HEADER CELL CYCLE 30-OCT-11 3UEG
TITLE CRYSTAL STRUCTURE OF HUMAN SURVIVIN K62A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: APOPTOSIS INHIBITOR 4, APOPTOSIS INHIBITOR SURVIVIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: API4, BIRC5, IAP4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P8HIS
KEYWDS ZINC FINGER, BIR DOMAIN, CHROMOSOMAL PASSENGER COMPLEX, CELL
KEYWDS 2 DIVISION, MITOSIS, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.NIEDZIALKOWSKA,P.J.POREBSKI,F.WANG,J.M.HIGGINS,P.T.STUKENBERG,
AUTHOR 2 W.MINOR
REVDAT 4 13-SEP-23 3UEG 1 REMARK
REVDAT 3 13-APR-22 3UEG 1 AUTHOR JRNL REMARK SEQADV
REVDAT 3 2 1 LINK
REVDAT 2 25-JUL-12 3UEG 1 JRNL
REVDAT 1 07-MAR-12 3UEG 0
JRNL AUTH E.NIEDZIALKOWSKA,F.WANG,P.J.POREBSKI,W.MINOR,J.M.HIGGINS,
JRNL AUTH 2 P.T.STUKENBERG
JRNL TITL MOLECULAR BASIS FOR PHOSPHOSPECIFIC RECOGNITION OF HISTONE
JRNL TITL 2 H3 TAILS BY SURVIVIN PARALOGUES AT INNER CENTROMERES.
JRNL REF MOL.BIOL.CELL V. 23 1457 2012
JRNL REFN ISSN 1059-1524
JRNL PMID 22357620
JRNL DOI 10.1091/MBC.E11-11-0904
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 11884
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 : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 606
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 801
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 44
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2131
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 93.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.24000
REMARK 3 B22 (A**2) : -2.79000
REMARK 3 B33 (A**2) : 3.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.62000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.290
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2204 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1504 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2984 ; 1.644 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3670 ; 1.124 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 5.410 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;32.359 ;25.048
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 343 ;16.926 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;25.023 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 315 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2479 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 443 ; 0.004 ; 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 : 4
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 5 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3130 -3.3164 -8.0900
REMARK 3 T TENSOR
REMARK 3 T11: 0.3317 T22: 0.1758
REMARK 3 T33: 0.2832 T12: -0.0337
REMARK 3 T13: 0.0188 T23: 0.0908
REMARK 3 L TENSOR
REMARK 3 L11: 5.4239 L22: 6.9263
REMARK 3 L33: 2.7936 L12: 0.8655
REMARK 3 L13: 0.0299 L23: -0.3362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0486 S12: -0.0548 S13: 0.1142
REMARK 3 S21: 0.5082 S22: 0.0470 S23: 0.1232
REMARK 3 S31: 0.1249 S32: -0.0971 S33: 0.0016
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 : A 91 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): -29.1807 10.7308 1.4748
REMARK 3 T TENSOR
REMARK 3 T11: 0.5335 T22: 0.1203
REMARK 3 T33: 0.4579 T12: -0.0263
REMARK 3 T13: 0.0234 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 2.6510 L22: 0.0041
REMARK 3 L33: 15.9702 L12: 0.0457
REMARK 3 L13: -3.6885 L23: -0.1061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0292 S12: 0.0497 S13: 0.2797
REMARK 3 S21: 0.0035 S22: 0.0196 S23: 0.0299
REMARK 3 S31: -0.0113 S32: -0.1632 S33: 0.0096
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9038 30.7004 -29.4592
REMARK 3 T TENSOR
REMARK 3 T11: 0.0561 T22: 0.1750
REMARK 3 T33: 0.2517 T12: -0.0251
REMARK 3 T13: -0.0109 T23: 0.0661
REMARK 3 L TENSOR
REMARK 3 L11: 5.2629 L22: 9.4998
REMARK 3 L33: 3.1602 L12: 1.0275
REMARK 3 L13: 1.7904 L23: -0.5406
REMARK 3 S TENSOR
REMARK 3 S11: -0.1101 S12: 0.3614 S13: 0.3563
REMARK 3 S21: 0.0754 S22: 0.1492 S23: -0.6529
REMARK 3 S31: 0.0050 S32: 0.5504 S33: -0.0391
