HEADER LIGASE/LIGASE INHIBITOR 13-NOV-12 4HY5
TITLE CRYSTAL STRUCTURE OF CIAP1 BIR3 BOUND TO T3256336
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BIR3;
COMPND 5 SYNONYM: C-IAP1, IAP HOMOLOG B, INHIBITOR OF APOPTOSIS PROTEIN 2,
COMPND 6 IAP-2, HIAP-2, HIAP2, RING FINGER PROTEIN 48, TNFR2-TRAF-SIGNALING
COMPND 7 COMPLEX PROTEIN 2;
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: API1, BIRC2, IAP2, MIHB, RNF48;
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: PET28
KEYWDS IAP FAMILY, BIR REPEATS, CARD DOMAIN, RING-TYPE ZINC FINGER, LIGASE-
KEYWDS 2 LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.DOUGAN,G.P.SNELL
REVDAT 5 28-FEB-24 4HY5 1 REMARK SEQADV LINK
REVDAT 4 09-SEP-15 4HY5 1 AUTHOR
REVDAT 3 07-AUG-13 4HY5 1 HEADER HETATM REMARK
REVDAT 2 27-FEB-13 4HY5 1 JRNL
REVDAT 1 30-JAN-13 4HY5 0
JRNL AUTH K.HASHIMOTO,B.SAITO,N.MIYAMOTO,Y.OGURO,D.TOMITA,Z.SHIOKAWA,
JRNL AUTH 2 M.ASANO,H.KAKEI,N.TAYA,M.KAWASAKI,H.SUMI,M.YABUKI,K.IWAI,
JRNL AUTH 3 S.YOSHIDA,M.YOSHIMATSU,K.AOYAMA,Y.KOSUGI,T.KOJIMA,
JRNL AUTH 4 N.MORISHITA,D.R.DOUGAN,G.P.SNELL,S.IMAMURA,T.ISHIKAWA
JRNL TITL DESIGN AND SYNTHESIS OF POTENT INHIBITOR OF APOPTOSIS (IAP)
JRNL TITL 2 PROTEINS ANTAGONISTS BEARING AN
JRNL TITL 3 OCTAHYDROPYRROLO[1,2-A]PYRAZINE SCAFFOLD AS A NOVEL PROLINE
JRNL TITL 4 MIMETIC.
JRNL REF J.MED.CHEM. V. 56 1228 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23298277
JRNL DOI 10.1021/JM301674Z
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 24700
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1317
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1288
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1512
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.90000
REMARK 3 B22 (A**2) : -0.98000
REMARK 3 B33 (A**2) : 1.88000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.606
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1675 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6 ; 0.621 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2271 ; 1.242 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10 ;26.710 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 183 ; 4.321 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;33.407 ;22.727
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 256 ;13.511 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 217 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1315 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5 ; 0.063 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 252 A 346
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4251 17.9274 26.5793
REMARK 3 T TENSOR
REMARK 3 T11: 0.0300 T22: 0.0146
REMARK 3 T33: 0.0445 T12: -0.0085
REMARK 3 T13: -0.0214 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.4727 L22: 4.0453
REMARK 3 L33: 3.0779 L12: 0.2315
REMARK 3 L13: 0.8596 L23: 2.3858
REMARK 3 S TENSOR
REMARK 3 S11: -0.1092 S12: 0.0472 S13: 0.0806
REMARK 3 S21: -0.1671 S22: 0.0023 S23: 0.0753
REMARK 3 S31: -0.0329 S32: -0.0798 S33: 0.1069
