HEADER DNA BINDING PROTEIN 29-APR-10 2XD7
TITLE CRYSTAL STRUCTURE OF THE MACRO DOMAIN OF HUMAN CORE HISTONE H2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORE HISTONE MACRO-H2A.2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: MACRO DOMAIN, RESIDUES 177-369;
COMPND 5 SYNONYM: HISTONE MACROH2A2, MH2A2;
COMPND 6 ENGINEERED: YES
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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNH-TRXT
KEYWDS CHROMOSOMAL PROTEIN, NUCLEOSOME CORE, CHROMATIN REGULATOR, NUCLEUS,
KEYWDS 2 DNA-BINDING PROTEIN, PHOSPHOPROTEIN, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VOLLMAR,C.PHILLIPS,E.P.CARPENTER,J.R.C.MUNIZ,T.KROJER,E.UGOCHUKWU,
AUTHOR 2 F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,O.GILEADI
REVDAT 3 20-DEC-23 2XD7 1 REMARK
REVDAT 2 24-JAN-18 2XD7 1 AUTHOR JRNL
REVDAT 1 19-MAY-10 2XD7 0
JRNL AUTH M.VOLLMAR,C.PHILLIPPS,E.P.CARPENTER,J.R.C.MUNIZ,T.KROJER,
JRNL AUTH 2 E.UGOCHUKWU,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,
JRNL AUTH 3 A.EDWARDS,O.GILEADI
JRNL TITL CRYSTAL STRUCTURE OF THE MACRO DOMAIN OF HUMAN CORE HISTONE
JRNL TITL 2 H2A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0066
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) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 43253
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2281
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) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1803
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5584
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.93000
REMARK 3 B22 (A**2) : -10.95000
REMARK 3 B33 (A**2) : 9.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.32000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.054
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.043
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.914
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5688 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3756 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7690 ; 1.450 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9326 ; 1.314 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 759 ; 6.203 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 199 ;38.208 ;26.131
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 969 ;17.054 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;12.436 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 901 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6344 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1014 ; 0.003 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : C A B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 178 C 197 2
REMARK 3 1 A 178 A 197 2
REMARK 3 1 B 178 B 197 2
REMARK 3 1 D 178 D 197 2
REMARK 3 2 C 208 C 243 2
REMARK 3 2 A 208 A 243 2
REMARK 3 2 B 208 B 243 2
REMARK 3 2 D 208 D 243 2
REMARK 3 3 C 245 C 255 2
REMARK 3 3 A 245 A 255 2
REMARK 3 3 B 245 B 255 2
REMARK 3 3 D 245 D 255 2
REMARK 3 4 C 257 C 277 2
REMARK 3 4 A 257 A 277 2
REMARK 3 4 B 257 B 277 2
REMARK 3 4 D 257 D 277 2
REMARK 3 5 C 279 C 368 2
REMARK 3 5 A 279 A 368 2
REMARK 3 5 B 279 B 368 2
