARK 465 LYS C 376
REMARK 465 GLU C 377
REMARK 465 GLU C 378
REMARK 465 LYS C 379
REMARK 465 GLU C 380
REMARK 465 LYS C 381
REMARK 465 MET C 382
REMARK 465 GLN C 383
REMARK 465 ALA C 384
REMARK 465 GLN C 385
REMARK 465 LYS C 386
REMARK 465 GLU C 387
REMARK 465 GLU C 388
REMARK 465 VAL C 389
REMARK 465 LEU C 390
REMARK 465 SER C 391
REMARK 465 LEU C 484
REMARK 465 PHE C 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 VAL E 3
REMARK 465 SER E 4
REMARK 465 THR E 5
REMARK 465 GLY E 6
REMARK 465 ASN E 145
REMARK 465 GLY F -7
REMARK 465 PRO F -6
REMARK 465 LEU F -5
REMARK 465 GLY F -4
REMARK 465 SER F -3
REMARK 465 PRO F -2
REMARK 465 GLU F -1
REMARK 465 PHE F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 ASN F 151
REMARK 465 ILE F 152
REMARK 465 GLY G 337
REMARK 465 PRO G 338
REMARK 465 LEU G 339
REMARK 465 GLY G 340
REMARK 465 SER G 341
REMARK 465 PRO G 342
REMARK 465 GLU G 343
REMARK 465 PHE G 344
REMARK 465 LEU G 484
REMARK 465 PHE G 485
REMARK 465 GLY H 337
REMARK 465 PRO H 338
REMARK 465 LEU H 339
REMARK 465 GLY H 340
REMARK 465 SER H 341
REMARK 465 LEU H 484
REMARK 465 PHE H 485
REMARK 465 GLY I -7
REMARK 465 PRO I -6
REMARK 465 LEU I -5
REMARK 465 GLY I -4
REMARK 465 SER I -3
REMARK 465 PRO I -2
REMARK 465 GLU I -1
REMARK 465 PHE I 0
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 VAL I 3
REMARK 465 SER I 4
REMARK 465 THR I 5
REMARK 465 GLY I 6
REMARK 465 ASN I 145
REMARK 465 GLY J -7
REMARK 465 PRO J -6
REMARK 465 LEU J -5
REMARK 465 GLY J -4
REMARK 465 SER J -3
REMARK 465 PRO J -2
REMARK 465 GLU J -1
REMARK 465 PHE J 0
REMARK 465 MET J 1
REMARK 465 ALA J 2
REMARK 465 ASN J 151
REMARK 465 ILE J 152
REMARK 465 GLY K 337
REMARK 465 PRO K 338
REMARK 465 LEU K 339
REMARK 465 GLY K 340
REMARK 465 SER K 341
REMARK 465 PRO K 342
REMARK 465 GLU K 343
REMARK 465 PHE K 344
REMARK 465 LEU K 484
REMARK 465 PHE K 485
REMARK 465 GLY L 337
REMARK 465 PRO L 338
REMARK 465 LEU L 339
REMARK 465 GLY L 340
REMARK 465 SER L 341
REMARK 465 LEU L 484
REMARK 465 PHE L 485
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 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 LYS C 480 CG CD CE NZ
REMARK 470 LYS C 482 CG CD CE NZ
REMARK 470 ARG C 483 CG CD NE CZ NH1 NH2
REMARK 470 GLN G 345 CG CD OE1 NE2
REMARK 470 GLU G 346 CG CD OE1 OE2
REMARK 470 HIS G 347 CG ND1 CD2 CE1 NE2
REMARK 470 TRP G 348 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 348 CZ3 CH2
REMARK 470 LEU G 350 CG CD1 CD2
REMARK 470 MET G 351 CG SD CE
REMARK 470 GLU G 352 CG CD OE1 OE2
REMARK 470 GLU G 353 CG CD OE1 OE2
REMARK 470 LEU G 354 CG CD1 CD2
REMARK 470 ASN G 355 CG OD1 ND2
REMARK 470 ARG G 356 CG CD NE CZ NH1 NH2
REMARK 470 SER G 357 OG
REMARK 470 LYS G 358 CG CD CE NZ
REMARK 470 LYS G 359 CG CD CE NZ
REMARK 470 ASP G 360 CG OD1 OD2
REMARK 470 PHE G 361 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU G 362 CG CD OE1 OE2
REMARK 470 ILE G 364 CG1 CG2 CD1
REMARK 470 ILE G 365 CG1 CG2 CD1
REMARK 470 GLN G 366 CG CD OE1 NE2
REMARK 470 LYS G 368 CG CD CE NZ
REMARK 470 ASN G 369 CG OD1 ND2
REMARK 470 LYS G 370 CG CD CE NZ
REMARK 470 GLU G 371 CG CD OE1 OE2
REMARK 470 LEU G 372 CG CD1 CD2
REMARK 470 GLU G 373 CG CD OE1 OE2
REMARK 470 GLN G 374 CG CD OE1 NE2
REMARK 470 THR G 375 OG1 CG2
REMARK 470 LYS G 376 CG CD CE NZ
REMARK 470 GLU G 377 CG CD OE1 OE2
REMARK 470 GLU G 378 CG CD OE1 OE2
REMARK 470 LYS G 379 CG CD CE NZ
REMARK 470 GLU G 380 CG CD OE1 OE2
REMARK 470 LYS G 381 CG CD CE NZ
REMARK 470 MET G 382 CG SD CE
REMARK 470 GLN G 383 CG CD OE1 NE2
REMARK 470 GLN G 385 CG CD OE1 NE2
REMARK 470 LYS G 386 CG CD CE NZ
REMARK 470 GLU G 387 CG CD OE1 OE2
REMARK 470 GLU G 388 CG CD OE1 OE2
REMARK 470 VAL G 389 CG1 CG2
REMARK 470 LEU G 390 CG CD1 CD2
REMARK 470 SER G 391 OG
REMARK 470 HIS G 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET G 393 CG SD CE
REMARK 470 ASN G 394 CG OD1 ND2
REMARK 470 ASP G 395 CG OD1 OD2
REMARK 470 VAL G 396 CG1 CG2
REMARK 470 LEU G 397 CG CD1 CD2
REMARK 470 LYS G 480 CG CD CE NZ
REMARK 470 LYS G 482 CG CD CE NZ
REMARK 470 ARG G 483 CG CD NE CZ NH1 NH2
REMARK 470 PRO H 342 CG CD
