HEADER DNA BINDING PROTEIN 13-OCT-14 4WNN
TITLE SPT16-H2A-H2B FACT HISTONE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H2A.1;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H2B.1;
COMPND 7 CHAIN: B, D, F, H;
COMPND 8 FRAGMENT: UNP RESIDUES 31-131;
COMPND 9 SYNONYM: SUPPRESSOR OF TY PROTEIN 12;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: SPT16;
COMPND 13 CHAIN: T;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: HTA1, H2A1, SPT11, YDR225W, YD9934.10;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 559292;
SOURCE 13 STRAIN: ATCC 204508 / S288C;
SOURCE 14 GENE: HTB1, H2B1, SPT12, YDR224C, YD9934.09C;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FACT, SPT16, HISTONE, POB3, H2A, H2B, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.KEMBLE,C.P.HILL,F.G.WHITBY,T.FORMOSA,L.L.MCCULLOUGH
REVDAT 4 04-DEC-19 4WNN 1 REMARK
REVDAT 3 27-SEP-17 4WNN 1 JRNL REMARK
REVDAT 2 28-OCT-15 4WNN 1 JRNL
REVDAT 1 21-OCT-15 4WNN 0
JRNL AUTH D.J.KEMBLE,L.L.MCCULLOUGH,F.G.WHITBY,T.FORMOSA,C.P.HILL
JRNL TITL FACT DISRUPTS NUCLEOSOME STRUCTURE BY BINDING H2A-H2B WITH
JRNL TITL 2 CONSERVED PEPTIDE MOTIFS.
JRNL REF MOL.CELL V. 60 294 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 26455391
JRNL DOI 10.1016/J.MOLCEL.2015.09.008
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 77580
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3900
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 21.2243 - 5.4133 0.88 2349 137 0.1657 0.2019
REMARK 3 2 5.4133 - 4.3085 0.98 2637 145 0.1413 0.1803
REMARK 3 3 4.3085 - 3.7673 0.98 2650 125 0.1530 0.1940
REMARK 3 4 3.7673 - 3.4245 0.99 2623 132 0.1606 0.1999
REMARK 3 5 3.4245 - 3.1799 1.00 2688 137 0.1892 0.2958
REMARK 3 6 3.1799 - 2.9929 1.00 2679 143 0.1975 0.2448
REMARK 3 7 2.9929 - 2.8434 1.00 2654 167 0.1886 0.2297
REMARK 3 8 2.8434 - 2.7199 1.00 2661 125 0.1830 0.2163
REMARK 3 9 2.7199 - 2.6154 1.00 2638 138 0.1808 0.2197
REMARK 3 10 2.6154 - 2.5253 1.00 2678 153 0.1797 0.2066
REMARK 3 11 2.5253 - 2.4464 1.00 2682 141 0.1784 0.2233
REMARK 3 12 2.4464 - 2.3766 1.00 2654 162 0.1867 0.2448
REMARK 3 13 2.3766 - 2.3141 1.00 2702 123 0.1884 0.2536
REMARK 3 14 2.3141 - 2.2577 1.00 2630 152 0.1911 0.2413
REMARK 3 15 2.2577 - 2.2065 1.00 2685 126 0.1987 0.2326
REMARK 3 16 2.2065 - 2.1595 1.00 2689 140 0.1796 0.2299
REMARK 3 17 2.1595 - 2.1164 1.00 2655 139 0.1863 0.2414
REMARK 3 18 2.1164 - 2.0765 1.00 2683 125 0.1864 0.2186
REMARK 3 19 2.0765 - 2.0394 1.00 2719 138 0.1964 0.2038
REMARK 3 20 2.0394 - 2.0049 1.00 2673 120 0.1995 0.2484
REMARK 3 21 2.0049 - 1.9726 1.00 2656 151 0.2150 0.3007
REMARK 3 22 1.9726 - 1.9422 1.00 2661 159 0.2516 0.3259
REMARK 3 23 1.9422 - 1.9137 1.00 2701 144 0.2534 0.3117
REMARK 3 24 1.9137 - 1.8868 1.00 2623 126 0.3001 0.3523
REMARK 3 25 1.8868 - 1.8613 0.98 2607 155 0.3282 0.3991
REMARK 3 26 1.8613 - 1.8371 0.97 2642 124 0.2748 0.2995
REMARK 3 27 1.8371 - 1.8142 0.95 2497 141 0.2719 0.2841
REMARK 3 28 1.8142 - 1.8000 0.84 2264 132 0.2832 0.3409
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 5853
REMARK 3 ANGLE : 0.952 7871
REMARK 3 CHIRALITY : 0.039 906
REMARK 3 PLANARITY : 0.005 997
REMARK 3 DIHEDRAL : 13.663 2256
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6745 -6.7327 -32.1876
REMARK 3 T TENSOR
REMARK 3 T11: 0.2261 T22: 0.2678
REMARK 3 T33: 0.2556 T12: 0.0215
REMARK 3 T13: -0.0037 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.5860 L22: 0.6357
REMARK 3 L33: 0.7295 L12: 0.1995
REMARK 3 L13: 0.0803 L23: 0.2432
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: 0.1093 S13: -0.0999
REMARK 3 S21: -0.0332 S22: -0.0360 S23: -0.1065
REMARK 3 S31: 0.0889 S32: -0.0423 S33: 0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WNN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-11
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 : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.127090
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77661
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.92800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1ID3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF ~ 60 X 60 MM FORMED WITHIN
REMARK 280 10 DAYS IN 0.1M SPG (SUCCINIC ACID:SODIUM DIHYDROGEN PHOSPHATE:
