HEADER LIGASE 26-MAY-09 3HL5
TITLE CRYSTAL STRUCTURE OF XIAP BIR3 WITH CS3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BIR3, UNP RESIDUES 256-346;
COMPND 5 SYNONYM: E3 UBIQUITIN-PROTEIN LIGASE XIAP, INHIBITOR OF APOPTOSIS
COMPND 6 PROTEIN 3, X-LINKED INHIBITOR OF APOPTOSIS PROTEIN, X-LINKED IAP,
COMPND 7 IAP-LIKE PROTEIN, HILP;
COMPND 8 EC: 6.3.2.-;
COMPND 9 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: API3, BIRC4, IAP3, XIAP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BIR, IAP, APOPTOSIS, SMALL MOLECULE DRUG DISCOVERY, STRUCTURE-BASED
KEYWDS 2 DRUG DESIGN, LIGASE, METAL-BINDING, PHOSPHOPROTEIN, PROTEASE
KEYWDS 3 INHIBITOR, THIOL PROTEASE INHIBITOR, UBL CONJUGATION PATHWAY, ZINC-
KEYWDS 4 FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.HYMOWITZ
REVDAT 4 06-SEP-23 3HL5 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 3HL5 1 VERSN
REVDAT 2 28-JUL-09 3HL5 1 JRNL
REVDAT 1 16-JUN-09 3HL5 0
JRNL AUTH C.NDUBAKU,E.VARFOLOMEEV,L.WANG,K.ZOBEL,K.LAU,L.O.ELLIOTT,
JRNL AUTH 2 B.MAURER,A.V.FEDOROVA,J.N.DYNEK,M.KOEHLER,S.G.HYMOWITZ,
JRNL AUTH 3 V.TSUI,K.DESHAYES,W.J.FAIRBROTHER,J.A.FLYGARE,D.VUCIC
JRNL TITL ANTAGONISM OF C-IAP AND XIAP PROTEINS IS REQUIRED FOR
JRNL TITL 2 EFFICIENT INDUCTION OF CELL DEATH BY SMALL-MOLECULE IAP
JRNL TITL 3 ANTAGONISTS.
JRNL REF ACS CHEM.BIOL. V. 4 557 2009
JRNL REFN ISSN 1554-8929
JRNL PMID 19492850
JRNL DOI 10.1021/CB900083M
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 16220
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1855
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 836
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71000
REMARK 3 B22 (A**2) : 1.25000
REMARK 3 B33 (A**2) : -0.55000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.993
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1645 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2226 ; 1.126 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 182 ; 4.413 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;32.983 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 248 ;12.769 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;14.463 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 210 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1292 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 761 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1115 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 120 ; 0.108 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 67 ; 0.152 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.117 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 934 ; 1.955 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1450 ; 2.979 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 845 ; 2.268 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 776 ; 3.469 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 256 A 346
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2673 14.8870 -9.6435
REMARK 3 T TENSOR
REMARK 3 T11: -0.0395 T22: -0.0088
REMARK 3 T33: -0.0455 T12: -0.0101
REMARK 3 T13: 0.0078 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.2218 L22: 0.7250
REMARK 3 L33: 0.5811 L12: 0.1179
REMARK 3 L13: 0.1481 L23: -0.0729
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: 0.0645 S13: 0.0739
REMARK 3 S21: -0.0563 S22: -0.0062 S23: -0.0088
REMARK 3 S31: -0.0630 S32: 0.0311 S33: 0.0234
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3HL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053268.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
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
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19119
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: CHAIN D FROM PDB ENTRY 1G73
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DROPS CONTAIN 2 UL PROTEIN AND 2 UL
REMARK 280 WELL SOLUTIONS. PROTEIN SOLUTION: 4 MG/ML IN 20 MM TRIS PH 8.3,
REMARK 280 200MM NAL. 2 MM CS3. WELL SOLUTION: 3.5 M NA FORMATE PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.95650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.95650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.97000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 38 LIES ON A SPECIAL POSITION.
