HEADER PEPTIDE BINDING PROTEIN 09-APR-18 6G8R
TITLE SP140 PHD-BROMODOMAIN COMPLEX WITH SCFV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SINGLE-CHAIN VARIABLE FRAGMENT;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: MISSING DENSITY FOR LINKER REGION;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NUCLEAR BODY PROTEIN SP140;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 687-862;
COMPND 10 SYNONYM: LYMPHOID-RESTRICTED HOMOLOG OF SP100,LYSP100,NUCLEAR
COMPND 11 AUTOANTIGEN SP-140,SPECKLED 140 KDA;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: ZINC ATOMS NUMBERED 1000 AND 1001
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: SP140, LYSP100;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EPIGENETICS PHD BROMODOMAIN SHORT-CHAIN VARIABLE FRAGMENT, STRUCTURAL
KEYWDS 2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, PEPTIDE BINDING
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FAIRHEAD,S.GRASLUND,C.STRAIN-DAMERELL,S.S.PICAUD,A.C.W.PIKE,
AUTHOR 2 D.M.PINKAS,E.WIGREN,C.PREGER,H.PERSSON LOTSHOLM,E.OSSIPOVA,
AUTHOR 3 P.FILIPPAKOPOULOS,N.A.BURGESS-BROWN,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 4 C.BOUNTRA,F.VON DELFT,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 17-JAN-24 6G8R 1 REMARK
REVDAT 3 13-NOV-19 6G8R 1 COMPND REMARK HELIX SHEET
REVDAT 3 2 1 SSBOND LINK SITE SCALE
REVDAT 3 3 1 ATOM
REVDAT 2 16-JAN-19 6G8R 1 COMPND REMARK HETNAM
REVDAT 1 18-APR-18 6G8R 0
JRNL AUTH M.FAIRHEAD,S.GRASLUND,C.STRAIN-DAMERELL,S.S.PICAUD,
JRNL AUTH 2 A.C.W.PIKE,D.M.PINKAS,E.WIGREN,C.PREGER,H.PERSSON LOTSHOLM,
JRNL AUTH 3 E.OSSIPOVA,P.FILIPPAKOPOULOS,N.A.BURGESS-BROWN,
JRNL AUTH 4 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,F.VON DELFT
JRNL TITL SP140 PHD-BROMODOMAIN COMPLEX WITH SCFV
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
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) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 21107
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1140
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) : 2.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1522
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3980
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3040
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.55000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -1.78000
REMARK 3 B12 (A**2) : 0.27000
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): 0.353
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.265
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.234
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.812
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3124 ; 0.004 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2759 ; 0.001 ; 0.018
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4212 ; 1.301 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6391 ; 1.128 ; 1.573
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 385 ; 6.555 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;29.940 ;21.635
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 507 ;14.893 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;15.022 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 396 ; 0.043 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3501 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 707 ; 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 : 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 1 A 242
REMARK 3 ORIGIN FOR THE GROUP (A): -44.0417 43.2150 -5.2119
REMARK 3 T TENSOR
REMARK 3 T11: 0.1808 T22: 0.1376
REMARK 3 T33: 0.0062 T12: -0.0467
REMARK 3 T13: 0.0171 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.5401 L22: 2.6171
REMARK 3 L33: 0.9711 L12: -0.3115
REMARK 3 L13: 0.9060 L23: -0.0975
REMARK 3 S TENSOR
REMARK 3 S11: -0.0482 S12: 0.1236 S13: 0.0465
REMARK 3 S21: -0.0148 S22: 0.0141 S23: -0.0826
REMARK 3 S31: -0.0637 S32: 0.1353 S33: 0.0340
