HEADER SIGNALING PROTEIN 10-NOV-17 6EXW
TITLE CRYSTAL STRUCTURE OF CIAP1-BIR3 IN COMPLEX WITH A COVALENTLY BOUND SM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: ZINC-FINGER PROTEIN;
COMPND 5 SYNONYM: CELLULAR INHIBITOR OF APOPTOSIS 1,C-IAP1,IAP HOMOLOG B,
COMPND 6 INHIBITOR OF APOPTOSIS PROTEIN 2,HIAP2,RING FINGER PROTEIN 48,RING-
COMPND 7 TYPE E3 UBIQUITIN TRANSFERASE BIRC2,TNFR2-TRAF-SIGNALING COMPLEX
COMPND 8 PROTEIN 2;
COMPND 9 EC: 2.3.2.27;
COMPND 10 ENGINEERED: YES;
COMPND 11 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: BIRC2, API1, MIHB, RNF48;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS ZINC FINGER MOTIF, SMAC-MIMETIC, PROTEIN-LIGAND COMPLEX, BIR DOMAIN,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CORTI,F.COSSU,M.MILANI,E.MASTRANGELO
REVDAT 3 17-JAN-24 6EXW 1 REMARK LINK
REVDAT 2 19-SEP-18 6EXW 1 JRNL
REVDAT 1 08-AUG-18 6EXW 0
JRNL AUTH A.CORTI,M.MILANI,D.LECIS,P.SENECI,M.DE ROSA,E.MASTRANGELO,
JRNL AUTH 2 F.COSSU
JRNL TITL STRUCTURE-BASED DESIGN AND MOLECULAR PROFILING OF
JRNL TITL 2 SMAC-MIMETICS SELECTIVE FOR CELLULAR IAPS.
JRNL REF FEBS J. V. 285 3286 2018
JRNL REFN ISSN 1742-4658
JRNL PMID 30055105
JRNL DOI 10.1111/FEBS.14616
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 14821
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 779
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1095
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.07000
REMARK 3 B22 (A**2) : -1.07000
REMARK 3 B33 (A**2) : 3.48000
REMARK 3 B12 (A**2) : -0.54000
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): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.141
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1738 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1549 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2346 ; 1.651 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3566 ; 0.866 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 226 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1967 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 457 ; 0.002 ; 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 : NULL
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 ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6EXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200007428.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939
REMARK 200 MONOCHROMATOR : CHANNEL CUT ESRF MONOCHROMATOR
REMARK 200 OPTICS : VERTICALLY BENDED MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15655
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 58.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55100
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: MOLREP
REMARK 200 STARTING MODEL: 3MUP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3350, 0.22 M MGCL2, 0.1M
REMARK 280 BISTRIS, PH 5.9, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 117.75133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.87567
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.87567
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.75133
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: 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 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 C 715 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 MET A 244
REMARK 465 GLU A 245
REMARK 465 ASN A 246
REMARK 465 SER A 247
REMARK 465 LEU A 248
REMARK 465 GLU A 249
REMARK 465 THR A 250
REMARK 465 LEU A 251
REMARK 465 ARG A 252
REMARK 465 PHE A 253
REMARK 465 GLN A 352