REMARK 3 5 D 279 D 368 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1016 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1016 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1016 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1016 ; 0.04 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1070 ; 0.05 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1070 ; 0.04 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1070 ; 0.05 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1070 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1016 ; 2.85 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1016 ; 3.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1016 ; 2.25 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1016 ; 4.90 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1070 ; 3.20 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1070 ; 3.48 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1070 ; 2.90 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1070 ; 4.84 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B A C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 198 B 201 2
REMARK 3 1 A 198 A 201 2
REMARK 3 1 C 198 C 201 2
REMARK 3 1 D 198 D 201 2
REMARK 3 2 B 204 B 207 2
REMARK 3 2 A 204 A 207 2
REMARK 3 2 C 204 C 207 2
REMARK 3 2 D 204 D 207 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 48 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 48 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 C (A): 48 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 48 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 A (A): 45 ; 0.06 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 45 ; 0.06 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 45 ; 0.04 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 45 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 2 A (A**2): 48 ; 2.20 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 48 ; 1.58 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 48 ; 2.23 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 48 ; 2.04 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 45 ; 6.21 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 45 ; 4.33 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 45 ; 3.95 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 45 ; 7.32 ; 2.00
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.563
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : H,-K,-L
REMARK 3 TWIN FRACTION : 0.437
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 185 A 229
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5111 -2.3618 54.5483
REMARK 3 T TENSOR
REMARK 3 T11: 0.3598 T22: 0.2830
REMARK 3 T33: 0.1836 T12: 0.0600
REMARK 3 T13: 0.0684 T23: -0.1134
REMARK 3 L TENSOR
REMARK 3 L11: 7.1573 L22: 7.2380
REMARK 3 L33: 5.7141 L12: -3.8298
REMARK 3 L13: 4.6868 L23: -4.7138
REMARK 3 S TENSOR
REMARK 3 S11: 0.3227 S12: -0.4256 S13: -0.5056
REMARK 3 S21: -0.1483 S22: 0.0701 S23: 0.2363
REMARK 3 S31: 0.2659 S32: -0.2125 S33: -0.3928
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 230 A 270
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4700 -13.9308 40.2324
REMARK 3 T TENSOR
REMARK 3 T11: 0.3563 T22: 0.2952
REMARK 3 T33: 0.1881 T12: 0.1408
