HEADER LIGASE 09-DEC-12 4IC3
TITLE CRYSTAL STRUCTURE OF THE F495L MUTANT XIAP RING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE XIAP;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RING DOMAIN, UNP RESIDUES 429-497;
COMPND 5 SYNONYM: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 4, IAP-LIKE
COMPND 6 PROTEIN, ILP, HILP, INHIBITOR OF APOPTOSIS PROTEIN 3, IAP-3, HIAP-3,
COMPND 7 HIAP3, X-LINKED INHIBITOR OF APOPTOSIS PROTEIN, X-LINKED IAP;
COMPND 8 EC: 6.3.2.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: API3, BIR4, IAP3, XIAP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P3
KEYWDS RING DOMAIN, ZINC-FINGER, E3 LIGASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAKATANI,C.L.DAY
REVDAT 3 08-NOV-23 4IC3 1 REMARK SEQADV LINK
REVDAT 2 10-JUL-13 4IC3 1 JRNL
REVDAT 1 19-DEC-12 4IC3 0
JRNL AUTH Y.NAKATANI,T.KLEFFMANN,K.LINKE,S.M.CONDON,M.G.HINDS,C.L.DAY
JRNL TITL REGULATION OF UBIQUITIN TRANSFER BY XIAP, A DIMERIC RING E3
JRNL TITL 2 LIGASE
JRNL REF BIOCHEM.J. V. 450 629 2013
JRNL REFN ISSN 0264-6021
JRNL PMID 23259674
JRNL DOI 10.1042/BJ20121702
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 12946
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 632
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 18.3417 - 3.0445 1.00 2532 122 0.1782 0.2185
REMARK 3 2 3.0445 - 2.4183 1.00 2465 132 0.1755 0.2202
REMARK 3 3 2.4183 - 2.1131 1.00 2463 127 0.1637 0.2109
REMARK 3 4 2.1131 - 1.9201 1.00 2460 134 0.1706 0.2388
REMARK 3 5 1.9201 - 1.7826 0.97 2394 117 0.1985 0.2317
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 : 0.38
REMARK 3 B_SOL : 61.29
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.13660
REMARK 3 B22 (A**2) : -1.88040
REMARK 3 B33 (A**2) : 4.01700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.84070
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 1046
REMARK 3 ANGLE : 1.085 1408
REMARK 3 CHIRALITY : 0.079 168
REMARK 3 PLANARITY : 0.006 172
REMARK 3 DIHEDRAL : 13.800 411
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4IC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076566.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12946
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 18.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.49600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: PDB ENTRY 3EB5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL, 20% MME PEG2000, 10MM
REMARK 280 NICL2, 1MM TCEP, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 24.23550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 424
REMARK 465 PRO A 425
REMARK 465 LEU A 426
REMARK 465 GLY A 427
REMARK 465 SER A 428
REMARK 465 THR A 429
REMARK 465 SER A 430
REMARK 465 LEU A 431
REMARK 465 GLN A 432
REMARK 465 LYS A 433
REMARK 465 SER A 497
REMARK 465 GLY B 424
REMARK 465 PRO B 425
REMARK 465 LEU B 426
REMARK 465 GLY B 427
REMARK 465 SER B 428
REMARK 465 THR B 429
REMARK 465 SER B 430
REMARK 465 LEU B 431
REMARK 465 GLN B 432
REMARK 465 LYS B 433
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 MET B 454 26.22 49.82
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 A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 450 SG
REMARK 620 2 CYS A 453 SG 107.1
REMARK 620 3 CYS A 471 SG 111.6 117.0
REMARK 620 4 CYS A 474 SG 110.0 110.1 101.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A1003 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 455 OD1
REMARK 620 2 ASP A 455 OD2 49.2
REMARK 620 3 HOH A1118 O 81.6 114.9
REMARK 620 4 HOH A1120 O 95.9 60.9 91.8
REMARK 620 5 HOH A1145 O 87.7 86.6 137.6 130.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 465 SG
REMARK 620 2 HIS A 467 ND1 112.2
REMARK 620 3 CYS A 481 SG 106.6 109.8
REMARK 620 4 CYS A 484 SG 108.4 107.7 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 450 SG
REMARK 620 2 CYS B 453 SG 108.3
REMARK 620 3 CYS B 471 SG 114.4 112.6
REMARK 620 4 CYS B 474 SG 106.6 110.7 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B1003 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 455 OD1
REMARK 620 2 HOH B1130 O 161.0
REMARK 620 3 HOH B1144 O 99.1 62.3
REMARK 620 4 HOH B1148 O 82.6 103.4 100.6
REMARK 620 5 HOH B1149 O 104.8 91.2 146.9 104.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 465 SG