REMARK 280 GLYCINE ) PH 7, 25 % PEG 1500 (A4 OF THE PACT SUITE COMMERCIAL
REMARK 280 SCREEN (QIAGEN)., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.83350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.65814
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.49000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 54.83350
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 31.65814
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 62.49000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 54.83350
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 31.65814
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.49000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.31627
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 124.98000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 63.31627
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 124.98000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 63.31627
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 124.98000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 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: 4990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, T
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 MET A 0
REMARK 465 SER A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 LYS A 13
REMARK 465 ALA A 14
REMARK 465 SER A 15
REMARK 465 THR A 102
REMARK 465 ILE A 103
REMARK 465 ALA A 104
REMARK 465 GLN A 105
REMARK 465 GLY A 106
REMARK 465 GLY A 107
REMARK 465 VAL A 108
REMARK 465 LEU A 109
REMARK 465 PRO A 110
REMARK 465 ASN A 111
REMARK 465 ILE A 112
REMARK 465 HIS A 113
REMARK 465 GLN A 114
REMARK 465 ASN A 115
REMARK 465 LEU A 116
REMARK 465 LEU A 117
REMARK 465 PRO A 118
REMARK 465 LYS A 119
REMARK 465 LYS A 120
REMARK 465 SER A 121
REMARK 465 ALA A 122
REMARK 465 LYS A 123
REMARK 465 ALA A 124
REMARK 465 THR A 125
REMARK 465 LYS A 126
REMARK 465 ALA A 127
REMARK 465 SER A 128
REMARK 465 GLN A 129
REMARK 465 GLU A 130
REMARK 465 LEU A 131
REMARK 465 SER B 127
REMARK 465 THR B 128
REMARK 465 GLN B 129
REMARK 465 ALA B 130
REMARK 465 MET C 0
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 GLY C 3
REMARK 465 LYS C 4
REMARK 465 GLY C 5
REMARK 465 GLY C 6
REMARK 465 LYS C 7
REMARK 465 ALA C 8
REMARK 465 GLY C 9
REMARK 465 SER C 10
REMARK 465 ALA C 11
REMARK 465 ALA C 12
REMARK 465 LYS C 13
REMARK 465 ALA C 14
REMARK 465 SER C 15
REMARK 465 GLN C 16
REMARK 465 ASN C 100
REMARK 465 VAL C 101
REMARK 465 THR C 102
REMARK 465 ILE C 103
REMARK 465 ALA C 104
REMARK 465 GLN C 105
REMARK 465 GLY C 106
REMARK 465 GLY C 107
REMARK 465 VAL C 108
REMARK 465 LEU C 109
REMARK 465 PRO C 110
REMARK 465 ASN C 111
REMARK 465 ILE C 112
REMARK 465 HIS C 113
REMARK 465 GLN C 114
REMARK 465 ASN C 115
REMARK 465 LEU C 116
REMARK 465 LEU C 117
REMARK 465 PRO C 118
REMARK 465 LYS C 119
REMARK 465 LYS C 120
REMARK 465 SER C 121
REMARK 465 ALA C 122
REMARK 465 LYS C 123
REMARK 465 ALA C 124
REMARK 465 THR C 125
REMARK 465 LYS C 126
REMARK 465 ALA C 127
REMARK 465 SER C 128
REMARK 465 GLN C 129
REMARK 465 GLU C 130
REMARK 465 LEU C 131
REMARK 465 MET D 29
REMARK 465 SER D 127
REMARK 465 THR D 128
REMARK 465 GLN D 129
REMARK 465 ALA D 130
REMARK 465 MET E 0
REMARK 465 SER E 1
REMARK 465 GLY E 2
REMARK 465 GLY E 3
REMARK 465 LYS E 4
REMARK 465 GLY E 5
REMARK 465 GLY E 6
REMARK 465 LYS E 7
REMARK 465 ALA E 8
REMARK 465 GLY E 9
REMARK 465 SER E 10
REMARK 465 ALA E 11
REMARK 465 ALA E 12
REMARK 465 LYS E 13
REMARK 465 ALA E 14
REMARK 465 SER E 15
REMARK 465 GLN E 16
REMARK 465 ASN E 100
REMARK 465 VAL E 101
REMARK 465 THR E 102
REMARK 465 ILE E 103
REMARK 465 ALA E 104
REMARK 465 GLN E 105
REMARK 465 GLY E 106
REMARK 465 GLY E 107
REMARK 465 VAL E 108
REMARK 465 LEU E 109
REMARK 465 PRO E 110
REMARK 465 ASN E 111
REMARK 465 ILE E 112
REMARK 465 HIS E 113
REMARK 465 GLN E 114
REMARK 465 ASN E 115
REMARK 465 LEU E 116
REMARK 465 LEU E 117
REMARK 465 PRO E 118
REMARK 465 LYS E 119
REMARK 465 LYS E 120
REMARK 465 SER E 121
REMARK 465 ALA E 122
REMARK 465 LYS E 123
REMARK 465 ALA E 124
REMARK 465 THR E 125
REMARK 465 LYS E 126
REMARK 465 ALA E 127
REMARK 465 SER E 128