REMARK 465 LEU A 353
REMARK 465 LEU A 354
REMARK 465 SER A 355
REMARK 465 THR A 356
REMARK 465 SER A 357
REMARK 465 LEU A 358
REMARK 465 GLU A 359
REMARK 465 HIS A 360
REMARK 465 HIS A 361
REMARK 465 HIS A 362
REMARK 465 HIS A 363
REMARK 465 HIS A 364
REMARK 465 HIS A 365
REMARK 465 MET C 244
REMARK 465 GLU C 245
REMARK 465 ASN C 246
REMARK 465 SER C 247
REMARK 465 LEU C 248
REMARK 465 GLU C 249
REMARK 465 THR C 250
REMARK 465 LEU C 251
REMARK 465 ARG C 252
REMARK 465 LEU C 350
REMARK 465 GLU C 351
REMARK 465 GLN C 352
REMARK 465 LEU C 353
REMARK 465 LEU C 354
REMARK 465 SER C 355
REMARK 465 THR C 356
REMARK 465 SER C 357
REMARK 465 LEU C 358
REMARK 465 GLU C 359
REMARK 465 HIS C 360
REMARK 465 HIS C 361
REMARK 465 HIS C 362
REMARK 465 HIS C 363
REMARK 465 HIS C 364
REMARK 465 HIS C 365
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 PHE C 253 CG CD1 CD2 CE1 CE2 CZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG C 332 CD
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 LEU A 349 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG C 332 CG - CD - NE ANGL. DEV. = -22.0 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 -128.68 53.91
REMARK 500 CYS A 302 -61.97 -93.85
REMARK 500 PHE C 270 31.81 -91.77
REMARK 500 PRO C 278 42.78 -83.03
REMARK 500 ASN C 295 -121.56 63.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 777 DISTANCE = 8.94 ANGSTROMS
REMARK 525 HOH C 776 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH C 777 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH C 778 DISTANCE = 10.45 ANGSTROMS
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 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 300 SG
REMARK 620 2 CYS A 303 SG 110.5
REMARK 620 3 HIS A 320 NE2 101.3 116.3
REMARK 620 4 CYS A 327 SG 107.5 107.1 113.8
REMARK 620 5 HOH A 709 O 166.3 75.1 65.4 81.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 300 SG
REMARK 620 2 CYS C 303 SG 111.0
REMARK 620 3 HIS C 320 NE2 113.0 97.3
REMARK 620 4 CYS C 327 SG 115.0 109.1 110.0
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C3K A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide C3K C 602 and CYS C
REMARK 800 309
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MUP RELATED DB: PDB
DBREF 6EXW A 245 357 UNP Q13490 BIRC2_HUMAN 251 363
DBREF 6EXW C 245 357 UNP Q13490 BIRC2_HUMAN 251 363
SEQADV 6EXW MET A 244 UNP Q13490 INITIATING METHIONINE
SEQADV 6EXW LEU A 358 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW GLU A 359 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS A 360 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS A 361 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS A 362 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS A 363 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS A 364 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS A 365 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW MET C 244 UNP Q13490 INITIATING METHIONINE
SEQADV 6EXW LEU C 358 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW GLU C 359 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS C 360 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS C 361 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS C 362 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS C 363 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS C 364 UNP Q13490 EXPRESSION TAG
SEQADV 6EXW HIS C 365 UNP Q13490 EXPRESSION TAG
SEQRES 1 A 122 MET GLU ASN SER LEU GLU THR LEU ARG PHE SER ILE SER
SEQRES 2 A 122 ASN LEU SER MET GLN THR HIS ALA ALA ARG MET ARG THR