REMARK 3 T13: 0.0405 T23: -0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 2.4994 L22: 5.4495
REMARK 3 L33: 2.6260 L12: 0.5425
REMARK 3 L13: -0.2511 L23: -1.5566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: 0.1560 S13: -0.3310
REMARK 3 S21: -0.3903 S22: -0.0279 S23: -0.3760
REMARK 3 S31: 0.4023 S32: 0.3531 S33: -0.0004
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 : A 271 A 313
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1745 -2.1399 38.1987
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.2349
REMARK 3 T33: 0.0132 T12: 0.0932
REMARK 3 T13: -0.0053 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 6.9468 L22: 6.4681
REMARK 3 L33: 2.5039 L12: 3.7150
REMARK 3 L13: -1.0885 L23: -2.2532
REMARK 3 S TENSOR
REMARK 3 S11: -0.1239 S12: 0.5704 S13: 0.0159
REMARK 3 S21: -0.3559 S22: 0.1437 S23: 0.0454
REMARK 3 S31: -0.0439 S32: 0.0100 S33: -0.0198
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 : A 314 A 367
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7906 2.4040 47.5396
REMARK 3 T TENSOR
REMARK 3 T11: 0.3114 T22: 0.2826
REMARK 3 T33: 0.0579 T12: 0.0979
REMARK 3 T13: 0.0461 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 4.0891 L22: 5.6449
REMARK 3 L33: 2.3970 L12: 1.4940
REMARK 3 L13: -1.4632 L23: -1.0861
REMARK 3 S TENSOR
REMARK 3 S11: 0.2907 S12: 0.0922 S13: 0.0632
REMARK 3 S21: -0.0371 S22: -0.1750 S23: -0.0382
REMARK 3 S31: -0.2830 S32: 0.4204 S33: -0.1158
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 185 B 229
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2593 -14.1752 7.5473
REMARK 3 T TENSOR
REMARK 3 T11: 0.2506 T22: 0.2794
REMARK 3 T33: 0.1673 T12: 0.0194
REMARK 3 T13: 0.0573 T23: -0.0852
REMARK 3 L TENSOR
REMARK 3 L11: 10.2068 L22: 12.0148
REMARK 3 L33: 6.3898 L12: -7.6787
REMARK 3 L13: 4.2494 L23: -4.6106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1221 S12: 0.3075 S13: -0.1868
REMARK 3 S21: -0.7141 S22: 0.0766 S23: 0.3837
REMARK 3 S31: 0.2836 S32: -0.1628 S33: -0.1986
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 230 B 270
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9108 -0.7335 21.7799
REMARK 3 T TENSOR
REMARK 3 T11: 0.2926 T22: 0.2203
REMARK 3 T33: 0.1490 T12: 0.0882
REMARK 3 T13: 0.0566 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 6.2677 L22: 3.4227
REMARK 3 L33: 4.7445 L12: -0.6355
REMARK 3 L13: -0.0421 L23: 1.2639
REMARK 3 S TENSOR
REMARK 3 S11: 0.1629 S12: -0.1866 S13: 0.3693
REMARK 3 S21: -0.0181 S22: 0.0748 S23: 0.4192
REMARK 3 S31: -0.1766 S32: -0.2816 S33: -0.2377
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 271 B 313
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6253 -6.6129 23.4042
REMARK 3 T TENSOR
REMARK 3 T11: 0.2682 T22: 0.2713
REMARK 3 T33: 0.0644 T12: 0.0944
REMARK 3 T13: 0.0407 T23: -0.0654
REMARK 3 L TENSOR
REMARK 3 L11: 7.8578 L22: 6.8522
REMARK 3 L33: 4.3267 L12: 2.2589
REMARK 3 L13: 1.1673 L23: -0.1432
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: -0.7466 S13: -0.0080
REMARK 3 S21: 0.3700 S22: 0.0937 S23: -0.2468
REMARK 3 S31: -0.2886 S32: 0.2300 S33: -0.0467
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 314 B 367
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6649 -6.7585 13.6847
REMARK 3 T TENSOR
REMARK 3 T11: 0.3427 T22: 0.2746