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 91 B 140
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0659 16.1140 -31.9213
REMARK 3 T TENSOR
REMARK 3 T11: 0.1689 T22: 0.0824
REMARK 3 T33: 0.4776 T12: -0.0142
REMARK 3 T13: 0.0558 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 16.7651 L22: 0.1721
REMARK 3 L33: 1.8484 L12: 0.0813
REMARK 3 L13: -1.6223 L23: -0.5026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: 1.0032 S13: 0.4413
REMARK 3 S21: -0.0952 S22: 0.0622 S23: -0.0019
REMARK 3 S31: 0.0992 S32: -0.2618 S33: -0.0726
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
REMARK 4
REMARK 4 3UEG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : C(111) DIAMOND LAUE
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : BERYLLIUM LENS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12510
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.53200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3UEC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES-NA, 20% PEG 3350, 0.18 M
REMARK 280 AMMONIUM SULFATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
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 56.70300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.51650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.70300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.51650
REMARK 290 SMTRY3 4 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: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 GLU A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 ASP A 142
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 GLU B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ALA B 3
REMARK 465 PRO B 4
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 LYS A 23 CG CD CE NZ
REMARK 470 ARG A 37 NE CZ NH1 NH2
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 LYS A 78 CE NZ
REMARK 470 LYS A 79 CG CD CE NZ
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 GLU A 95 CG CD OE1 OE2
REMARK 470 LYS A 103 CG CD CE NZ
REMARK 470 LYS A 110 CE NZ
REMARK 470 GLU A 116 CG CD OE1 OE2
REMARK 470 LYS A 122 CD CE NZ
REMARK 470 LYS A 129 CD CE NZ
REMARK 470 LYS A 130 CD CE NZ
REMARK 470 ARG A 133 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 137 CG CD OE1 NE2
REMARK 470 MET A 141 CG SD CE
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 ARG B 37 NE CZ NH1 NH2
REMARK 470 GLU B 49 CG CD OE1 OE2
REMARK 470 GLU B 75 CG CD OE1 OE2
REMARK 470 LYS B 79 CG CD CE NZ
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 LYS B 110 CG CD CE NZ
REMARK 470 LYS B 115 CE NZ
REMARK 470 LYS B 122 CD CE NZ
REMARK 470 ARG B 133 CG CD NE CZ NH1 NH2
REMARK 470 MET B 141 SD CE
REMARK 470 ASP B 142 CG OD1 OD2
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 LEU A 28 -133.82 -111.98
REMARK 500 CYS A 33 59.08 -97.19
REMARK 500 SER A 81 72.72 -168.31
REMARK 500 ASN B 24 8.87 80.61
REMARK 500 LEU B 28 -135.05 -115.77
REMARK 500 SER B 81 74.53 -166.44
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 143 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 57 SG
REMARK 620 2 CYS A 60 SG 99.6
REMARK 620 3 HIS A 77 NE2 116.7 109.4
REMARK 620 4 CYS A 84 SG 119.6 104.9 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 143 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 57 SG
REMARK 620 2 CYS B 60 SG 101.8
REMARK 620 3 HIS B 77 NE2 112.4 110.0
REMARK 620 4 CYS B 84 SG 117.7 108.5 106.2
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
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 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 144
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 145
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 143
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UEC RELATED DB: PDB
REMARK 900 RELATED ID: 3UED RELATED DB: PDB
REMARK 900 RELATED ID: 3UEE RELATED DB: PDB
REMARK 900 RELATED ID: 3UEF RELATED DB: PDB
REMARK 900 RELATED ID: 3UEH RELATED DB: PDB
REMARK 900 RELATED ID: 3UEI RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 E129K REPRESENTS A NATURAL VARIANT