REMARK 470 GLU H 343 CB CG CD OE1 OE2
REMARK 470 PHE H 344 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN H 345 CG CD OE1 NE2
REMARK 470 GLU H 346 CG CD OE1 OE2
REMARK 470 HIS H 347 CG ND1 CD2 CE1 NE2
REMARK 470 TRP H 348 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP H 348 CZ3 CH2
REMARK 470 LEU H 350 CG CD1 CD2
REMARK 470 MET H 351 CG SD CE
REMARK 470 GLU H 352 CG CD OE1 OE2
REMARK 470 GLU H 353 CG CD OE1 OE2
REMARK 470 LEU H 354 CG CD1 CD2
REMARK 470 ASN H 355 CG OD1 ND2
REMARK 470 ARG H 356 CG CD NE CZ NH1 NH2
REMARK 470 SER H 357 OG
REMARK 470 LYS H 358 CG CD CE NZ
REMARK 470 LYS H 359 CG CD CE NZ
REMARK 470 ASP H 360 CG OD1 OD2
REMARK 470 PHE H 361 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU H 362 CG CD OE1 OE2
REMARK 470 ILE H 364 CG1 CG2 CD1
REMARK 470 ILE H 365 CG1 CG2 CD1
REMARK 470 GLN H 366 CG CD OE1 NE2
REMARK 470 LYS H 368 CG CD CE NZ
REMARK 470 ASN H 369 CG OD1 ND2
REMARK 470 LYS H 370 CG CD CE NZ
REMARK 470 GLU H 371 CG CD OE1 OE2
REMARK 470 LEU H 372 CG CD1 CD2
REMARK 470 GLU H 373 CG CD OE1 OE2
REMARK 470 GLN H 374 CG CD OE1 NE2
REMARK 470 THR H 375 OG1 CG2
REMARK 470 LYS H 376 CG CD CE NZ
REMARK 470 GLU H 377 CG CD OE1 OE2
REMARK 470 GLU H 378 CG CD OE1 OE2
REMARK 470 LYS H 379 CG CD CE NZ
REMARK 470 GLU H 380 CG CD OE1 OE2
REMARK 470 LYS H 381 CG CD CE NZ
REMARK 470 MET H 382 CG SD CE
REMARK 470 GLN H 383 CG CD OE1 NE2
REMARK 470 GLN H 385 CG CD OE1 NE2
REMARK 470 LYS H 386 CG CD CE NZ
REMARK 470 GLU H 387 CG CD OE1 OE2
REMARK 470 GLU H 388 CG CD OE1 OE2
REMARK 470 VAL H 389 CG1 CG2
REMARK 470 LEU H 390 CG CD1 CD2
REMARK 470 SER H 391 OG
REMARK 470 HIS H 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET H 393 CG SD CE
REMARK 470 ASN H 394 CG OD1 ND2
REMARK 470 ASP H 395 CG OD1 OD2
REMARK 470 VAL H 396 CG1 CG2
REMARK 470 LEU H 397 CG CD1 CD2
REMARK 470 LYS H 480 CG CD CE NZ
REMARK 470 LYS H 482 CG CD CE NZ
REMARK 470 ARG H 483 CG CD NE CZ NH1 NH2
REMARK 470 GLN K 345 CG CD OE1 NE2
REMARK 470 GLU K 346 CG CD OE1 OE2
REMARK 470 HIS K 347 CG ND1 CD2 CE1 NE2
REMARK 470 TRP K 348 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP K 348 CZ3 CH2
REMARK 470 LEU K 350 CG CD1 CD2
REMARK 470 MET K 351 CG SD CE
REMARK 470 GLU K 352 CG CD OE1 OE2
REMARK 470 GLU K 353 CG CD OE1 OE2
REMARK 470 LEU K 354 CG CD1 CD2
REMARK 470 ASN K 355 CG OD1 ND2
REMARK 470 ARG K 356 CG CD NE CZ NH1 NH2
REMARK 470 SER K 357 OG
REMARK 470 LYS K 358 CG CD CE NZ
REMARK 470 LYS K 359 CG CD CE NZ
REMARK 470 ASP K 360 CG OD1 OD2
REMARK 470 PHE K 361 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU K 362 CG CD OE1 OE2
REMARK 470 ILE K 364 CG1 CG2 CD1
REMARK 470 ILE K 365 CG1 CG2 CD1
REMARK 470 GLN K 366 CG CD OE1 NE2
REMARK 470 LYS K 368 CG CD CE NZ
REMARK 470 ASN K 369 CG OD1 ND2
REMARK 470 LYS K 370 CG CD CE NZ
REMARK 470 GLU K 371 CG CD OE1 OE2
REMARK 470 LEU K 372 CG CD1 CD2
REMARK 470 GLU K 373 CG CD OE1 OE2
REMARK 470 GLN K 374 CG CD OE1 NE2
REMARK 470 THR K 375 OG1 CG2
REMARK 470 LYS K 376 CG CD CE NZ
REMARK 470 GLU K 377 CG CD OE1 OE2
REMARK 470 GLU K 378 CG CD OE1 OE2
REMARK 470 LYS K 379 CG CD CE NZ
REMARK 470 GLU K 380 CG CD OE1 OE2
REMARK 470 LYS K 381 CG CD CE NZ
REMARK 470 MET K 382 CG SD CE
REMARK 470 GLN K 383 CG CD OE1 NE2
REMARK 470 GLN K 385 CG CD OE1 NE2
REMARK 470 LYS K 386 CG CD CE NZ
REMARK 470 GLU K 387 CG CD OE1 OE2
REMARK 470 GLU K 388 CG CD OE1 OE2
REMARK 470 VAL K 389 CG1 CG2
REMARK 470 LEU K 390 CG CD1 CD2
REMARK 470 SER K 391 OG
REMARK 470 HIS K 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET K 393 CG SD CE
REMARK 470 ASN K 394 CG OD1 ND2
REMARK 470 ASP K 395 CG OD1 OD2
REMARK 470 VAL K 396 CG1 CG2
REMARK 470 LEU K 397 CG CD1 CD2
REMARK 470 LYS K 480 CG CD CE NZ
REMARK 470 LYS K 482 CG CD CE NZ
REMARK 470 ARG K 483 CG CD NE CZ NH1 NH2
REMARK 470 PRO L 342 CG CD
REMARK 470 GLU L 343 CB CG CD OE1 OE2
REMARK 470 PHE L 344 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN L 345 CG CD OE1 NE2
REMARK 470 GLU L 346 CG CD OE1 OE2
REMARK 470 HIS L 347 CG ND1 CD2 CE1 NE2
REMARK 470 TRP L 348 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP L 348 CZ3 CH2