REMARK 3 T33: 0.1035 T12: 0.0729
REMARK 3 T13: 0.1010 T23: -0.0566
REMARK 3 L TENSOR
REMARK 3 L11: 5.1781 L22: 3.7108
REMARK 3 L33: 1.7586 L12: 0.0496
REMARK 3 L13: 0.8739 L23: 0.5108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0597 S12: -0.0028 S13: 0.2399
REMARK 3 S21: 0.1206 S22: 0.2711 S23: -0.3436
REMARK 3 S31: -0.4219 S32: 0.4059 S33: -0.2114
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 185 C 229
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3328 12.4674 67.1744
REMARK 3 T TENSOR
REMARK 3 T11: 0.2904 T22: 0.2202
REMARK 3 T33: 0.1141 T12: -0.0095
REMARK 3 T13: 0.0002 T23: -0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 7.4492 L22: 6.2457
REMARK 3 L33: 5.5262 L12: 4.0856
REMARK 3 L13: -3.2541 L23: -3.1461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0375 S12: 0.4507 S13: 0.1903
REMARK 3 S21: -0.0959 S22: 0.0962 S23: 0.0763
REMARK 3 S31: -0.1586 S32: -0.1721 S33: -0.0587
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 230 C 270
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4680 23.7585 81.5082
REMARK 3 T TENSOR
REMARK 3 T11: 0.3295 T22: 0.3237
REMARK 3 T33: 0.1565 T12: -0.1257
REMARK 3 T13: -0.0027 T23: -0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 1.3662 L22: 4.7993
REMARK 3 L33: 2.7907 L12: -0.3579
REMARK 3 L13: -0.5189 L23: -0.3410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: -0.0801 S13: 0.3698
REMARK 3 S21: 0.3302 S22: -0.0091 S23: -0.3198
REMARK 3 S31: -0.3863 S32: 0.3633 S33: 0.0096
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 271 C 313
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1193 12.0103 83.5316
REMARK 3 T TENSOR
REMARK 3 T11: 0.2814 T22: 0.2438
REMARK 3 T33: 0.0468 T12: -0.0881
REMARK 3 T13: 0.0695 T23: -0.0468
REMARK 3 L TENSOR
REMARK 3 L11: 4.5807 L22: 4.3773
REMARK 3 L33: 2.2628 L12: -2.6906
REMARK 3 L13: 0.9338 L23: -0.3131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0786 S12: -0.5415 S13: -0.1372
REMARK 3 S21: 0.3586 S22: 0.1159 S23: 0.1122
REMARK 3 S31: 0.0415 S32: -0.0109 S33: -0.0373
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 314 C 367
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2540 7.5648 74.2717
REMARK 3 T TENSOR
REMARK 3 T11: 0.2999 T22: 0.3666
REMARK 3 T33: 0.1056 T12: -0.0715
REMARK 3 T13: 0.0134 T23: -0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 0.9725 L22: 4.1395
REMARK 3 L33: 1.6589 L12: 0.1547
REMARK 3 L13: 1.2301 L23: -0.3692
REMARK 3 S TENSOR
REMARK 3 S11: 0.2085 S12: 0.0803 S13: -0.1467
REMARK 3 S21: 0.0286 S22: -0.0344 S23: -0.0654
REMARK 3 S31: 0.2116 S32: 0.1978 S33: -0.1741
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 185 D 229
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4330 24.4235 114.1812
REMARK 3 T TENSOR
REMARK 3 T11: 0.3520 T22: 0.3042
REMARK 3 T33: 0.2624 T12: -0.0757
REMARK 3 T13: -0.0533 T23: -0.1100
REMARK 3 L TENSOR
REMARK 3 L11: 4.1167 L22: 8.7908
REMARK 3 L33: 6.3795 L12: -0.0355
REMARK 3 L13: -0.9861 L23: -4.4628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: -0.3520 S13: -0.0702
REMARK 3 S21: 0.4743 S22: -0.0003 S23: 0.2158
REMARK 3 S31: -0.1158 S32: -0.0396 S33: -0.0097
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 230 D 270