DBREF 3UEG A 1 142 UNP O15392 BIRC5_HUMAN 1 142
DBREF 3UEG B 1 142 UNP O15392 BIRC5_HUMAN 1 142
SEQADV 3UEG GLY A -3 UNP O15392 EXPRESSION TAG
SEQADV 3UEG SER A -2 UNP O15392 EXPRESSION TAG
SEQADV 3UEG HIS A -1 UNP O15392 EXPRESSION TAG
SEQADV 3UEG GLU A 0 UNP O15392 EXPRESSION TAG
SEQADV 3UEG ALA A 62 UNP O15392 LYS 62 ENGINEERED MUTATION
SEQADV 3UEG LYS A 129 UNP O15392 GLU 129 SEE REMARK 999
SEQADV 3UEG GLY B -3 UNP O15392 EXPRESSION TAG
SEQADV 3UEG SER B -2 UNP O15392 EXPRESSION TAG
SEQADV 3UEG HIS B -1 UNP O15392 EXPRESSION TAG
SEQADV 3UEG GLU B 0 UNP O15392 EXPRESSION TAG
SEQADV 3UEG ALA B 62 UNP O15392 LYS 62 ENGINEERED MUTATION
SEQADV 3UEG LYS B 129 UNP O15392 GLU 129 SEE REMARK 999
SEQRES 1 A 146 GLY SER HIS GLU MET GLY ALA PRO THR LEU PRO PRO ALA
SEQRES 2 A 146 TRP GLN PRO PHE LEU LYS ASP HIS ARG ILE SER THR PHE
SEQRES 3 A 146 LYS ASN TRP PRO PHE LEU GLU GLY CYS ALA CYS THR PRO
SEQRES 4 A 146 GLU ARG MET ALA GLU ALA GLY PHE ILE HIS CYS PRO THR
SEQRES 5 A 146 GLU ASN GLU PRO ASP LEU ALA GLN CYS PHE PHE CYS PHE
SEQRES 6 A 146 ALA GLU LEU GLU GLY TRP GLU PRO ASP ASP ASP PRO ILE
SEQRES 7 A 146 GLU GLU HIS LYS LYS HIS SER SER GLY CYS ALA PHE LEU
SEQRES 8 A 146 SER VAL LYS LYS GLN PHE GLU GLU LEU THR LEU GLY GLU
SEQRES 9 A 146 PHE LEU LYS LEU ASP ARG GLU ARG ALA LYS ASN LYS ILE
SEQRES 10 A 146 ALA LYS GLU THR ASN ASN LYS LYS LYS GLU PHE GLU GLU
SEQRES 11 A 146 THR ALA LYS LYS VAL ARG ARG ALA ILE GLU GLN LEU ALA
SEQRES 12 A 146 ALA MET ASP
SEQRES 1 B 146 GLY SER HIS GLU MET GLY ALA PRO THR LEU PRO PRO ALA
SEQRES 2 B 146 TRP GLN PRO PHE LEU LYS ASP HIS ARG ILE SER THR PHE
SEQRES 3 B 146 LYS ASN TRP PRO PHE LEU GLU GLY CYS ALA CYS THR PRO
SEQRES 4 B 146 GLU ARG MET ALA GLU ALA GLY PHE ILE HIS CYS PRO THR
SEQRES 5 B 146 GLU ASN GLU PRO ASP LEU ALA GLN CYS PHE PHE CYS PHE
SEQRES 6 B 146 ALA GLU LEU GLU GLY TRP GLU PRO ASP ASP ASP PRO ILE
SEQRES 7 B 146 GLU GLU HIS LYS LYS HIS SER SER GLY CYS ALA PHE LEU
SEQRES 8 B 146 SER VAL LYS LYS GLN PHE GLU GLU LEU THR LEU GLY GLU
SEQRES 9 B 146 PHE LEU LYS LEU ASP ARG GLU ARG ALA LYS ASN LYS ILE
SEQRES 10 B 146 ALA LYS GLU THR ASN ASN LYS LYS LYS GLU PHE GLU GLU
SEQRES 11 B 146 THR ALA LYS LYS VAL ARG ARG ALA ILE GLU GLN LEU ALA
SEQRES 12 B 146 ALA MET ASP
HET ZN A 143 1
HET EDO A 144 4
HET PG4 A 145 13
HET ZN B 143 1
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 EDO C2 H6 O2
FORMUL 5 PG4 C8 H18 O5
FORMUL 7 HOH *8(H2 O)
HELIX 1 1 PRO A 8 PHE A 13 5 6
HELIX 2 2 LYS A 15 THR A 21 1 7
HELIX 3 3 PRO A 35 ALA A 41 1 7
HELIX 4 4 PRO A 73 HIS A 80 1 8
HELIX 5 5 ALA A 85 SER A 88 5 4
HELIX 6 6 PHE A 93 GLU A 95 5 3
HELIX 7 7 LEU A 98 MET A 141 1 44
HELIX 8 8 PRO B 8 PHE B 13 5 6
HELIX 9 9 LYS B 15 THR B 21 1 7
HELIX 10 10 PRO B 35 ALA B 41 1 7
HELIX 11 11 PRO B 73 HIS B 80 1 8
HELIX 12 12 ALA B 85 SER B 88 5 4
HELIX 13 13 PHE B 93 GLU B 95 5 3
HELIX 14 14 LEU B 98 MET B 141 1 44
SHEET 1 A 3 PHE A 43 HIS A 45 0
SHEET 2 A 3 ALA A 55 CYS A 57 -1 O GLN A 56 N ILE A 44
SHEET 3 A 3 PHE A 61 LEU A 64 -1 O LEU A 64 N ALA A 55
SHEET 1 B 3 PHE B 43 HIS B 45 0
SHEET 2 B 3 ALA B 55 CYS B 57 -1 O GLN B 56 N ILE B 44
SHEET 3 B 3 PHE B 61 LEU B 64 -1 O LEU B 64 N ALA B 55
LINK SG CYS A 57 ZN ZN A 143 1555 1555 2.12
LINK SG CYS A 60 ZN ZN A 143 1555 1555 2.22
LINK NE2 HIS A 77 ZN ZN A 143 1555 1555 1.93
LINK SG CYS A 84 ZN ZN A 143 1555 1555 2.10
LINK SG CYS B 57 ZN ZN B 143 1555 1555 2.10
LINK SG CYS B 60 ZN ZN B 143 1555 1555 2.18
LINK NE2 HIS B 77 ZN ZN B 143 1555 1555 2.01
LINK SG CYS B 84 ZN ZN B 143 1555 1555 2.09
SITE 1 AC1 4 CYS A 57 CYS A 60 HIS A 77 CYS A 84
SITE 1 AC2 1 SER A 88
SITE 1 AC3 4 LEU A 14 LYS A 15 ASP A 16 GLN A 92
SITE 1 AC4 4 CYS B 57 CYS B 60 HIS B 77 CYS B 84
CRYST1 113.406 71.033 83.631 90.00 130.71 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 0.008818 0.000000 0.007587 0.00000
SCALE2 0.000000 0.014078 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015774 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
