HEADER TRANSCRIPTION 19-MAY-14 4QF2
TITLE CRYSTAL STRUCTURE OF HUMAN BAZ2A PHD ZINC FINGER IN THE FREE FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 1673-1728;
COMPND 5 SYNONYM: TRANSCRIPTION TERMINATION FACTOR I-INTERACTING PROTEIN 5,
COMPND 6 TTF-I-INTERACTING PROTEIN 5, TIP5, HWALP3;
COMPND 7 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: BAZ2A, KIAA0314, TIP5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A, TRANSCRIPTION
KEYWDS 2 TERMINATION FACTOR I-INTERACTING PROTEIN 5, TTF-I-INTERACTING
KEYWDS 3 PROTEIN 5, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TALLANT,L.OVERVOORDE,I.VAN MOLLE,D.Y.CHIRGADZE,A.CIULLI
REVDAT 5 03-APR-24 4QF2 1 REMARK
REVDAT 4 28-FEB-24 4QF2 1 REMARK SEQADV LINK
REVDAT 3 22-APR-15 4QF2 1 JRNL
REVDAT 2 04-FEB-15 4QF2 1 REMARK
REVDAT 1 02-JUL-14 4QF2 0
JRNL AUTH C.TALLANT,E.VALENTINI,O.FEDOROV,L.OVERVOORDE,F.M.FERGUSON,
JRNL AUTH 2 P.FILIPPAKOPOULOS,D.I.SVERGUN,S.KNAPP,A.CIULLI
JRNL TITL MOLECULAR BASIS OF HISTONE TAIL RECOGNITION BY HUMAN TIP5
JRNL TITL 2 PHD FINGER AND BROMODOMAIN OF THE CHROMATIN REMODELING
JRNL TITL 3 COMPLEX NORC.
JRNL REF STRUCTURE V. 23 80 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25533489
JRNL DOI 10.1016/J.STR.2014.10.017
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 27298
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1468
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1865
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1635
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.94000
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): 0.094
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.001
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1684 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1548 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2271 ; 1.926 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3580 ; 0.891 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 205 ; 5.789 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;29.149 ;23.924
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 288 ;13.060 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.028 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 244 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1881 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 379 ; 0.001 ; 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 1676 A 1728
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5238 32.8325 19.7531
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0620
REMARK 3 T33: 0.0412 T12: 0.0189
REMARK 3 T13: -0.0216 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.2153 L22: 0.6421
REMARK 3 L33: 1.9770 L12: -0.8702
REMARK 3 L13: 1.1586 L23: -0.7217
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: 0.1510 S13: -0.0944
REMARK 3 S21: -0.0705 S22: -0.0871 S23: 0.0735
REMARK 3 S31: 0.1217 S32: 0.1854 S33: -0.0253
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 1676 B 1726
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4527 24.8960 45.4485
REMARK 3 T TENSOR
REMARK 3 T11: 0.0123 T22: 0.0786
REMARK 3 T33: 0.0571 T12: -0.0139
REMARK 3 T13: 0.0073 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 0.5341 L22: 1.1766
REMARK 3 L33: 1.7243 L12: -0.1681
REMARK 3 L13: -0.5738 L23: 0.3163
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.1144 S13: -0.0189
REMARK 3 S21: -0.0503 S22: -0.0737 S23: -0.0899
REMARK 3 S31: -0.0213 S32: 0.1885 S33: 0.0744
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 : C 1676 C 1727
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0841 38.7973 34.5003
REMARK 3 T TENSOR
REMARK 3 T11: 0.0636 T22: 0.0343
REMARK 3 T33: 0.0461 T12: 0.0056
REMARK 3 T13: -0.0061 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.5493 L22: 0.8966
REMARK 3 L33: 0.4970 L12: 0.2268
REMARK 3 L13: -0.2339 L23: -0.3654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0447 S12: 0.0381 S13: 0.0210
REMARK 3 S21: 0.0707 S22: 0.0591 S23: 0.0096
REMARK 3 S31: 0.0666 S32: 0.0480 S33: -0.0144
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 : D 1676 D 1728
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5936 23.8062 30.2576
REMARK 3 T TENSOR
REMARK 3 T11: 0.0684 T22: 0.0336
REMARK 3 T33: 0.0493 T12: -0.0095
REMARK 3 T13: 0.0298 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 1.4303 L22: 0.5330
REMARK 3 L33: 1.2110 L12: 0.6757
REMARK 3 L13: -0.3852 L23: -0.6681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0534 S12: 0.1039 S13: -0.0513
REMARK 3 S21: -0.0546 S22: -0.0059 S23: -0.0428