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 257 B 346
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0707 -6.2676 12.0859
REMARK 3 T TENSOR
REMARK 3 T11: 0.0530 T22: 0.0763
REMARK 3 T33: 0.0367 T12: 0.0044
REMARK 3 T13: -0.0179 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 2.0009 L22: 4.5434
REMARK 3 L33: 4.0470 L12: 0.0695
REMARK 3 L13: -0.5058 L23: 3.3632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: 0.2165 S13: -0.0768
REMARK 3 S21: -0.1211 S22: -0.1468 S23: 0.1113
REMARK 3 S31: -0.3458 S32: -0.1629 S33: 0.1717
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4HY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27152
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M NACL 100MM TRIS, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 15.55300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.15500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.08800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.15500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 15.55300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.08800
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 232
REMARK 465 GLY A 233
REMARK 465 SER A 234
REMARK 465 SER A 235
REMARK 465 HIS A 236
REMARK 465 HIS A 237
REMARK 465 HIS A 238
REMARK 465 HIS A 239
REMARK 465 HIS A 240
REMARK 465 HIS A 241
REMARK 465 SER A 242
REMARK 465 SER A 243
REMARK 465 GLY A 244
REMARK 465 GLU A 245
REMARK 465 ASN A 246
REMARK 465 LEU A 247
REMARK 465 TYR A 248
REMARK 465 PHE A 249
REMARK 465 GLN A 250
REMARK 465 GLY A 251
REMARK 465 MET B 232
REMARK 465 GLY B 233
REMARK 465 SER B 234
REMARK 465 SER B 235
REMARK 465 HIS B 236
REMARK 465 HIS B 237
REMARK 465 HIS B 238
REMARK 465 HIS B 239
REMARK 465 HIS B 240
REMARK 465 HIS B 241
REMARK 465 SER B 242
REMARK 465 SER B 243
REMARK 465 GLY B 244
REMARK 465 GLU B 245
REMARK 465 ASN B 246
REMARK 465 LEU B 247
REMARK 465 TYR B 248
REMARK 465 PHE B 249
REMARK 465 GLN B 250
REMARK 465 GLY B 251
REMARK 465 GLY B 252
REMARK 465 SER B 253
REMARK 465 SER B 254
REMARK 465 ILE B 255
REMARK 465 SER B 256
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
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 ASN A 295 -125.17 48.42
REMARK 500 ASN B 295 -123.24 51.20
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 300 SG
REMARK 620 2 CYS A 303 SG 108.4
REMARK 620 3 HIS A 320 NE2 101.4 114.4
REMARK 620 4 CYS A 327 SG 114.9 109.1 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 300 SG
REMARK 620 2 CYS B 303 SG 109.4
REMARK 620 3 HIS B 320 NE2 99.9 116.9
REMARK 620 4 CYS B 327 SG 114.7 108.8 107.1
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ANTAGONIST
REMARK 630 MOLECULE NAME: (3S,7R,8AR)-2-{(2S)-2-(4,4-DIFLUOROCYCLOHEXYL)-2-
REMARK 630 [(N-METHYL-L-ALANYL)AMINO]ACETYL}-N-[(4R)-3,4-DIHYDRO-2H-CHROMEN-4-
REMARK 630 YL]-7-ETHOXYOCTAHYDROPYRROLO[1,2-A]PYRAZINE-3-CARBOXAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 1AQ A 402
REMARK 630 1AQ B 402