SEQRES 3 A 122 PHE MET TYR TRP PRO SER SER VAL PRO VAL GLN PRO GLU
SEQRES 4 A 122 GLN LEU ALA SER ALA GLY PHE TYR TYR VAL GLY ARG ASN
SEQRES 5 A 122 ASP ASP VAL LYS CYS PHE CYS CYS ASP GLY GLY LEU ARG
SEQRES 6 A 122 CYS TRP GLU SER GLY ASP ASP PRO TRP VAL GLU HIS ALA
SEQRES 7 A 122 LYS TRP PHE PRO ARG CYS GLU PHE LEU ILE ARG MET LYS
SEQRES 8 A 122 GLY GLN GLU PHE VAL ASP GLU ILE GLN GLY ARG TYR PRO
SEQRES 9 A 122 HIS LEU LEU GLU GLN LEU LEU SER THR SER LEU GLU HIS
SEQRES 10 A 122 HIS HIS HIS HIS HIS
SEQRES 1 C 122 MET GLU ASN SER LEU GLU THR LEU ARG PHE SER ILE SER
SEQRES 2 C 122 ASN LEU SER MET GLN THR HIS ALA ALA ARG MET ARG THR
SEQRES 3 C 122 PHE MET TYR TRP PRO SER SER VAL PRO VAL GLN PRO GLU
SEQRES 4 C 122 GLN LEU ALA SER ALA GLY PHE TYR TYR VAL GLY ARG ASN
SEQRES 5 C 122 ASP ASP VAL LYS CYS PHE CYS CYS ASP GLY GLY LEU ARG
SEQRES 6 C 122 CYS TRP GLU SER GLY ASP ASP PRO TRP VAL GLU HIS ALA
SEQRES 7 C 122 LYS TRP PHE PRO ARG CYS GLU PHE LEU ILE ARG MET LYS
SEQRES 8 C 122 GLY GLN GLU PHE VAL ASP GLU ILE GLN GLY ARG TYR PRO
SEQRES 9 C 122 HIS LEU LEU GLU GLN LEU LEU SER THR SER LEU GLU HIS
SEQRES 10 C 122 HIS HIS HIS HIS HIS
HET ZN A 601 1
HET C3K A 602 34
HET ZN C 601 1
HET C3K C 602 34
HETNAM ZN ZINC ION
HETNAM C3K (3~{S},6~{S},7~{R},9~{A}~{S})-6-[[(2~{S})-2-
HETNAM 2 C3K (METHYLAMINO)PROPANOYL]AMINO]-5-OXIDANYLIDENE-~{N}-
HETNAM 3 C3K (PHENYLMETHYL)-7-[(PROPANOYLAMINO)METHYL]-3,6,7,8,9,
HETNAM 4 C3K 9~{A}-HEXAHYDROPYRROLO[1,2-A]AZEPINE-3-CARBOXAMIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 C3K 2(C25 H35 N5 O4)
FORMUL 7 HOH *155(H2 O)
HELIX 1 AA1 ASN A 257 GLN A 261 5 5
HELIX 2 AA2 THR A 262 THR A 269 1 8
HELIX 3 AA3 GLN A 280 ALA A 287 1 8
HELIX 4 AA4 ASP A 315 PHE A 324 1 10
HELIX 5 AA5 CYS A 327 TYR A 346 1 20
HELIX 6 AA6 ASN C 257 GLN C 261 5 5
HELIX 7 AA7 THR C 262 PHE C 270 1 9
HELIX 8 AA8 GLN C 280 ALA C 287 1 8
HELIX 9 AA9 ASP C 315 PHE C 324 1 10
HELIX 10 AB1 CYS C 327 TYR C 346 1 20
SHEET 1 AA1 3 PHE A 289 TYR A 291 0
SHEET 2 AA1 3 VAL A 298 CYS A 300 -1 O LYS A 299 N TYR A 290
SHEET 3 AA1 3 GLY A 306 LEU A 307 -1 O LEU A 307 N VAL A 298
SHEET 1 AA2 3 PHE C 289 TYR C 291 0
SHEET 2 AA2 3 VAL C 298 CYS C 300 -1 O LYS C 299 N TYR C 290
SHEET 3 AA2 3 GLY C 306 LEU C 307 -1 O LEU C 307 N VAL C 298
LINK SG CYS A 309 CAA C3K A 602 1555 1555 1.84
LINK SG CYS C 309 CAA C3K C 602 1555 1555 1.84
LINK SG CYS A 300 ZN ZN A 601 1555 1555 2.33
LINK SG CYS A 303 ZN ZN A 601 1555 1555 2.31
LINK NE2 HIS A 320 ZN ZN A 601 1555 1555 2.15
LINK SG CYS A 327 ZN ZN A 601 1555 1555 2.33
LINK ZN ZN A 601 O HOH A 709 1555 1555 2.61
LINK SG CYS C 300 ZN ZN C 601 1555 1555 2.36
LINK SG CYS C 303 ZN ZN C 601 1555 1555 2.31
LINK NE2 HIS C 320 ZN ZN C 601 1555 1555 2.09
LINK SG CYS C 327 ZN ZN C 601 1555 1555 2.33
SITE 1 AC1 5 CYS A 300 CYS A 303 HIS A 320 CYS A 327
SITE 2 AC1 5 HOH A 709
SITE 1 AC2 13 ARG A 308 CYS A 309 HOH A 712 HOH A 717
SITE 2 AC2 13 GLY C 306 LEU C 307 ARG C 308 CYS C 309
SITE 3 AC2 13 GLU C 311 ASP C 314 GLU C 319 TRP C 323
SITE 4 AC2 13 HOH C 706
SITE 1 AC3 4 CYS C 300 CYS C 303 HIS C 320 CYS C 327
SITE 1 AC4 14 GLY A 306 LEU A 307 ARG A 308 CYS A 309
SITE 2 AC4 14 GLU A 311 ASP A 314 GLU A 319 TRP A 323
SITE 3 AC4 14 C3K A 602 HOH A 712 ASP C 296 ARG C 308
SITE 4 AC4 14 TRP C 310 HOH C 712
CRYST1 53.799 53.799 176.627 90.00 90.00 120.00 P 32 2 1 12
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 0.018588 0.010732 0.000000 0.00000
SCALE2 0.000000 0.021463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