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 686 B 862
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2408 28.5601 17.6872
REMARK 3 T TENSOR
REMARK 3 T11: 0.1658 T22: 0.1322
REMARK 3 T33: 0.0190 T12: -0.0073
REMARK 3 T13: 0.0228 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.5959 L22: 3.0882
REMARK 3 L33: 1.8833 L12: -0.4523
REMARK 3 L13: 0.3171 L23: -0.5506
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: -0.0221 S13: -0.1416
REMARK 3 S21: -0.0335 S22: -0.0139 S23: 0.0960
REMARK 3 S31: 0.1231 S32: -0.0767 S33: 0.0207
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6G8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96861
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22312
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 64.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 10.53
REMARK 200 R MERGE (I) : 0.22500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 10.59
REMARK 200 R MERGE FOR SHELL (I) : 3.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.720
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2MD8, 5FBO, 5GS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM MALONATE, 0.5 % JEFFAMINE
REMARK 280 ED-2003, 0.1 M HEPES PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 114.45000
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 228.90000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 171.67500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 286.12500
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 57.22500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 114.45000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 228.90000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 286.12500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 171.67500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 57.22500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 SER A 119
REMARK 465 GLY A 120
REMARK 465 GLY A 121
REMARK 465 GLY A 122
REMARK 465 GLY A 123
REMARK 465 SER A 124
REMARK 465 GLY A 125
REMARK 465 GLY A 126
REMARK 465 GLY A 127
REMARK 465 GLY A 128
REMARK 465 SER A 129
REMARK 465 GLY A 130
REMARK 465 GLY A 131
REMARK 465 GLY A 132
REMARK 465 GLY A 133
REMARK 465 ALA A 243
REMARK 465 GLU A 244
REMARK 465 ASN A 245
REMARK 465 LEU A 246
REMARK 465 TYR A 247
REMARK 465 PHE A 248
REMARK 465 GLN A 249
REMARK 465 SER A 250
REMARK 465 GLY B 740
REMARK 465 SER B 741
REMARK 465 GLN B 742
REMARK 465 GLN B 743
REMARK 465 CYS B 744
REMARK 465 GLU B 790
REMARK 465 ALA B 791
REMARK 465 CYS B 792
REMARK 465 GLN B 793
REMARK 465 GLY B 794
REMARK 465 LYS B 835
REMARK 465 TYR B 836
REMARK 465 LYS B 837
REMARK 465 SER B 863
REMARK 465 SER B 864
REMARK 465 LYS B 865
REMARK 465 GLY B 866
REMARK 465 GLY B 867
REMARK 465 TYR B 868
REMARK 465 GLY B 869
REMARK 465 LEU B 870
REMARK 465 ASN B 871
REMARK 465 ASP B 872
REMARK 465 ILE B 873
REMARK 465 PHE B 874
REMARK 465 GLU B 875
REMARK 465 ALA B 876
REMARK 465 GLN B 877
REMARK 465 LYS B 878
REMARK 465 ILE B 879
REMARK 465 GLU B 880
REMARK 465 TRP B 881
REMARK 465 HIS B 882
REMARK 465 GLU B 883
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 GLN A 13 CG CD OE1 NE2
REMARK 470 ASP A 62 CG OD1 OD2
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 SER A 141 OG
REMARK 470 MET B 687 CG SD CE
REMARK 470 GLU B 724 CG CD OE1 OE2
REMARK 470 GLN B 746 CG CD OE1 NE2
REMARK 470 GLU B 752 CG CD OE1 OE2
REMARK 470 TYR B 784 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 788 CG1 CG2 CD1
REMARK 470 ARG B 789 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 796 CG CD CE NZ
REMARK 470 TYR B 834 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 838 CG OD1 OD2
REMARK 470 LYS B 852 CG CD CE NZ
REMARK 470 GLN B 861 CG CD OE1 NE2
REMARK 470 GLU B 862 CG CD OE1 OE2
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 VAL A 48 -61.95 -108.57
REMARK 500 TYR A 52 -119.26 -111.16
REMARK 500 ARG A 67 -45.02 -137.19