REMARK 470 LEU L 350 CG CD1 CD2
REMARK 470 MET L 351 CG SD CE
REMARK 470 GLU L 352 CG CD OE1 OE2
REMARK 470 GLU L 353 CG CD OE1 OE2
REMARK 470 LEU L 354 CG CD1 CD2
REMARK 470 ASN L 355 CG OD1 ND2
REMARK 470 ARG L 356 CG CD NE CZ NH1 NH2
REMARK 470 SER L 357 OG
REMARK 470 LYS L 358 CG CD CE NZ
REMARK 470 LYS L 359 CG CD CE NZ
REMARK 470 ASP L 360 CG OD1 OD2
REMARK 470 PHE L 361 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU L 362 CG CD OE1 OE2
REMARK 470 ILE L 364 CG1 CG2 CD1
REMARK 470 ILE L 365 CG1 CG2 CD1
REMARK 470 GLN L 366 CG CD OE1 NE2
REMARK 470 LYS L 368 CG CD CE NZ
REMARK 470 ASN L 369 CG OD1 ND2
REMARK 470 LYS L 370 CG CD CE NZ
REMARK 470 GLU L 371 CG CD OE1 OE2
REMARK 470 LEU L 372 CG CD1 CD2
REMARK 470 GLU L 373 CG CD OE1 OE2
REMARK 470 GLN L 374 CG CD OE1 NE2
REMARK 470 THR L 375 OG1 CG2
REMARK 470 LYS L 376 CG CD CE NZ
REMARK 470 GLU L 377 CG CD OE1 OE2
REMARK 470 GLU L 378 CG CD OE1 OE2
REMARK 470 LYS L 379 CG CD CE NZ
REMARK 470 GLU L 380 CG CD OE1 OE2
REMARK 470 LYS L 381 CG CD CE NZ
REMARK 470 MET L 382 CG SD CE
REMARK 470 GLN L 383 CG CD OE1 NE2
REMARK 470 GLN L 385 CG CD OE1 NE2
REMARK 470 LYS L 386 CG CD CE NZ
REMARK 470 GLU L 387 CG CD OE1 OE2
REMARK 470 GLU L 388 CG CD OE1 OE2
REMARK 470 VAL L 389 CG1 CG2
REMARK 470 LEU L 390 CG CD1 CD2
REMARK 470 SER L 391 OG
REMARK 470 HIS L 392 CG ND1 CD2 CE1 NE2
REMARK 470 MET L 393 CG SD CE
REMARK 470 ASN L 394 CG OD1 ND2
REMARK 470 ASP L 395 CG OD1 OD2
REMARK 470 VAL L 396 CG1 CG2
REMARK 470 LEU L 397 CG CD1 CD2
REMARK 470 LYS L 480 CG CD CE NZ
REMARK 470 LYS L 482 CG CD CE NZ
REMARK 470 ARG L 483 CG CD NE CZ NH1 NH2
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 O LEU F 99 OG1 THR F 103 1.91
REMARK 500 O MET F 64 NH2 ARG G 433 1.97
REMARK 500 O MET J 64 NH2 ARG K 433 2.12
REMARK 500 NE2 GLN F 135 OG1 THR J 103 2.13
REMARK 500 O LEU J 99 OG1 THR J 103 2.16
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 -72.94 -145.55
REMARK 500 LYS B 94 40.54 -94.33
REMARK 500 PRO B 97 -7.31 -55.75
REMARK 500 GLN B 100 171.95 79.21
REMARK 500 ASN B 116 78.75 -119.14
REMARK 500 LEU B 121 36.76 -92.56
REMARK 500 ASN B 123 -100.21 -48.56
REMARK 500 ASP B 124 -25.43 177.79
REMARK 500 GLU C 400 -54.85 -137.75
REMARK 500 ALA C 419 1.73 83.75
REMARK 500 LYS F 92 -72.90 -145.52
REMARK 500 LYS F 94 40.53 -94.33
REMARK 500 PRO F 97 -7.31 -55.76
REMARK 500 GLN F 100 172.02 79.20
REMARK 500 ASN F 116 78.70 -119.14
REMARK 500 LEU F 121 36.74 -92.59
REMARK 500 ASN F 123 -100.23 -48.60
REMARK 500 ASP F 124 -25.41 177.87
REMARK 500 LEU G 397 -89.91 -54.90
REMARK 500 GLU G 400 -17.88 -142.26
REMARK 500 ALA G 419 3.75 85.45
REMARK 500 ILE G 435 57.62 -98.49
REMARK 500 GLU H 400 -54.77 -137.79
REMARK 500 ALA H 419 1.88 83.64
REMARK 500 LYS J 92 -72.88 -145.57
REMARK 500 LYS J 94 40.58 -94.36
REMARK 500 PRO J 97 -7.27 -55.81
REMARK 500 GLN J 100 172.00 79.21
REMARK 500 ASN J 116 78.64 -119.10
REMARK 500 LEU J 121 36.78 -92.58
REMARK 500 ASN J 123 -100.18 -48.66
REMARK 500 ASP J 124 -25.31 177.86
REMARK 500 LEU K 397 -77.22 -52.80
REMARK 500 GLU K 400 -33.25 -135.24
REMARK 500 ALA K 419 3.62 85.44
REMARK 500 ILE K 435 57.66 -98.56
REMARK 500 ALA L 419 1.83 83.83
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 K 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 420 ND1
REMARK 620 2 CYS K 440 SG 113.8
REMARK 620 3 CYS K 418 SG 114.5 108.8
REMARK 620 4 CYS K 437 SG 104.0 109.4 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 420 ND1
REMARK 620 2 CYS G 440 SG 113.8
REMARK 620 3 CYS G 418 SG 114.6 108.8
REMARK 620 4 CYS G 437 SG 104.0 109.4 105.8
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 HIS C 420 ND1
REMARK 620 2 CYS C 418 SG 112.0
REMARK 620 3 CYS C 440 SG 109.6 107.9
REMARK 620 4 CYS C 437 SG 108.7 109.2 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 420 ND1
REMARK 620 2 CYS L 418 SG 112.0
REMARK 620 3 CYS L 440 SG 109.5 107.9
REMARK 620 4 CYS L 437 SG 108.7 109.2 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 420 ND1
REMARK 620 2 CYS H 418 SG 112.0
REMARK 620 3 CYS H 440 SG 109.5 107.9
REMARK 620 4 CYS H 437 SG 108.7 109.2 109.5