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 252
REMARK 465 GLY B 252
REMARK 465 SER B 253
REMARK 465 HIS B 254
REMARK 465 MET B 255
REMARK 465 HIS B 346
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 HIS A 302 -65.74 -90.81
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 A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 300 SG
REMARK 620 2 CYS A 303 SG 107.5
REMARK 620 3 HIS A 320 NE2 99.2 116.5
REMARK 620 4 CYS A 327 SG 115.1 109.2 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 300 SG
REMARK 620 2 CYS B 303 SG 108.2
REMARK 620 3 HIS B 320 NE2 105.0 112.3
REMARK 620 4 CYS B 327 SG 114.5 111.0 105.6
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 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9JZ B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9JZ A 1
DBREF 3HL5 A 256 346 UNP P98170 XIAP_HUMAN 256 346
DBREF 3HL5 B 256 346 UNP P98170 XIAP_HUMAN 256 346
SEQADV 3HL5 GLY A 252 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 SER A 253 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 HIS A 254 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 MET A 255 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 GLY B 252 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 SER B 253 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 HIS B 254 UNP P98170 EXPRESSION TAG
SEQADV 3HL5 MET B 255 UNP P98170 EXPRESSION TAG
SEQRES 1 A 95 GLY SER HIS MET LEU PRO ARG ASN PRO SER MET ALA ASP
SEQRES 2 A 95 TYR GLU ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR
SEQRES 3 A 95 SER VAL ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR
SEQRES 4 A 95 ALA LEU GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS
SEQRES 5 A 95 GLY GLY GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO
SEQRES 6 A 95 TRP GLU GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR
SEQRES 7 A 95 LEU LEU GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE
SEQRES 8 A 95 HIS LEU THR HIS
SEQRES 1 B 95 GLY SER HIS MET LEU PRO ARG ASN PRO SER MET ALA ASP
SEQRES 2 B 95 TYR GLU ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR
SEQRES 3 B 95 SER VAL ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR
SEQRES 4 B 95 ALA LEU GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS
SEQRES 5 B 95 GLY GLY GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO
SEQRES 6 B 95 TRP GLU GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR
SEQRES 7 B 95 LEU LEU GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE
SEQRES 8 B 95 HIS LEU THR HIS
HET ZN A 502 1
HET 9JZ A 1 37
HET ZN B 502 1
HET 9JZ B 1 37
HETNAM ZN ZINC ION
HETNAM 9JZ (3S)-1-{(2S)-2-CYCLOHEXYL-2-[(N-METHYL-L-ALANYL)
HETNAM 2 9JZ AMINO]ACETYL}-3-METHYL-N-(2-PYRIMIDIN-2-YLPHENYL)-L-
HETNAM 3 9JZ PROLINAMIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 9JZ 2(C28 H38 N6 O3)
FORMUL 7 HOH *146(H2 O)
HELIX 1 1 ASN A 259 ALA A 263 5 5
HELIX 2 2 ASP A 264 THR A 271 1 8
HELIX 3 3 ASN A 280 ALA A 287 1 8
HELIX 4 4 ASP A 315 TYR A 324 1 10
HELIX 5 5 CYS A 327 LYS A 334 1 8
HELIX 6 6 GLY A 335 HIS A 343 1 9
HELIX 7 7 ASN B 259 ALA B 263 5 5
HELIX 8 8 ASP B 264 GLY B 273 1 10
HELIX 9 9 ASN B 280 ALA B 287 1 8
HELIX 10 10 ASP B 315 TYR B 324 1 10
HELIX 11 11 CYS B 327 GLY B 335 1 9
HELIX 12 12 GLY B 335 LEU B 344 1 10
SHEET 1 A 3 PHE A 289 ALA A 291 0
SHEET 2 A 3 VAL A 298 CYS A 300 -1 O LYS A 299 N TYR A 290
SHEET 3 A 3 GLY A 306 LEU A 307 -1 O LEU A 307 N VAL A 298
SHEET 1 B 3 PHE B 289 ALA B 291 0
SHEET 2 B 3 VAL B 298 CYS B 300 -1 O LYS B 299 N TYR B 290
SHEET 3 B 3 GLY B 306 LEU B 307 -1 O LEU B 307 N VAL B 298
LINK SG CYS A 300 ZN ZN A 502 1555 1555 2.34
LINK SG CYS A 303 ZN ZN A 502 1555 1555 2.33
LINK NE2 HIS A 320 ZN ZN A 502 1555 1555 2.14
LINK SG CYS A 327 ZN ZN A 502 1555 1555 2.34
LINK SG CYS B 300 ZN ZN B 502 1555 1555 2.33
LINK SG CYS B 303 ZN ZN B 502 1555 1555 2.33
LINK NE2 HIS B 320 ZN ZN B 502 1555 1555 2.05
LINK SG CYS B 327 ZN ZN B 502 1555 1555 2.32
CISPEP 1 LEU B 256 PRO B 257 0 0.31
SITE 1 AC1 4 CYS A 300 CYS A 303 HIS A 320 CYS A 327
SITE 1 AC2 4 CYS B 300 CYS B 303 HIS B 320 CYS B 327
SITE 1 AC3 16 9JZ A 1 HOH A 141 LYS A 322 TRP A 323
SITE 2 AC3 16 PRO A 325 HIS A 346 HOH B 55 GLY B 306
SITE 3 AC3 16 LEU B 307 THR B 308 ASP B 309 TRP B 310
SITE 4 AC3 16 GLU B 314 GLN B 319 TRP B 323 TYR B 324
SITE 1 AC4 12 HOH A 159 GLY A 306 LEU A 307 THR A 308
SITE 2 AC4 12 ASP A 309 GLU A 314 GLN A 319 LYS A 322
SITE 3 AC4 12 TRP A 323 TYR A 324 9JZ B 1 ASP B 309
CRYST1 103.913 39.940 49.929 90.00 100.00 90.00 C 1 2 1 8
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 0.009623 0.000000 0.001698 0.00000
SCALE2 0.000000 0.025038 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020338 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