REMARK 500 TYR A 103 30.60 -145.66
REMARK 500 SER A 164 -120.04 48.36
REMARK 500 ALA A 185 -36.91 72.49
REMARK 500 LEU A 228 -153.48 60.83
REMARK 500 THR B 707 -61.73 -97.56
REMARK 500 GLU B 797 123.86 -179.01
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 B1009 DISTANCE = 6.10 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 B 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 693 SG
REMARK 620 2 CYS B 696 SG 109.5
REMARK 620 3 HIS B 713 ND1 101.9 100.8
REMARK 620 4 CYS B 716 SG 104.9 119.3 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 705 SG
REMARK 620 2 CYS B 708 SG 101.8
REMARK 620 3 CYS B 730 SG 112.4 117.1
REMARK 620 4 CYS B 733 SG 109.5 100.6 114.2
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 901
DBREF 6G8R A 1 250 PDB 6G8R 6G8R 1 250
DBREF 6G8R B 687 862 UNP Q13342 SP140_HUMAN 687 862
SEQADV 6G8R SER B 686 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R SER B 863 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R SER B 864 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R LYS B 865 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLY B 866 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLY B 867 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R TYR B 868 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLY B 869 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R LEU B 870 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R ASN B 871 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R ASP B 872 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R ILE B 873 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R PHE B 874 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLU B 875 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R ALA B 876 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLN B 877 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R LYS B 878 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R ILE B 879 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLU B 880 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R TRP B 881 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R HIS B 882 UNP Q13342 EXPRESSION TAG
SEQADV 6G8R GLU B 883 UNP Q13342 EXPRESSION TAG
SEQRES 1 A 250 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 A 250 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 A 250 PHE THR PHE TYR GLY SER GLY MET GLY TRP VAL ARG GLN
SEQRES 4 A 250 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE TYR
SEQRES 5 A 250 SER GLY SER GLY SER THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 A 250 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 A 250 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 A 250 ALA VAL TYR TYR CYS ALA ARG THR SER ILE TYR TYR TYR
SEQRES 9 A 250 TYR MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 A 250 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY
SEQRES 11 A 250 GLY GLY GLY SER ASP ILE GLN MET THR GLN SER PRO SER
SEQRES 12 A 250 SER LEU SER ALA SER VAL GLY ASP ARG VAL THR ILE THR
SEQRES 13 A 250 CYS ARG ALA SER GLN SER ILE SER SER TYR LEU ASN TRP
SEQRES 14 A 250 TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE
SEQRES 15 A 250 TYR ALA ALA SER SER LEU GLN SER GLY VAL PRO SER ARG
SEQRES 16 A 250 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR
SEQRES 17 A 250 ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR
SEQRES 18 A 250 CYS GLN GLN SER SER SER LEU PHE THR PHE GLY GLN GLY
SEQRES 19 A 250 THR LYS LEU GLU ILE LYS ARG THR ALA GLU ASN LEU TYR
SEQRES 20 A 250 PHE GLN SER
SEQRES 1 B 198 SER MET ARG ASN LEU ASP GLU CYS GLU VAL CYS ARG ASP
SEQRES 2 B 198 GLY GLY GLU LEU PHE CYS CYS ASP THR CYS SER ARG VAL
SEQRES 3 B 198 PHE HIS GLU ASP CYS HIS ILE PRO PRO VAL GLU ALA GLU
SEQRES 4 B 198 ARG THR PRO TRP ASN CYS ILE PHE CYS ARG MET LYS GLU
SEQRES 5 B 198 SER PRO GLY SER GLN GLN CYS CYS GLN GLU SER GLU VAL