REMARK 620 N 1 2 3
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 426 SG
REMARK 620 2 CYS C 406 SG 106.3
REMARK 620 3 CYS C 403 SG 120.2 110.7
REMARK 620 4 CYS C 423 SG 113.3 101.3 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 426 SG
REMARK 620 2 CYS H 406 SG 106.3
REMARK 620 3 CYS H 403 SG 120.2 110.6
REMARK 620 4 CYS H 423 SG 113.4 101.3 103.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 426 SG
REMARK 620 2 CYS L 406 SG 106.3
REMARK 620 3 CYS L 403 SG 120.2 110.6
REMARK 620 4 CYS L 423 SG 113.3 101.3 103.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 426 SG
REMARK 620 2 CYS K 406 SG 108.6
REMARK 620 3 CYS K 423 SG 111.6 101.8
REMARK 620 4 CYS K 403 SG 117.9 112.1 103.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 426 SG
REMARK 620 2 CYS G 406 SG 108.6
REMARK 620 3 CYS G 423 SG 111.6 101.9
REMARK 620 4 CYS G 403 SG 117.8 112.1 103.6
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 G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 502
DBREF 4ORH A 1 145 UNP Q15819 UB2V2_HUMAN 1 145
DBREF 4ORH B 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4ORH C 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4ORH E 1 145 UNP Q15819 UB2V2_HUMAN 1 145
DBREF 4ORH F 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4ORH G 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4ORH H 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4ORH I 1 145 UNP Q15819 UB2V2_HUMAN 1 145
DBREF 4ORH J 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 4ORH K 345 485 UNP O76064 RNF8_HUMAN 345 485
DBREF 4ORH L 345 485 UNP O76064 RNF8_HUMAN 345 485
SEQADV 4ORH GLY A -7 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PRO A -6 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH LEU A -5 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLY A -4 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH SER A -3 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PRO A -2 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLU A -1 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PHE A 0 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLY B -7 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PRO B -6 UNP P61088 EXPRESSION TAG
SEQADV 4ORH LEU B -5 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLY B -4 UNP P61088 EXPRESSION TAG
SEQADV 4ORH SER B -3 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PRO B -2 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLU B -1 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PHE B 0 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLY C 337 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO C 338 UNP O76064 EXPRESSION TAG
SEQADV 4ORH LEU C 339 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY C 340 UNP O76064 EXPRESSION TAG
SEQADV 4ORH SER C 341 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO C 342 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLU C 343 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PHE C 344 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY E -7 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PRO E -6 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH LEU E -5 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLY E -4 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH SER E -3 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PRO E -2 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLU E -1 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PHE E 0 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLY F -7 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PRO F -6 UNP P61088 EXPRESSION TAG
SEQADV 4ORH LEU F -5 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLY F -4 UNP P61088 EXPRESSION TAG
SEQADV 4ORH SER F -3 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PRO F -2 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLU F -1 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PHE F 0 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLY G 337 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO G 338 UNP O76064 EXPRESSION TAG