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: MAA 1Y2 1Y3 1XY
REMARK 630 DETAILS: NULL
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AQ A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AQ B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HY4 RELATED DB: PDB
REMARK 900 SAME PROTEIN(CIAP)COMPLEXED WITH A DIFFERENT LIGAND.(T3170284)
REMARK 900 RELATED ID: 4HY0 RELATED DB: PDB
REMARK 900 REALTED PROTEIN(XIAP)IN COMPLEX WITH SAME LIGAND.(T3256336)
DBREF 4HY5 A 234 346 UNP Q13490 BIRC2_HUMAN 238 352
DBREF 4HY5 B 234 346 UNP Q13490 BIRC2_HUMAN 238 352
SEQADV 4HY5 MET A 232 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 GLY A 233 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 SER A 235 UNP Q13490 GLU 239 CONFLICT
SEQADV 4HY5 HIS A 237 UNP Q13490 ARG 241 CONFLICT
SEQADV 4HY5 HIS A 238 UNP Q13490 ARG 242 CONFLICT
SEQADV 4HY5 A UNP Q13490 PHE 244 DELETION
SEQADV 4HY5 A UNP Q13490 PRO 245 DELETION
SEQADV 4HY5 A UNP Q13490 ASN 246 DELETION
SEQADV 4HY5 A UNP Q13490 CYS 247 DELETION
SEQADV 4HY5 A UNP Q13490 PRO 248 DELETION
SEQADV 4HY5 A UNP Q13490 PHE 249 DELETION
SEQADV 4HY5 HIS A 240 UNP Q13490 LEU 250 CONFLICT
SEQADV 4HY5 HIS A 241 UNP Q13490 GLU 251 CONFLICT
SEQADV 4HY5 SER A 242 UNP Q13490 ASN 252 CONFLICT
SEQADV 4HY5 GLY A 244 UNP Q13490 LEU 254 CONFLICT
SEQADV 4HY5 ASN A 246 UNP Q13490 THR 256 CONFLICT
SEQADV 4HY5 TYR A 248 UNP Q13490 ARG 258 CONFLICT
SEQADV 4HY5 GLN A 250 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 GLY A 251 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 GLY A 252 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 SER A 253 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 MET B 232 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 GLY B 233 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 SER B 235 UNP Q13490 GLU 239 CONFLICT
SEQADV 4HY5 HIS B 237 UNP Q13490 ARG 241 CONFLICT
SEQADV 4HY5 HIS B 238 UNP Q13490 ARG 242 CONFLICT
SEQADV 4HY5 B UNP Q13490 PHE 244 DELETION
SEQADV 4HY5 B UNP Q13490 PRO 245 DELETION
SEQADV 4HY5 B UNP Q13490 ASN 246 DELETION
SEQADV 4HY5 B UNP Q13490 CYS 247 DELETION
SEQADV 4HY5 B UNP Q13490 PRO 248 DELETION
SEQADV 4HY5 B UNP Q13490 PHE 249 DELETION
SEQADV 4HY5 HIS B 240 UNP Q13490 LEU 250 CONFLICT
SEQADV 4HY5 HIS B 241 UNP Q13490 GLU 251 CONFLICT
SEQADV 4HY5 SER B 242 UNP Q13490 ASN 252 CONFLICT
SEQADV 4HY5 GLY B 244 UNP Q13490 LEU 254 CONFLICT
SEQADV 4HY5 ASN B 246 UNP Q13490 THR 256 CONFLICT
SEQADV 4HY5 TYR B 248 UNP Q13490 ARG 258 CONFLICT
SEQADV 4HY5 GLN B 250 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 GLY B 251 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 GLY B 252 UNP Q13490 EXPRESSION TAG
SEQADV 4HY5 SER B 253 UNP Q13490 EXPRESSION TAG
SEQRES 1 A 115 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 115 GLU ASN LEU TYR PHE GLN GLY GLY SER SER ILE SER ASN
SEQRES 3 A 115 LEU SER MET GLN THR HIS ALA ALA ARG MET ARG THR PHE
SEQRES 4 A 115 MET TYR TRP PRO SER SER VAL PRO VAL GLN PRO GLU GLN