REMARK 620 2 HIS B 467 ND1 108.1
REMARK 620 3 CYS B 481 SG 107.5 110.2
REMARK 620 4 CYS B 484 SG 108.3 110.4 112.2
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 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IC2 RELATED DB: PDB
DBREF 4IC3 A 429 497 UNP P98170 XIAP_HUMAN 429 497
DBREF 4IC3 B 429 497 UNP P98170 XIAP_HUMAN 429 497
SEQADV 4IC3 GLY A 424 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 PRO A 425 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 LEU A 426 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 GLY A 427 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 SER A 428 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 LEU A 495 UNP P98170 PHE 495 ENGINEERED MUTATION
SEQADV 4IC3 GLY B 424 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 PRO B 425 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 LEU B 426 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 GLY B 427 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 SER B 428 UNP P98170 EXPRESSION TAG
SEQADV 4IC3 LEU B 495 UNP P98170 PHE 495 ENGINEERED MUTATION
SEQRES 1 A 74 GLY PRO LEU GLY SER THR SER LEU GLN LYS GLU ILE SER
SEQRES 2 A 74 THR GLU GLU GLN LEU ARG ARG LEU GLN GLU GLU LYS LEU
SEQRES 3 A 74 CYS LYS ILE CYS MET ASP ARG ASN ILE ALA ILE VAL PHE
SEQRES 4 A 74 VAL PRO CYS GLY HIS LEU VAL THR CYS LYS GLN CYS ALA
SEQRES 5 A 74 GLU ALA VAL ASP LYS CYS PRO MET CYS TYR THR VAL ILE
SEQRES 6 A 74 THR PHE LYS GLN LYS ILE LEU MET SER
SEQRES 1 B 74 GLY PRO LEU GLY SER THR SER LEU GLN LYS GLU ILE SER
SEQRES 2 B 74 THR GLU GLU GLN LEU ARG ARG LEU GLN GLU GLU LYS LEU
SEQRES 3 B 74 CYS LYS ILE CYS MET ASP ARG ASN ILE ALA ILE VAL PHE
SEQRES 4 B 74 VAL PRO CYS GLY HIS LEU VAL THR CYS LYS GLN CYS ALA
SEQRES 5 B 74 GLU ALA VAL ASP LYS CYS PRO MET CYS TYR THR VAL ILE
SEQRES 6 B 74 THR PHE LYS GLN LYS ILE LEU MET SER
HET ZN A1001 1
HET ZN A1002 1
HET NI A1003 1
HET ZN B1001 1
HET ZN B1002 1
HET NI B1003 1
HETNAM ZN ZINC ION
HETNAM NI NICKEL (II) ION
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 NI 2(NI 2+)
FORMUL 9 HOH *94(H2 O)
HELIX 1 1 SER A 436 LYS A 448 1 13
HELIX 2 2 CYS A 471 GLU A 476 1 6
HELIX 3 3 SER B 436 LYS B 448 1 13
HELIX 4 4 CYS B 471 GLU B 476 1 6
SHEET 1 A 2 ILE A 460 VAL A 463 0
SHEET 2 A 2 PHE A 490 LYS A 493 -1 O GLN A 492 N VAL A 461
SHEET 1 B 2 ILE B 460 VAL B 463 0
SHEET 2 B 2 PHE B 490 LYS B 493 -1 O PHE B 490 N VAL B 463
LINK SG CYS A 450 ZN ZN A1001 1555 1555 2.35
LINK SG CYS A 453 ZN ZN A1001 1555 1555 2.31
LINK OD1 ASP A 455 NI NI A1003 1555 1555 2.59
LINK OD2 ASP A 455 NI NI A1003 1555 1555 2.71
LINK SG CYS A 465 ZN ZN A1002 1555 1555 2.35
LINK ND1 HIS A 467 ZN ZN A1002 1555 1555 2.01
LINK SG CYS A 471 ZN ZN A1001 1555 1555 2.35
LINK SG CYS A 474 ZN ZN A1001 1555 1555 2.33
LINK SG CYS A 481 ZN ZN A1002 1555 1555 2.32
LINK SG CYS A 484 ZN ZN A1002 1555 1555 2.33
LINK NI NI A1003 O HOH A1118 1555 1555 2.60
LINK NI NI A1003 O HOH A1120 1555 1555 2.63
LINK NI NI A1003 O HOH A1145 1555 1555 2.53
LINK SG CYS B 450 ZN ZN B1001 1555 1555 2.34
LINK SG CYS B 453 ZN ZN B1001 1555 1555 2.35
LINK OD1 ASP B 455 NI NI B1003 1555 1555 2.16
LINK SG CYS B 465 ZN ZN B1002 1555 1555 2.32
LINK ND1 HIS B 467 ZN ZN B1002 1555 1555 1.99
LINK SG CYS B 471 ZN ZN B1001 1555 1555 2.36
LINK SG CYS B 474 ZN ZN B1001 1555 1555 2.37
LINK SG CYS B 481 ZN ZN B1002 1555 1555 2.35
LINK SG CYS B 484 ZN ZN B1002 1555 1555 2.31
LINK NI NI B1003 O HOH B1130 1555 1555 2.56
LINK NI NI B1003 O HOH B1144 1555 1555 2.58
LINK NI NI B1003 O HOH B1148 1555 1555 2.26
LINK NI NI B1003 O HOH B1149 1555 1555 2.37
CISPEP 1 VAL A 463 PRO A 464 0 6.08
CISPEP 2 VAL B 463 PRO B 464 0 8.92
SITE 1 AC1 4 CYS A 450 CYS A 453 CYS A 471 CYS A 474
SITE 1 AC2 4 CYS A 465 HIS A 467 CYS A 481 CYS A 484
SITE 1 AC3 4 ASP A 455 HOH A1118 HOH A1120 HOH A1145
SITE 1 AC4 4 CYS B 450 CYS B 453 CYS B 471 CYS B 474
SITE 1 AC5 4 CYS B 465 HIS B 467 CYS B 481 CYS B 484
SITE 1 AC6 5 ASP B 455 HOH B1130 HOH B1144 HOH B1148
SITE 2 AC6 5 HOH B1149
CRYST1 35.735 48.471 39.967 90.00 97.47 90.00 P 1 21 1 4
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 0.027984 0.000000 0.003669 0.00000
SCALE2 0.000000 0.020631 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025235 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