SEQADV 4ORH LEU G 339 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY G 340 UNP O76064 EXPRESSION TAG
SEQADV 4ORH SER G 341 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO G 342 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLU G 343 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PHE G 344 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY H 337 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO H 338 UNP O76064 EXPRESSION TAG
SEQADV 4ORH LEU H 339 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY H 340 UNP O76064 EXPRESSION TAG
SEQADV 4ORH SER H 341 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO H 342 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLU H 343 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PHE H 344 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY I -7 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PRO I -6 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH LEU I -5 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLY I -4 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH SER I -3 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PRO I -2 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLU I -1 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH PHE I 0 UNP Q15819 EXPRESSION TAG
SEQADV 4ORH GLY J -7 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PRO J -6 UNP P61088 EXPRESSION TAG
SEQADV 4ORH LEU J -5 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLY J -4 UNP P61088 EXPRESSION TAG
SEQADV 4ORH SER J -3 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PRO J -2 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLU J -1 UNP P61088 EXPRESSION TAG
SEQADV 4ORH PHE J 0 UNP P61088 EXPRESSION TAG
SEQADV 4ORH GLY K 337 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO K 338 UNP O76064 EXPRESSION TAG
SEQADV 4ORH LEU K 339 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY K 340 UNP O76064 EXPRESSION TAG
SEQADV 4ORH SER K 341 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO K 342 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLU K 343 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PHE K 344 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY L 337 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO L 338 UNP O76064 EXPRESSION TAG
SEQADV 4ORH LEU L 339 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLY L 340 UNP O76064 EXPRESSION TAG
SEQADV 4ORH SER L 341 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PRO L 342 UNP O76064 EXPRESSION TAG
SEQADV 4ORH GLU L 343 UNP O76064 EXPRESSION TAG
SEQADV 4ORH PHE L 344 UNP O76064 EXPRESSION TAG
SEQRES 1 A 153 GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR
SEQRES 2 A 153 GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU
SEQRES 3 A 153 LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL
SEQRES 4 A 153 SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR
SEQRES 5 A 153 ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN
SEQRES 6 A 153 TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY
SEQRES 7 A 153 PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL
SEQRES 8 A 153 THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY
SEQRES 9 A 153 MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP
SEQRES 10 A 153 GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU
SEQRES 11 A 153 ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO
SEQRES 12 A 153 GLN PRO PRO GLU GLY GLN THR TYR ASN ASN
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 CYS 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 E 153 GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR
SEQRES 2 E 153 GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU
SEQRES 3 E 153 LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL
SEQRES 4 E 153 SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR
SEQRES 5 E 153 ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN
SEQRES 6 E 153 TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY
SEQRES 7 E 153 PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL
SEQRES 8 E 153 THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY
SEQRES 9 E 153 MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP
SEQRES 10 E 153 GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU
SEQRES 11 E 153 ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO
SEQRES 12 E 153 GLN PRO PRO GLU GLY GLN THR TYR ASN ASN
SEQRES 1 F 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 F 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 F 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 F 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 F 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 F 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 F 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 F 160 GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 F 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 F 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 F 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 F 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 F 160 MET ASN ASN ILE
SEQRES 1 G 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 G 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 G 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 G 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 G 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 G 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 G 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 G 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 G 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 G 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 G 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 G 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 H 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 H 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 H 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 H 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 H 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 H 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 H 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 H 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 H 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 H 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 H 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 H 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 I 153 GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR
SEQRES 2 I 153 GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU
SEQRES 3 I 153 LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL
SEQRES 4 I 153 SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR
SEQRES 5 I 153 ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN
SEQRES 6 I 153 TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY
SEQRES 7 I 153 PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL
SEQRES 8 I 153 THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY
SEQRES 9 I 153 MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP
SEQRES 10 I 153 GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU
SEQRES 11 I 153 ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO
SEQRES 12 I 153 GLN PRO PRO GLU GLY GLN THR TYR ASN ASN
SEQRES 1 J 160 GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO
SEQRES 2 J 160 ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU
SEQRES 3 J 160 PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN
SEQRES 4 J 160 ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP
SEQRES 5 J 160 SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE
SEQRES 6 J 160 LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG
SEQRES 7 J 160 PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU
SEQRES 8 J 160 GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER
SEQRES 9 J 160 PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN
SEQRES 10 J 160 ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA
SEQRES 11 J 160 ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN
SEQRES 12 J 160 ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA
SEQRES 13 J 160 MET ASN ASN ILE
SEQRES 1 K 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 K 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 K 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 K 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 K 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 K 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 K 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 K 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 K 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 K 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 K 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 K 149 LYS ALA LYS ARG LEU PHE
SEQRES 1 L 149 GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA
SEQRES 2 L 149 LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU
SEQRES 3 L 149 ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR
SEQRES 4 L 149 LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU
SEQRES 5 L 149 VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU
SEQRES 6 L 149 GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL
SEQRES 7 L 149 THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE
SEQRES 8 L 149 ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS
SEQRES 9 L 149 ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU
SEQRES 10 L 149 ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER
SEQRES 11 L 149 GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG
SEQRES 12 L 149 LYS ALA LYS ARG LEU PHE
HET ZN C 501 1
HET ZN C 502 1
HET ZN G 501 1
HET ZN G 502 1
HET ZN H 501 1
HET ZN H 502 1
HET ZN K 501 1
HET ZN K 502 1
HET ZN L 501 1
HET ZN L 502 1
HETNAM ZN ZINC ION
FORMUL 12 ZN 10(ZN 2+)
HELIX 1 1 PRO A 10 GLY A 25 1 16
HELIX 2 2 ASP A 99 SER A 102 5 4
HELIX 3 3 ILE A 103 LYS A 108 1 6
HELIX 4 4 SER A 114 MET A 127 1 14
HELIX 5 5 SER A 128 LYS A 133 1 6
HELIX 6 6 PRO B 5 GLU B 18 1 14
HELIX 7 7 LEU B 88 LYS B 92 5 5
HELIX 8 8 GLN B 100 ALA B 114 1 15
HELIX 9 9 ASP B 124 ASN B 132 1 9
HELIX 10 10 ASN B 132 ALA B 148 1 17
HELIX 11 11 MET C 393 LEU C 397 1 5
HELIX 12 12 SER C 424 LYS C 434 1 11
HELIX 13 13 SER C 450 ASN C 462 1 13
HELIX 14 14 SER C 465 ARG C 483 1 19
HELIX 15 15 PRO E 10 GLY E 25 1 16
HELIX 16 16 ASP E 99 SER E 102 5 4
HELIX 17 17 ILE E 103 LYS E 108 1 6
HELIX 18 18 SER E 114 MET E 127 1 14
HELIX 19 19 SER E 128 LYS E 133 1 6
HELIX 20 20 PRO F 5 GLU F 18 1 14
HELIX 21 21 LEU F 88 LYS F 92 5 5
HELIX 22 22 GLN F 100 ALA F 114 1 15
HELIX 23 23 ASP F 124 ASN F 132 1 9
HELIX 24 24 ASN F 132 ALA F 148 1 17
HELIX 25 25 GLU G 346 LEU G 401 1 56
HELIX 26 26 SER G 424 MET G 431 1 8
HELIX 27 27 SER G 450 ASN G 462 1 13
HELIX 28 28 SER G 465 ARG G 483 1 19
HELIX 29 29 GLU H 343 LEU H 397 1 55
HELIX 30 30 SER H 424 LYS H 434 1 11
HELIX 31 31 SER H 450 ASN H 462 1 13
HELIX 32 32 SER H 465 ARG H 483 1 19
HELIX 33 33 PRO I 10 GLY I 25 1 16
HELIX 34 34 ASP I 99 SER I 102 5 4
HELIX 35 35 ILE I 103 LYS I 108 1 6
HELIX 36 36 SER I 114 MET I 127 1 14
HELIX 37 37 SER I 128 LYS I 133 1 6
HELIX 38 38 PRO J 5 GLU J 18 1 14
HELIX 39 39 LEU J 88 LYS J 92 5 5
HELIX 40 40 GLN J 100 ALA J 114 1 15
HELIX 41 41 ASP J 124 ASN J 132 1 9
HELIX 42 42 ASN J 132 ALA J 148 1 17
HELIX 43 43 GLU K 346 LEU K 401 1 56
HELIX 44 44 SER K 424 MET K 431 1 8
HELIX 45 45 SER K 450 ASN K 462 1 13
HELIX 46 46 SER K 465 ARG K 483 1 19
HELIX 47 47 GLU L 343 ASN L 394 1 52
HELIX 48 48 SER L 424 LYS L 434 1 11
HELIX 49 49 SER L 450 ASN L 462 1 13
HELIX 50 50 SER L 465 ARG L 483 1 19
SHEET 1 A 4 VAL A 31 LEU A 35 0
SHEET 2 A 4 ARG A 45 ILE A 51 -1 O THR A 47 N GLY A 34
SHEET 3 A 4 ILE A 62 GLU A 68 -1 O TYR A 63 N ILE A 50
SHEET 4 A 4 SER A 79 PHE A 82 -1 O SER A 79 N GLU A 68
SHEET 1 B 4 ILE B 23 PRO B 27 0
SHEET 2 B 4 TYR B 34 ALA B 40 -1 O HIS B 36 N GLU B 26
SHEET 3 B 4 THR B 51 PHE B 57 -1 O LEU B 56 N PHE B 35
SHEET 4 B 4 LYS B 68 PHE B 71 -1 O LYS B 68 N PHE B 57
SHEET 1 C 3 SER C 421 CYS C 423 0
SHEET 2 C 3 ALA C 413 LEU C 416 -1 N VAL C 414 O PHE C 422
SHEET 3 C 3 LYS C 447 TYR C 449 -1 O THR C 448 N THR C 415
SHEET 1 D 4 VAL E 31 LEU E 35 0