SEQRES 6 B 198 LEU GLU ARG GLN MET CYS PRO GLU GLU GLN LEU LYS CYS
SEQRES 7 B 198 GLU PHE LEU LEU LEU LYS VAL TYR CYS CYS SER GLU SER
SEQRES 8 B 198 SER PHE PHE ALA LYS ILE PRO TYR TYR TYR TYR ILE ARG
SEQRES 9 B 198 GLU ALA CYS GLN GLY LEU LYS GLU PRO MET TRP LEU ASP
SEQRES 10 B 198 LYS ILE LYS LYS ARG LEU ASN GLU HIS GLY TYR PRO GLN
SEQRES 11 B 198 VAL GLU GLY PHE VAL GLN ASP MET ARG LEU ILE PHE GLN
SEQRES 12 B 198 ASN HIS ARG ALA SER TYR LYS TYR LYS ASP PHE GLY GLN
SEQRES 13 B 198 MET GLY PHE ARG LEU GLU ALA GLU PHE GLU LYS ASN PHE
SEQRES 14 B 198 LYS GLU VAL PHE ALA ILE GLN GLU SER SER LYS GLY GLY
SEQRES 15 B 198 TYR GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU
SEQRES 16 B 198 TRP HIS GLU
HET EDO A 301 4
HET EDO A 302 4
HET ZN B 900 1
HET ZN B 901 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *13(H2 O)
HELIX 1 AA1 THR A 28 SER A 32 5 5
HELIX 2 AA2 ASP A 62 LYS A 65 5 4
HELIX 3 AA3 GLN A 213 PHE A 217 5 5
HELIX 4 AA4 CYS B 730 LYS B 736 1 7
HELIX 5 AA5 GLN B 746 ARG B 753 1 8
HELIX 6 AA6 CYS B 756 CYS B 773 1 18
HELIX 7 AA7 GLU B 775 LYS B 781 1 7
HELIX 8 AA8 PRO B 783 ILE B 788 5 6
HELIX 9 AA9 TRP B 800 GLU B 810 1 11
HELIX 10 AB1 GLN B 815 ALA B 832 1 18
HELIX 11 AB2 GLY B 843 PHE B 858 1 16
SHEET 1 AA1 4 GLN A 3 SER A 7 0
SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N LEU A 5
SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18
SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82
SHEET 1 AA2 6 LEU A 11 VAL A 12 0
SHEET 2 AA2 6 THR A 113 VAL A 117 1 O THR A 116 N VAL A 12
SHEET 3 AA2 6 ALA A 92 SER A 100 -1 N TYR A 94 O THR A 113
SHEET 4 AA2 6 GLY A 33 GLN A 39 -1 N VAL A 37 O TYR A 95
SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O SER A 49 N TRP A 36
SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O TYR A 59 N SER A 50
SHEET 1 AA3 4 LEU A 11 VAL A 12 0
SHEET 2 AA3 4 THR A 113 VAL A 117 1 O THR A 116 N VAL A 12
SHEET 3 AA3 4 ALA A 92 SER A 100 -1 N TYR A 94 O THR A 113
SHEET 4 AA3 4 TYR A 105 TRP A 109 -1 O TYR A 105 N SER A 100
SHEET 1 AA4 4 MET A 138 SER A 141 0
SHEET 2 AA4 4 VAL A 153 ALA A 159 -1 O ARG A 158 N THR A 139
SHEET 3 AA4 4 ASP A 204 ILE A 209 -1 O PHE A 205 N CYS A 157
SHEET 4 AA4 4 PHE A 196 SER A 201 -1 N SER A 197 O THR A 208
SHEET 1 AA5 6 SER A 144 ALA A 147 0
SHEET 2 AA5 6 THR A 235 ILE A 239 1 O GLU A 238 N LEU A 145
SHEET 3 AA5 6 ALA A 218 GLN A 224 -1 N ALA A 218 O LEU A 237
SHEET 4 AA5 6 LEU A 167 GLN A 172 -1 N TYR A 170 O TYR A 221
SHEET 5 AA5 6 LYS A 179 TYR A 183 -1 O LYS A 179 N GLN A 171
SHEET 6 AA5 6 SER A 187 LEU A 188 -1 O SER A 187 N TYR A 183
SHEET 1 AA6 4 SER A 144 ALA A 147 0
SHEET 2 AA6 4 THR A 235 ILE A 239 1 O GLU A 238 N LEU A 145
SHEET 3 AA6 4 ALA A 218 GLN A 224 -1 N ALA A 218 O LEU A 237
SHEET 4 AA6 4 THR A 230 PHE A 231 -1 O THR A 230 N GLN A 224
SHEET 1 AA7 2 PHE B 703 CYS B 704 0
SHEET 2 AA7 2 VAL B 711 PHE B 712 -1 O PHE B 712 N PHE B 703
SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 157 CYS A 222 1555 1555 2.02
LINK SG CYS B 693 ZN ZN B 900 1555 1555 2.33
LINK SG CYS B 696 ZN ZN B 900 1555 1555 2.35
LINK SG CYS B 705 ZN ZN B 901 1555 1555 2.33
LINK SG CYS B 708 ZN ZN B 901 1555 1555 2.35
LINK ND1 HIS B 713 ZN ZN B 900 1555 1555 2.12
LINK SG CYS B 716 ZN ZN B 900 1555 1555 2.32
LINK SG CYS B 730 ZN ZN B 901 1555 1555 2.34
LINK SG CYS B 733 ZN ZN B 901 1555 1555 2.33
CISPEP 1 SER A 141 PRO A 142 0 -7.36
CISPEP 2 ILE B 718 PRO B 719 0 -2.06
CISPEP 3 THR B 726 PRO B 727 0 -5.17
SITE 1 AC1 4 GLN A 171 LYS A 179 PHE A 196 ASP A 216
SITE 1 AC2 4 GLN A 172 PRO A 174 GLY A 175 LYS A 176
SITE 1 AC3 4 CYS B 693 CYS B 696 HIS B 713 CYS B 716
SITE 1 AC4 4 CYS B 705 CYS B 708 CYS B 730 CYS B 733
CRYST1 89.200 89.200 343.350 90.00 90.00 120.00 P 61 2 2 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 0.011211 0.006473 0.000000 0.00000
SCALE2 0.000000 0.012945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002912 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