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7708 10.6227 99.7110
REMARK 3 T TENSOR
REMARK 3 T11: 0.3295 T22: 0.3272
REMARK 3 T33: 0.2243 T12: -0.0168
REMARK 3 T13: -0.0348 T23: -0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 4.5409 L22: 2.3712
REMARK 3 L33: 2.9532 L12: 0.8704
REMARK 3 L13: 0.7411 L23: 1.1667
REMARK 3 S TENSOR
REMARK 3 S11: 0.1897 S12: 0.1130 S13: -0.4746
REMARK 3 S21: 0.0617 S22: 0.1482 S23: 0.1539
REMARK 3 S31: 0.1665 S32: -0.2407 S33: -0.3379
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 271 D 313
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6760 17.4947 98.3094
REMARK 3 T TENSOR
REMARK 3 T11: 0.2395 T22: 0.2837
REMARK 3 T33: 0.1281 T12: -0.0291
REMARK 3 T13: -0.0348 T23: -0.1160
REMARK 3 L TENSOR
REMARK 3 L11: 6.7423 L22: 8.5102
REMARK 3 L33: 5.6196 L12: -1.3418
REMARK 3 L13: -1.4751 L23: 0.0289
REMARK 3 S TENSOR
REMARK 3 S11: 0.2671 S12: 0.6645 S13: -0.1223
REMARK 3 S21: -0.4749 S22: -0.0909 S23: -0.4794
REMARK 3 S31: 0.0741 S32: 0.2140 S33: -0.1762
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 314 D 367
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6559 17.7795 108.0807
REMARK 3 T TENSOR
REMARK 3 T11: 0.3364 T22: 0.3026
REMARK 3 T33: 0.2243 T12: -0.0343
REMARK 3 T13: -0.1140 T23: -0.0751
REMARK 3 L TENSOR
REMARK 3 L11: 5.3891 L22: 4.4674
REMARK 3 L33: 3.7610 L12: 0.2779
REMARK 3 L13: -1.1411 L23: -0.3140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0622 S12: 0.0959 S13: -0.4853
REMARK 3 S21: -0.0513 S22: -0.0946 S23: -0.5375
REMARK 3 S31: 0.3585 S32: 0.4117 S33: 0.0324
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 WITH TLS ADDED. ATOM RECORD CONTAINS SUM OF
REMARK 3 TLS AND RESIDUAL B FACTORS
REMARK 4
REMARK 4 2XD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1290043785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45536
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 41.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 1YD9, 1ZR3, 1ZR5, 3IID
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MGCL2; 0.1M HEPES PH 7.5; 30%
REMARK 280 MPEG 550
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 28.51500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.51500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.82000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASP A 177
REMARK 465 ASP B 177
REMARK 465 SER D 316
REMARK 465 GLY D 317
REMARK 465 ARG D 318
REMARK 465 ASN D 319
REMARK 465 CYS D 320
REMARK 465 LEU D 369
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 ASP A 181 CG OD1 OD2
REMARK 470 ILE A 204 CG1 CG2 CD1
REMARK 470 SER A 209 OG
REMARK 470 ARG A 211 NE CZ NH1 NH2
REMARK 470 LYS A 226 CG CD CE NZ
REMARK 470 GLU A 243 CG CD OE1 OE2
REMARK 470 GLU A 247 CG CD OE1 OE2
REMARK 470 LYS A 250 CG CD CE NZ
REMARK 470 SER A 251 OG
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 SER A 266 OG
REMARK 470 GLU A 288 CG CD OE1 OE2
REMARK 470 ARG A 318 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 369 CG CD1 CD2
REMARK 470 ASP B 181 CG OD1 OD2
REMARK 470 ILE B 204 CG1 CG2 CD1
REMARK 470 SER B 209 OG
REMARK 470 ARG B 211 NE CZ NH1 NH2
REMARK 470 LYS B 226 CG CD CE NZ
REMARK 470 LYS B 239 CG CD CE NZ
REMARK 470 GLU B 243 CG CD OE1 OE2
REMARK 470 GLU B 247 CG CD OE1 OE2