SHEET 2 D 4 ARG E 45 ILE E 51 -1 O THR E 47 N GLY E 34
SHEET 3 D 4 ILE E 62 GLU E 68 -1 O TYR E 63 N ILE E 50
SHEET 4 D 4 SER E 79 PHE E 82 -1 O SER E 79 N GLU E 68
SHEET 1 E 4 ILE F 23 PRO F 27 0
SHEET 2 E 4 TYR F 34 ALA F 40 -1 O HIS F 36 N GLU F 26
SHEET 3 E 4 THR F 51 PHE F 57 -1 O LEU F 56 N PHE F 35
SHEET 4 E 4 LYS F 68 PHE F 71 -1 O LYS F 68 N PHE F 57
SHEET 1 F 3 SER G 421 CYS G 423 0
SHEET 2 F 3 ALA G 413 LEU G 416 -1 N VAL G 414 O PHE G 422
SHEET 3 F 3 LYS G 447 TYR G 449 -1 O THR G 448 N THR G 415
SHEET 1 G 3 SER H 421 CYS H 423 0
SHEET 2 G 3 ALA H 413 LEU H 416 -1 N VAL H 414 O PHE H 422
SHEET 3 G 3 LYS H 447 TYR H 449 -1 O THR H 448 N THR H 415
SHEET 1 H 4 VAL I 31 LEU I 35 0
SHEET 2 H 4 ARG I 45 ILE I 51 -1 O THR I 47 N GLY I 34
SHEET 3 H 4 ILE I 62 GLU I 68 -1 O TYR I 63 N ILE I 50
SHEET 4 H 4 SER I 79 PHE I 82 -1 O SER I 79 N GLU I 68
SHEET 1 I 4 ILE J 23 PRO J 27 0
SHEET 2 I 4 TYR J 34 ALA J 40 -1 O HIS J 36 N GLU J 26
SHEET 3 I 4 THR J 51 PHE J 57 -1 O LEU J 56 N PHE J 35
SHEET 4 I 4 LYS J 68 PHE J 71 -1 O LYS J 68 N PHE J 57
SHEET 1 J 3 SER K 421 CYS K 423 0
SHEET 2 J 3 ALA K 413 LEU K 416 -1 N VAL K 414 O PHE K 422
SHEET 3 J 3 LYS K 447 TYR K 449 -1 O THR K 448 N THR K 415
SHEET 1 K 3 SER L 421 CYS L 423 0
SHEET 2 K 3 ALA L 413 LEU L 416 -1 N VAL L 414 O PHE L 422
SHEET 3 K 3 LYS L 447 TYR L 449 -1 O THR L 448 N THR L 415
LINK ND1 HIS K 420 ZN ZN K 501 1555 1555 2.07
LINK ND1 HIS G 420 ZN ZN G 501 1555 1555 2.07
LINK ND1 HIS C 420 ZN ZN C 501 1555 1555 2.22
LINK ND1 HIS L 420 ZN ZN L 501 1555 1555 2.22
LINK ND1 HIS H 420 ZN ZN H 501 1555 1555 2.22
LINK SG CYS H 418 ZN ZN H 501 1555 1555 2.23
LINK SG CYS C 418 ZN ZN C 501 1555 1555 2.23
LINK SG CYS L 418 ZN ZN L 501 1555 1555 2.23
LINK SG CYS L 440 ZN ZN L 501 1555 1555 2.24
LINK SG CYS C 440 ZN ZN C 501 1555 1555 2.24
LINK SG CYS H 440 ZN ZN H 501 1555 1555 2.24
LINK SG CYS C 426 ZN ZN C 502 1555 1555 2.28
LINK SG CYS H 426 ZN ZN H 502 1555 1555 2.28
LINK SG CYS L 426 ZN ZN L 502 1555 1555 2.28
LINK SG CYS K 440 ZN ZN K 501 1555 1555 2.30
LINK SG CYS G 440 ZN ZN G 501 1555 1555 2.30
LINK SG CYS G 418 ZN ZN G 501 1555 1555 2.30
LINK SG CYS K 418 ZN ZN K 501 1555 1555 2.30
LINK SG CYS C 406 ZN ZN C 502 1555 1555 2.31
LINK SG CYS H 406 ZN ZN H 502 1555 1555 2.31
LINK SG CYS L 406 ZN ZN L 502 1555 1555 2.31
LINK SG CYS G 437 ZN ZN G 501 1555 1555 2.32
LINK SG CYS K 437 ZN ZN K 501 1555 1555 2.32
LINK SG CYS L 437 ZN ZN L 501 1555 1555 2.32
LINK SG CYS H 437 ZN ZN H 501 1555 1555 2.32
LINK SG CYS C 437 ZN ZN C 501 1555 1555 2.32
LINK SG CYS K 426 ZN ZN K 502 1555 1555 2.32
LINK SG CYS G 426 ZN ZN G 502 1555 1555 2.32
LINK SG CYS K 406 ZN ZN K 502 1555 1555 2.32
LINK SG CYS G 406 ZN ZN G 502 1555 1555 2.32
LINK SG CYS L 403 ZN ZN L 502 1555 1555 2.33
LINK SG CYS H 403 ZN ZN H 502 1555 1555 2.33
LINK SG CYS C 403 ZN ZN C 502 1555 1555 2.33
LINK SG CYS H 423 ZN ZN H 502 1555 1555 2.35
LINK SG CYS L 423 ZN ZN L 502 1555 1555 2.35
LINK SG CYS C 423 ZN ZN C 502 1555 1555 2.35
LINK SG CYS G 423 ZN ZN G 502 1555 1555 2.39
LINK SG CYS K 423 ZN ZN K 502 1555 1555 2.39
LINK SG CYS K 403 ZN ZN K 502 1555 1555 2.40
LINK SG CYS G 403 ZN ZN G 502 1555 1555 2.40
CISPEP 1 TYR A 73 PRO A 74 0 -0.72
CISPEP 2 TYR B 62 PRO B 63 0 9.57
CISPEP 3 TYR E 73 PRO E 74 0 -0.72
CISPEP 4 TYR F 62 PRO F 63 0 9.51
CISPEP 5 TYR I 73 PRO I 74 0 -0.77
CISPEP 6 TYR J 62 PRO J 63 0 9.41
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 G 418 HIS G 420 CYS G 437 CYS G 440
SITE 1 AC4 4 CYS G 403 CYS G 406 CYS G 423 CYS G 426
SITE 1 AC5 4 CYS H 418 HIS H 420 CYS H 437 CYS H 440
SITE 1 AC6 4 CYS H 403 CYS H 406 CYS H 423 CYS H 426
SITE 1 AC7 4 CYS K 418 HIS K 420 CYS K 437 CYS K 440
SITE 1 AC8 4 CYS K 403 CYS K 406 CYS K 423 CYS K 426
SITE 1 AC9 4 CYS L 418 HIS L 420 CYS L 437 CYS L 440
SITE 1 BC1 4 CYS L 403 CYS L 406 CYS L 423 CYS L 426
CRYST1 205.258 205.258 235.372 90.00 90.00 90.00 P 42 21 2 40
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 0.004872 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004249 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