REMARK 3 S31: 0.0937 S32: 0.0894 S33: 0.0592
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 4QF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085973.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2822
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27299
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 58.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.80
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
REMARK 200 R SYM FOR SHELL (I) : 0.15300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: ARP/WARP AUTOBUILDING MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA/K PHOSPHATE, PH 8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 49.53050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.00700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.00700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 74.29575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.00700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.00700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.76525
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.00700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.00700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 74.29575
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.00700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.00700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 24.76525
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.53050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
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: 6960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 HIS A 1671
REMARK 465 MET A 1672
REMARK 465 SER A 1673
REMARK 465 VAL A 1674
REMARK 465 ASN A 1675
REMARK 465 HIS B 1671
REMARK 465 MET B 1672
REMARK 465 SER B 1673
REMARK 465 VAL B 1674
REMARK 465 ASN B 1675
REMARK 465 GLN B 1727
REMARK 465 VAL B 1728
REMARK 465 HIS C 1671
REMARK 465 MET C 1672
REMARK 465 SER C 1673
REMARK 465 VAL C 1674
REMARK 465 ASN C 1675
REMARK 465 VAL C 1728
REMARK 465 HIS D 1671
REMARK 465 MET D 1672
REMARK 465 SER D 1673
REMARK 465 VAL D 1674
REMARK 465 ASN D 1675
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 CYS A1697 -168.41 -162.60
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 A1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1679 SG
REMARK 620 2 CYS A1682 SG 109.1
REMARK 620 3 HIS A1702 ND1 103.3 98.1
REMARK 620 4 CYS A1705 SG 111.2 117.0 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1694 SG
REMARK 620 2 CYS A1697 SG 115.1
REMARK 620 3 CYS A1720 SG 111.0 104.7
REMARK 620 4 CYS A1723 SG 102.7 109.8 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1679 SG
REMARK 620 2 CYS B1682 SG 109.5
REMARK 620 3 HIS B1702 ND1 104.0 99.5
REMARK 620 4 CYS B1705 SG 112.3 115.6 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1694 SG
REMARK 620 2 CYS B1697 SG 112.6
REMARK 620 3 CYS B1720 SG 110.3 107.6
REMARK 620 4 CYS B1723 SG 103.6 108.7 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1679 SG
REMARK 620 2 CYS C1682 SG 108.9
REMARK 620 3 HIS C1702 ND1 103.2 100.2
REMARK 620 4 CYS C1705 SG 114.6 115.6 112.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1694 SG
REMARK 620 2 CYS C1697 SG 114.4
REMARK 620 3 CYS C1720 SG 112.6 102.5
REMARK 620 4 CYS C1723 SG 103.6 110.4 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1679 SG
REMARK 620 2 CYS D1682 SG 108.9
REMARK 620 3 HIS D1702 ND1 101.3 99.9
REMARK 620 4 CYS D1705 SG 115.2 116.2 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1694 SG
REMARK 620 2 CYS D1697 SG 115.7
REMARK 620 3 CYS D1720 SG 111.7 102.7
REMARK 620 4 CYS D1723 SG 102.5 109.9 114.9
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 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QF3 RELATED DB: PDB
DBREF 4QF2 A 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 4QF2 B 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 4QF2 C 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
DBREF 4QF2 D 1673 1728 UNP Q9UIF9 BAZ2A_HUMAN 1673 1728
SEQADV 4QF2 HIS A 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 MET A 1672 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 HIS B 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 MET B 1672 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 HIS C 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 MET C 1672 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 HIS D 1671 UNP Q9UIF9 EXPRESSION TAG
SEQADV 4QF2 MET D 1672 UNP Q9UIF9 EXPRESSION TAG