REMARK 470 LYS B 250 CG CD CE NZ
REMARK 470 SER B 251 OG
REMARK 470 GLU B 256 CG CD OE1 OE2
REMARK 470 SER B 266 OG
REMARK 470 GLU B 288 CG CD OE1 OE2
REMARK 470 ARG B 318 CG CD NE CZ NH1 NH2
REMARK 470 SER B 342 OG
REMARK 470 LEU B 369 CG CD1 CD2
REMARK 470 ASP C 177 CG OD1 OD2
REMARK 470 ASP C 181 CG OD1 OD2
REMARK 470 ILE C 204 CG1 CG2 CD1
REMARK 470 SER C 209 OG
REMARK 470 ARG C 211 NE CZ NH1 NH2
REMARK 470 LYS C 226 CG CD CE NZ
REMARK 470 GLU C 243 CG CD OE1 OE2
REMARK 470 GLU C 247 CG CD OE1 OE2
REMARK 470 LYS C 250 CG CD CE NZ
REMARK 470 SER C 251 OG
REMARK 470 GLU C 256 CG CD OE1 OE2
REMARK 470 SER C 266 OG
REMARK 470 GLU C 288 CG CD OE1 OE2
REMARK 470 LEU C 369 CG CD1 CD2
REMARK 470 ASP D 181 CG OD1 OD2
REMARK 470 ASP D 203 CG OD1 OD2
REMARK 470 ILE D 204 CG1 CG2 CD1
REMARK 470 SER D 209 OG
REMARK 470 ARG D 211 NE CZ NH1 NH2
REMARK 470 LYS D 226 CG CD CE NZ
REMARK 470 LYS D 239 CG CD CE NZ
REMARK 470 GLU D 240 CG CD OE1 OE2
REMARK 470 GLU D 243 CG CD OE1 OE2
REMARK 470 LYS D 250 CG CD CE NZ
REMARK 470 SER D 251 OG
REMARK 470 SER D 266 OG
REMARK 470 GLN D 280 CG CD OE1 NE2
REMARK 470 TRP D 281 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 281 CZ3 CH2
REMARK 470 ASP D 284 CG OD1 OD2
REMARK 470 LYS D 285 CG CD CE NZ
REMARK 470 GLU D 288 CG CD OE1 OE2
REMARK 470 SER D 342 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH2 ARG D 249 O HOH D 2009 1.58
REMARK 500 OG1 THR C 220 OD1 ASP C 224 1.94
REMARK 500 O LEU B 346 O HOH B 2040 2.01
REMARK 500 O LEU B 268 O HOH B 2017 2.01
REMARK 500 OG1 THR D 220 OD1 ASP D 224 2.02
REMARK 500 OG1 THR A 220 OD1 ASP A 224 2.03
REMARK 500 OG1 THR B 220 OD1 ASP B 224 2.04
REMARK 500 O HOH C 2004 O HOH C 2012 2.06
REMARK 500 OE2 GLU A 227 N GLY A 230 2.07
REMARK 500 O ALA D 367 O HOH D 2031 2.15
REMARK 500 OD1 ASN A 296 O HOH A 2030 2.16
REMARK 500 O SER B 344 O HOH B 2038 2.17
REMARK 500 O HOH A 2017 O HOH A 2025 2.18
REMARK 500 O HOH B 2013 O HOH B 2016 2.19
REMARK 500 OE2 GLU A 291 O HOH A 2029 2.19
REMARK 500 O VAL A 192 O HOH A 2004 2.19
REMARK 500 NE2 GLN A 264 O HOH A 2019 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 297 CB CYS B 297 SG -0.106
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 GLN A 252 -61.51 -120.23
REMARK 500 ALA A 258 -7.70 77.65
REMARK 500 LYS A 368 92.42 -68.36
REMARK 500 SER B 202 -176.45 -170.38
REMARK 500 GLN B 252 -65.85 -120.24
REMARK 500 ALA B 258 -8.59 76.23
REMARK 500 ARG B 318 -60.97 -104.47
REMARK 500 ASN B 319 20.99 -77.74
REMARK 500 ASP C 181 125.04 -39.76
REMARK 500 ALA C 258 -12.63 80.65
REMARK 500 GLN D 252 -65.47 -120.93
REMARK 500 ALA D 258 -6.12 71.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAINS A AND B START WITH GLY178 CHAINS C AND D START WITH
REMARK 999 ASP177
DBREF 2XD7 A 177 369 UNP Q9P0M6 H2AW_HUMAN 177 369
DBREF 2XD7 B 177 369 UNP Q9P0M6 H2AW_HUMAN 177 369
DBREF 2XD7 C 177 369 UNP Q9P0M6 H2AW_HUMAN 177 369
DBREF 2XD7 D 177 369 UNP Q9P0M6 H2AW_HUMAN 177 369
SEQRES 1 A 193 ASP GLY PRO GLY ASP GLY PHE THR ILE LEU SER SER LYS
SEQRES 2 A 193 SER LEU VAL LEU GLY GLN LYS LEU SER LEU THR GLN SER
SEQRES 3 A 193 ASP ILE SER HIS ILE GLY SER MET ARG VAL GLU GLY ILE
SEQRES 4 A 193 VAL HIS PRO THR THR ALA GLU ILE ASP LEU LYS GLU ASP