SEQRES 5 A 115 LEU ALA SER ALA GLY PHE TYR TYR VAL GLY ARG ASN ASP
SEQRES 6 A 115 ASP VAL LYS CYS PHE CYS CYS ASP GLY GLY LEU ARG CYS
SEQRES 7 A 115 TRP GLU SER GLY ASP ASP PRO TRP VAL GLU HIS ALA LYS
SEQRES 8 A 115 TRP PHE PRO ARG CYS GLU PHE LEU ILE ARG MET LYS GLY
SEQRES 9 A 115 GLN GLU PHE VAL ASP GLU ILE GLN GLY ARG TYR
SEQRES 1 B 115 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 115 GLU ASN LEU TYR PHE GLN GLY GLY SER SER ILE SER ASN
SEQRES 3 B 115 LEU SER MET GLN THR HIS ALA ALA ARG MET ARG THR PHE
SEQRES 4 B 115 MET TYR TRP PRO SER SER VAL PRO VAL GLN PRO GLU GLN
SEQRES 5 B 115 LEU ALA SER ALA GLY PHE TYR TYR VAL GLY ARG ASN ASP
SEQRES 6 B 115 ASP VAL LYS CYS PHE CYS CYS ASP GLY GLY LEU ARG CYS
SEQRES 7 B 115 TRP GLU SER GLY ASP ASP PRO TRP VAL GLU HIS ALA LYS
SEQRES 8 B 115 TRP PHE PRO ARG CYS GLU PHE LEU ILE ARG MET LYS GLY
SEQRES 9 B 115 GLN GLU PHE VAL ASP GLU ILE GLN GLY ARG TYR
HET ZN A 401 1
HET 1AQ A 402 43
HET ZN B 401 1
HET 1AQ B 402 43
HETNAM ZN ZINC ION
HETNAM 1AQ (3S,7R,8AR)-2-{(2S)-2-(4,4-DIFLUOROCYCLOHEXYL)-2-[(N-
HETNAM 2 1AQ METHYL-L-ALANYL)AMINO]ACETYL}-N-[(4R)-3,4-DIHYDRO-2H-
HETNAM 3 1AQ CHROMEN-4-YL]-7-ETHOXYOCTAHYDROPYRROLO[1,2-A]PYRAZINE-
HETNAM 4 1AQ 3-CARBOXAMIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 1AQ 2(C31 H45 F2 N5 O5)
FORMUL 7 HOH *166(H2 O)
HELIX 1 1 ASN A 257 GLN A 261 5 5
HELIX 2 2 THR A 262 THR A 269 1 8
HELIX 3 3 PHE A 270 TRP A 273 5 4
HELIX 4 4 GLN A 280 ALA A 287 1 8
HELIX 5 5 ASP A 315 PHE A 324 1 10
HELIX 6 6 CYS A 327 GLY A 335 1 9
HELIX 7 7 GLY A 335 GLY A 344 1 10
HELIX 8 8 ARG A 345 TYR A 346 5 2
HELIX 9 9 ASN B 257 GLN B 261 5 5
HELIX 10 10 THR B 262 THR B 269 1 8
HELIX 11 11 PHE B 270 TRP B 273 5 4
HELIX 12 12 GLN B 280 ALA B 287 1 8
HELIX 13 13 ASP B 315 PHE B 324 1 10
HELIX 14 14 CYS B 327 GLY B 335 1 9
HELIX 15 15 GLY B 335 GLN B 343 1 9
SHEET 1 A 3 PHE A 289 TYR 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 TYR 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 401 1555 1555 2.32
LINK SG CYS A 303 ZN ZN A 401 1555 1555 2.35
LINK NE2 HIS A 320 ZN ZN A 401 1555 1555 2.04
LINK SG CYS A 327 ZN ZN A 401 1555 1555 2.32
LINK SG CYS B 300 ZN ZN B 401 1555 1555 2.34
LINK SG CYS B 303 ZN ZN B 401 1555 1555 2.33
LINK NE2 HIS B 320 ZN ZN B 401 1555 1555 2.07
LINK SG CYS B 327 ZN ZN B 401 1555 1555 2.31
SITE 1 AC1 4 CYS A 300 CYS A 303 HIS A 320 CYS A 327
SITE 1 AC2 12 ASP A 297 GLY A 306 LEU A 307 ARG A 308
SITE 2 AC2 12 CYS A 309 GLU A 311 ASP A 314 GLU A 319
SITE 3 AC2 12 TRP A 323 HOH A 550 HOH A 553 HOH A 589
SITE 1 AC3 4 CYS B 300 CYS B 303 HIS B 320 CYS B 327
SITE 1 AC4 17 MET A 267 PHE A 270 LEU B 258 GLN B 261
SITE 2 AC4 17 THR B 262 GLY B 306 LEU B 307 ARG B 308
SITE 3 AC4 17 CYS B 309 TRP B 310 GLU B 311 ASP B 314
SITE 4 AC4 17 GLU B 319 TRP B 323 HOH B 547 HOH B 549
SITE 5 AC4 17 HOH B 560
CRYST1 31.106 68.176 122.310 90.00 90.00 90.00 P 21 21 21 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 0.032148 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