SEQRES 1 A 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 A 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 A 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 A 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 A 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 B 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 B 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 B 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 B 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 B 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 C 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 C 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 C 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 C 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 C 58 CYS LEU ALA GLN GLN VAL
SEQRES 1 D 58 HIS MET SER VAL ASN LYS VAL THR CYS LEU VAL CYS ARG
SEQRES 2 D 58 LYS GLY ASP ASN ASP GLU PHE LEU LEU LEU CYS ASP GLY
SEQRES 3 D 58 CYS ASP ARG GLY CYS HIS ILE TYR CYS HIS ARG PRO LYS
SEQRES 4 D 58 MET GLU ALA VAL PRO GLU GLY ASP TRP PHE CYS THR VAL
SEQRES 5 D 58 CYS LEU ALA GLN GLN VAL
HET ZN A1801 1
HET ZN A1802 1
HET PO4 A1803 5
HET ZN B1801 1
HET ZN B1802 1
HET PO4 B1803 5
HET ZN C1801 1
HET ZN C1802 1
HET GOL C1803 6
HET ZN D1801 1
HET ZN D1802 1
HET PO4 D1803 5
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 PO4 3(O4 P 3-)
FORMUL 13 GOL C3 H8 O3
FORMUL 17 HOH *120(H2 O)
HELIX 1 1 ASN A 1687 GLU A 1689 5 3
HELIX 2 2 CYS A 1720 ALA A 1725 1 6
HELIX 3 3 ASN B 1687 GLU B 1689 5 3
HELIX 4 4 TYR B 1704 HIS B 1706 5 3
HELIX 5 5 CYS B 1720 GLN B 1726 1 7
HELIX 6 6 ASN C 1687 GLU C 1689 5 3
HELIX 7 7 CYS C 1720 GLN C 1727 1 8
HELIX 8 8 ASN D 1687 GLU D 1689 5 3
HELIX 9 9 CYS D 1720 ALA D 1725 1 6
SHEET 1 A 2 LEU A1691 LEU A1693 0
SHEET 2 A 2 GLY A1700 HIS A1702 -1 O CYS A1701 N LEU A1692
SHEET 1 B 2 LEU B1691 LEU B1693 0
SHEET 2 B 2 GLY B1700 HIS B1702 -1 O CYS B1701 N LEU B1692
SHEET 1 C 2 LEU C1691 LEU C1693 0
SHEET 2 C 2 GLY C1700 HIS C1702 -1 O CYS C1701 N LEU C1692
SHEET 1 D 2 LEU D1691 LEU D1693 0
SHEET 2 D 2 GLY D1700 HIS D1702 -1 O CYS D1701 N LEU D1692
LINK SG CYS A1679 ZN ZN A1801 1555 1555 2.32
LINK SG CYS A1682 ZN ZN A1801 1555 1555 2.28
LINK SG CYS A1694 ZN ZN A1802 1555 1555 2.19
LINK SG CYS A1697 ZN ZN A1802 1555 1555 2.26
LINK ND1 HIS A1702 ZN ZN A1801 1555 1555 2.12
LINK SG CYS A1705 ZN ZN A1801 1555 1555 2.31
LINK SG CYS A1720 ZN ZN A1802 1555 1555 2.35
LINK SG CYS A1723 ZN ZN A1802 1555 1555 2.33
LINK SG CYS B1679 ZN ZN B1801 1555 1555 2.31
LINK SG CYS B1682 ZN ZN B1801 1555 1555 2.28
LINK SG CYS B1694 ZN ZN B1802 1555 1555 2.31
LINK SG CYS B1697 ZN ZN B1802 1555 1555 2.24
LINK ND1 HIS B1702 ZN ZN B1801 1555 1555 2.15
LINK SG CYS B1705 ZN ZN B1801 1555 1555 2.30
LINK SG CYS B1720 ZN ZN B1802 1555 1555 2.39
LINK SG CYS B1723 ZN ZN B1802 1555 1555 2.30
LINK SG CYS C1679 ZN ZN C1801 1555 1555 2.34
LINK SG CYS C1682 ZN ZN C1801 1555 1555 2.27
LINK SG CYS C1694 ZN ZN C1802 1555 1555 2.28
LINK SG CYS C1697 ZN ZN C1802 1555 1555 2.28
LINK ND1 HIS C1702 ZN ZN C1801 1555 1555 2.18
LINK SG CYS C1705 ZN ZN C1801 1555 1555 2.32
LINK SG CYS C1720 ZN ZN C1802 1555 1555 2.36
LINK SG CYS C1723 ZN ZN C1802 1555 1555 2.31
LINK SG CYS D1679 ZN ZN D1801 1555 1555 2.33
LINK SG CYS D1682 ZN ZN D1801 1555 1555 2.38
LINK SG CYS D1694 ZN ZN D1802 1555 1555 2.24
LINK SG CYS D1697 ZN ZN D1802 1555 1555 2.33
LINK ND1 HIS D1702 ZN ZN D1801 1555 1555 2.17
LINK SG CYS D1705 ZN ZN D1801 1555 1555 2.29
LINK SG CYS D1720 ZN ZN D1802 1555 1555 2.39
LINK SG CYS D1723 ZN ZN D1802 1555 1555 2.33
CISPEP 1 ARG A 1707 PRO A 1708 0 8.42
CISPEP 2 ARG B 1707 PRO B 1708 0 13.08
CISPEP 3 ARG C 1707 PRO C 1708 0 5.99
CISPEP 4 ARG D 1707 PRO D 1708 0 5.07
SITE 1 AC1 4 CYS A1679 CYS A1682 HIS A1702 CYS A1705
SITE 1 AC2 4 CYS A1694 CYS A1697 CYS A1720 CYS A1723
SITE 1 AC3 2 ARG A1707 HOH C1914
SITE 1 AC4 4 CYS B1679 CYS B1682 HIS B1702 CYS B1705
SITE 1 AC5 4 CYS B1694 CYS B1697 CYS B1720 CYS B1723
SITE 1 AC6 2 ARG B1707 HOH B1910
SITE 1 AC7 4 CYS C1679 CYS C1682 HIS C1702 CYS C1705
SITE 1 AC8 4 CYS C1694 CYS C1697 CYS C1720 CYS C1723
SITE 1 AC9 3 ASN A1687 ARG C1707 LYS C1709
SITE 1 BC1 4 CYS D1679 CYS D1682 HIS D1702 CYS D1705
SITE 1 BC2 4 CYS D1694 CYS D1697 CYS D1720 CYS D1723
SITE 1 BC3 4 ARG D1707 LYS D1709 HOH D1930 HOH D1932
CRYST1 72.014 72.014 99.061 90.00 90.00 90.00 P 43 21 2 32
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 0.013886 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010095 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