SEQRES 5 A 193 ILE GLY LYS ALA LEU GLU LYS ALA GLY GLY LYS GLU PHE
SEQRES 6 A 193 LEU GLU THR VAL LYS GLU LEU ARG LYS SER GLN GLY PRO
SEQRES 7 A 193 LEU GLU VAL ALA GLU ALA ALA VAL SER GLN SER SER GLY
SEQRES 8 A 193 LEU ALA ALA LYS PHE VAL ILE HIS CYS HIS ILE PRO GLN
SEQRES 9 A 193 TRP GLY SER ASP LYS CYS GLU GLU GLN LEU GLU GLU THR
SEQRES 10 A 193 ILE LYS ASN CYS LEU SER ALA ALA GLU ASP LYS LYS LEU
SEQRES 11 A 193 LYS SER VAL ALA PHE PRO PRO PHE PRO SER GLY ARG ASN
SEQRES 12 A 193 CYS PHE PRO LYS GLN THR ALA ALA GLN VAL THR LEU LYS
SEQRES 13 A 193 ALA ILE SER ALA HIS PHE ASP ASP SER SER ALA SER SER
SEQRES 14 A 193 LEU LYS ASN VAL TYR PHE LEU LEU PHE ASP SER GLU SER
SEQRES 15 A 193 ILE GLY ILE TYR VAL GLN GLU MET ALA LYS LEU
SEQRES 1 B 193 ASP GLY PRO GLY ASP GLY PHE THR ILE LEU SER SER LYS
SEQRES 2 B 193 SER LEU VAL LEU GLY GLN LYS LEU SER LEU THR GLN SER
SEQRES 3 B 193 ASP ILE SER HIS ILE GLY SER MET ARG VAL GLU GLY ILE
SEQRES 4 B 193 VAL HIS PRO THR THR ALA GLU ILE ASP LEU LYS GLU ASP
SEQRES 5 B 193 ILE GLY LYS ALA LEU GLU LYS ALA GLY GLY LYS GLU PHE
SEQRES 6 B 193 LEU GLU THR VAL LYS GLU LEU ARG LYS SER GLN GLY PRO
SEQRES 7 B 193 LEU GLU VAL ALA GLU ALA ALA VAL SER GLN SER SER GLY
SEQRES 8 B 193 LEU ALA ALA LYS PHE VAL ILE HIS CYS HIS ILE PRO GLN
SEQRES 9 B 193 TRP GLY SER ASP LYS CYS GLU GLU GLN LEU GLU GLU THR
SEQRES 10 B 193 ILE LYS ASN CYS LEU SER ALA ALA GLU ASP LYS LYS LEU
SEQRES 11 B 193 LYS SER VAL ALA PHE PRO PRO PHE PRO SER GLY ARG ASN
SEQRES 12 B 193 CYS PHE PRO LYS GLN THR ALA ALA GLN VAL THR LEU LYS
SEQRES 13 B 193 ALA ILE SER ALA HIS PHE ASP ASP SER SER ALA SER SER
SEQRES 14 B 193 LEU LYS ASN VAL TYR PHE LEU LEU PHE ASP SER GLU SER
SEQRES 15 B 193 ILE GLY ILE TYR VAL GLN GLU MET ALA LYS LEU
SEQRES 1 C 193 ASP GLY PRO GLY ASP GLY PHE THR ILE LEU SER SER LYS
SEQRES 2 C 193 SER LEU VAL LEU GLY GLN LYS LEU SER LEU THR GLN SER
SEQRES 3 C 193 ASP ILE SER HIS ILE GLY SER MET ARG VAL GLU GLY ILE
SEQRES 4 C 193 VAL HIS PRO THR THR ALA GLU ILE ASP LEU LYS GLU ASP
SEQRES 5 C 193 ILE GLY LYS ALA LEU GLU LYS ALA GLY GLY LYS GLU PHE
SEQRES 6 C 193 LEU GLU THR VAL LYS GLU LEU ARG LYS SER GLN GLY PRO
SEQRES 7 C 193 LEU GLU VAL ALA GLU ALA ALA VAL SER GLN SER SER GLY
SEQRES 8 C 193 LEU ALA ALA LYS PHE VAL ILE HIS CYS HIS ILE PRO GLN
SEQRES 9 C 193 TRP GLY SER ASP LYS CYS GLU GLU GLN LEU GLU GLU THR
SEQRES 10 C 193 ILE LYS ASN CYS LEU SER ALA ALA GLU ASP LYS LYS LEU
SEQRES 11 C 193 LYS SER VAL ALA PHE PRO PRO PHE PRO SER GLY ARG ASN
SEQRES 12 C 193 CYS PHE PRO LYS GLN THR ALA ALA GLN VAL THR LEU LYS
SEQRES 13 C 193 ALA ILE SER ALA HIS PHE ASP ASP SER SER ALA SER SER
SEQRES 14 C 193 LEU LYS ASN VAL TYR PHE LEU LEU PHE ASP SER GLU SER
SEQRES 15 C 193 ILE GLY ILE TYR VAL GLN GLU MET ALA LYS LEU
SEQRES 1 D 193 ASP GLY PRO GLY ASP GLY PHE THR ILE LEU SER SER LYS
SEQRES 2 D 193 SER LEU VAL LEU GLY GLN LYS LEU SER LEU THR GLN SER
SEQRES 3 D 193 ASP ILE SER HIS ILE GLY SER MET ARG VAL GLU GLY ILE
SEQRES 4 D 193 VAL HIS PRO THR THR ALA GLU ILE ASP LEU LYS GLU ASP
SEQRES 5 D 193 ILE GLY LYS ALA LEU GLU LYS ALA GLY GLY LYS GLU PHE
SEQRES 6 D 193 LEU GLU THR VAL LYS GLU LEU ARG LYS SER GLN GLY PRO
SEQRES 7 D 193 LEU GLU VAL ALA GLU ALA ALA VAL SER GLN SER SER GLY
SEQRES 8 D 193 LEU ALA ALA LYS PHE VAL ILE HIS CYS HIS ILE PRO GLN
SEQRES 9 D 193 TRP GLY SER ASP LYS CYS GLU GLU GLN LEU GLU GLU THR
SEQRES 10 D 193 ILE LYS ASN CYS LEU SER ALA ALA GLU ASP LYS LYS LEU
SEQRES 11 D 193 LYS SER VAL ALA PHE PRO PRO PHE PRO SER GLY ARG ASN
SEQRES 12 D 193 CYS PHE PRO LYS GLN THR ALA ALA GLN VAL THR LEU LYS
SEQRES 13 D 193 ALA ILE SER ALA HIS PHE ASP ASP SER SER ALA SER SER
SEQRES 14 D 193 LEU LYS ASN VAL TYR PHE LEU LEU PHE ASP SER GLU SER
SEQRES 15 D 193 ILE GLY ILE TYR VAL GLN GLU MET ALA LYS LEU
FORMUL 5 HOH *176(H2 O)
HELIX 1 1 ASP A 203 MET A 210 5 8
HELIX 2 2 GLU A 227 GLN A 252 1 26
HELIX 3 3 LYS A 285 LYS A 304 1 20
HELIX 4 4 PRO A 322 SER A 341 1 20
HELIX 5 5 ASP A 355 LYS A 368 1 14
HELIX 6 6 ASP B 203 MET B 210 5 8
HELIX 7 7 GLU B 227 GLN B 252 1 26
HELIX 8 8 LYS B 285 LYS B 304 1 20
HELIX 9 9 PRO B 322 SER B 341 1 20
HELIX 10 10 ASP B 355 LYS B 368 1 14
HELIX 11 11 ASP C 203 MET C 210 5 8
HELIX 12 12 GLU C 227 GLN C 252 1 26
HELIX 13 13 LYS C 285 LYS C 304 1 20
HELIX 14 14 PRO C 322 SER C 341 1 20
HELIX 15 15 ASP C 355 LYS C 368 1 14
HELIX 16 16 ASP D 203 MET D 210 5 8
HELIX 17 17 GLU D 227 GLN D 252 1 26
HELIX 18 18 LYS D 285 LYS D 304 1 20
HELIX 19 19 PRO D 322 SER D 341 1 20
HELIX 20 20 ASP D 355 LYS D 368 1 14
SHEET 1 AA 7 THR A 184 SER A 190 0
SHEET 2 AA 7 LYS A 196 GLN A 201 -1 O LEU A 197 N LYS A 189
SHEET 3 AA 7 ASN A 348 LEU A 353 1 O VAL A 349 N SER A 198
SHEET 4 AA 7 SER A 308 PHE A 311 1 O VAL A 309 N TYR A 350
SHEET 5 AA 7 GLY A 214 THR A 219 1 O GLY A 214 N ALA A 310
SHEET 6 AA 7 PHE A 272 HIS A 277 1 O PHE A 272 N ILE A 215
SHEET 7 AA 7 ALA A 260 GLN A 264 -1 O ALA A 261 N HIS A 275
SHEET 1 BA 7 THR B 184 SER B 190 0
SHEET 2 BA 7 LYS B 196 GLN B 201 -1 O LEU B 197 N LYS B 189
SHEET 3 BA 7 ASN B 348 LEU B 353 1 O VAL B 349 N SER B 198
SHEET 4 BA 7 SER B 308 PHE B 311 1 O VAL B 309 N TYR B 350
SHEET 5 BA 7 GLY B 214 THR B 219 1 O GLY B 214 N ALA B 310
SHEET 6 BA 7 PHE B 272 HIS B 277 1 O PHE B 272 N ILE B 215
SHEET 7 BA 7 ALA B 260 GLN B 264 -1 O ALA B 261 N HIS B 275
SHEET 1 CA 7 THR C 184 SER C 190 0
SHEET 2 CA 7 LYS C 196 GLN C 201 -1 O LEU C 197 N LYS C 189
SHEET 3 CA 7 ASN C 348 LEU C 353 1 O VAL C 349 N SER C 198
SHEET 4 CA 7 SER C 308 PHE C 311 1 O VAL C 309 N TYR C 350
SHEET 5 CA 7 GLY C 214 THR C 219 1 O GLY C 214 N ALA C 310
SHEET 6 CA 7 PHE C 272 HIS C 277 1 O PHE C 272 N ILE C 215
SHEET 7 CA 7 ALA C 260 GLN C 264 -1 O ALA C 261 N HIS C 275
SHEET 1 DA 7 THR D 184 SER D 190 0
SHEET 2 DA 7 LYS D 196 GLN D 201 -1 O LEU D 197 N LYS D 189
SHEET 3 DA 7 ASN D 348 LEU D 353 1 O VAL D 349 N SER D 198
SHEET 4 DA 7 SER D 308 PHE D 311 1 O VAL D 309 N TYR D 350
SHEET 5 DA 7 GLY D 214 THR D 219 1 O GLY D 214 N ALA D 310
SHEET 6 DA 7 PHE D 272 HIS D 277 1 O PHE D 272 N ILE D 215
SHEET 7 DA 7 ALA D 260 GLN D 264 -1 O ALA D 261 N HIS D 275
CISPEP 1 GLY A 253 PRO A 254 0 5.66
CISPEP 2 GLY B 253 PRO B 254 0 4.60
CISPEP 3 GLY C 253 PRO C 254 0 7.54
CISPEP 4 GLY D 253 PRO D 254 0 5.22
CRYST1 57.030 61.640 242.230 90.00 89.64 90.00 C 1 2 1 16
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 0.017535 0.000000 -0.000110 0.00000
SCALE2 0.000000 0.016223 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004128 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