REMARK 465 GLN E 129
REMARK 465 GLU E 130
REMARK 465 LEU E 131
REMARK 465 SER F 127
REMARK 465 THR F 128
REMARK 465 GLN F 129
REMARK 465 ALA F 130
REMARK 465 MET G 0
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 GLY G 3
REMARK 465 LYS G 4
REMARK 465 GLY G 5
REMARK 465 GLY G 6
REMARK 465 LYS G 7
REMARK 465 ALA G 8
REMARK 465 GLY G 9
REMARK 465 SER G 10
REMARK 465 ALA G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 13
REMARK 465 ALA G 14
REMARK 465 SER G 15
REMARK 465 GLN G 16
REMARK 465 GLY G 99
REMARK 465 ASN G 100
REMARK 465 VAL G 101
REMARK 465 THR G 102
REMARK 465 ILE G 103
REMARK 465 ALA G 104
REMARK 465 GLN G 105
REMARK 465 GLY G 106
REMARK 465 GLY G 107
REMARK 465 VAL G 108
REMARK 465 LEU G 109
REMARK 465 PRO G 110
REMARK 465 ASN G 111
REMARK 465 ILE G 112
REMARK 465 HIS G 113
REMARK 465 GLN G 114
REMARK 465 ASN G 115
REMARK 465 LEU G 116
REMARK 465 LEU G 117
REMARK 465 PRO G 118
REMARK 465 LYS G 119
REMARK 465 LYS G 120
REMARK 465 SER G 121
REMARK 465 ALA G 122
REMARK 465 LYS G 123
REMARK 465 ALA G 124
REMARK 465 THR G 125
REMARK 465 LYS G 126
REMARK 465 ALA G 127
REMARK 465 SER G 128
REMARK 465 GLN G 129
REMARK 465 GLU G 130
REMARK 465 LEU G 131
REMARK 465 SER H 127
REMARK 465 THR H 128
REMARK 465 GLN H 129
REMARK 465 ALA H 130
REMARK 465 GLY T 953
REMARK 465 ILE T 954
REMARK 465 LYS T 955
REMARK 465 LYS T 956
REMARK 465 THR T 957
REMARK 465 ASP T 958
REMARK 465 ASP T 959
REMARK 465 GLU T 960
REMARK 465 ALA T 961
REMARK 465 SER T 962
REMARK 465 ASP T 963
REMARK 465 GLU T 964
REMARK 465 SER T 965
REMARK 465 GLU T 966
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 OH TYR B 45 O HOH B 201 2.13
REMARK 500 OD1 ASP B 71 O HOH B 231 2.14
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 LYS G 75 83.91 56.14
REMARK 500 ARG H 32 78.11 -67.65
REMARK 500 ALA H 35 -70.73 -138.42
REMARK 500 ARG H 36 -140.76 52.00
REMARK 500 LYS H 37 78.38 -169.96
REMARK 500 GLU H 38 107.56 -17.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 337 DISTANCE = 6.12 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 201
DBREF 4WNN A 0 131 UNP P04911 H2A1_YEAST 1 132
DBREF 4WNN B 30 130 UNP P02293 H2B1_YEAST 31 131
DBREF 4WNN C 0 131 UNP P04911 H2A1_YEAST 1 132
DBREF 4WNN D 30 130 UNP P02293 H2B1_YEAST 31 131
DBREF 4WNN E 0 131 UNP P04911 H2A1_YEAST 1 132
DBREF 4WNN F 30 130 UNP P02293 H2B1_YEAST 31 131
DBREF 4WNN G 0 131 UNP P04911 H2A1_YEAST 1 132
DBREF 4WNN H 30 130 UNP P02293 H2B1_YEAST 31 131
DBREF 4WNN T 953 972 PDB 4WNN 4WNN 953 972
SEQADV 4WNN MET B 29 UNP P02293 INITIATING METHIONINE
SEQADV 4WNN MET D 29 UNP P02293 INITIATING METHIONINE
SEQADV 4WNN MET F 29 UNP P02293 INITIATING METHIONINE
SEQADV 4WNN MET H 29 UNP P02293 INITIATING METHIONINE
SEQRES 1 A 132 MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA
SEQRES 2 A 132 LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR
SEQRES 3 A 132 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY
SEQRES 4 A 132 ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR
SEQRES 5 A 132 LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU
SEQRES 6 A 132 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 7 A 132 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN
SEQRES 8 A 132 ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE
SEQRES 9 A 132 ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU
SEQRES 10 A 132 LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN
SEQRES 11 A 132 GLU LEU
SEQRES 1 B 102 MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER
SEQRES 2 B 102 SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP
SEQRES 3 B 102 THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER
SEQRES 4 B 102 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA
SEQRES 5 B 102 SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER
SEQRES 6 B 102 ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO
SEQRES 7 B 102 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG
SEQRES 8 B 102 ALA VAL THR LYS TYR SER SER SER THR GLN ALA
SEQRES 1 C 132 MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA
SEQRES 2 C 132 LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR
SEQRES 3 C 132 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY
SEQRES 4 C 132 ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR
SEQRES 5 C 132 LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU
SEQRES 6 C 132 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 7 C 132 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN
SEQRES 8 C 132 ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE
SEQRES 9 C 132 ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU
SEQRES 10 C 132 LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN
SEQRES 11 C 132 GLU LEU
SEQRES 1 D 102 MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER
SEQRES 2 D 102 SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP
SEQRES 3 D 102 THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER
SEQRES 4 D 102 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA
SEQRES 5 D 102 SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER
SEQRES 6 D 102 ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO
SEQRES 7 D 102 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG
SEQRES 8 D 102 ALA VAL THR LYS TYR SER SER SER THR GLN ALA
SEQRES 1 E 132 MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA
SEQRES 2 E 132 LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR
SEQRES 3 E 132 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY
SEQRES 4 E 132 ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR
SEQRES 5 E 132 LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU
SEQRES 6 E 132 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 7 E 132 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN
SEQRES 8 E 132 ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE
SEQRES 9 E 132 ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU
SEQRES 10 E 132 LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN
SEQRES 11 E 132 GLU LEU
SEQRES 1 F 102 MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER
SEQRES 2 F 102 SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP
SEQRES 3 F 102 THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER
SEQRES 4 F 102 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA
SEQRES 5 F 102 SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER
SEQRES 6 F 102 ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO
SEQRES 7 F 102 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG
SEQRES 8 F 102 ALA VAL THR LYS TYR SER SER SER THR GLN ALA
SEQRES 1 G 132 MET SER GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA
SEQRES 2 G 132 LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR
SEQRES 3 G 132 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY
SEQRES 4 G 132 ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR
SEQRES 5 G 132 LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU
SEQRES 6 G 132 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 7 G 132 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN
SEQRES 8 G 132 ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE
SEQRES 9 G 132 ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU
SEQRES 10 G 132 LEU PRO LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN
SEQRES 11 G 132 GLU LEU
SEQRES 1 H 102 MET LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR SER
SEQRES 2 H 102 SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO ASP
SEQRES 3 H 102 THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN SER
SEQRES 4 H 102 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU ALA
SEQRES 5 H 102 SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE SER
SEQRES 6 H 102 ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU PRO
SEQRES 7 H 102 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR ARG
SEQRES 8 H 102 ALA VAL THR LYS TYR SER SER SER THR GLN ALA
SEQRES 1 T 20 GLY ILE LYS LYS THR ASP ASP GLU ALA SER ASP GLU SER
SEQRES 2 T 20 GLU GLU GLU VAL SER GLU TYR
HET PO4 A 201 5
HET PO4 E 201 5
HETNAM PO4 PHOSPHATE ION
FORMUL 10 PO4 2(O4 P 3-)
FORMUL 12 HOH *388(H2 O)
HELIX 1 AA1 SER A 17 GLY A 23 1 7
HELIX 2 AA2 PRO A 27 GLY A 38 1 12
HELIX 3 AA3 SER A 46 ASN A 74 1 29
HELIX 4 AA4 ILE A 80 ASN A 90 1 11
HELIX 5 AA5 ASP A 91 GLY A 99 1 9
HELIX 6 AA6 TYR B 40 HIS B 52 1 13
HELIX 7 AA7 SER B 58 ASN B 87 1 30
HELIX 8 AA8 SER B 93 LEU B 105 1 13
HELIX 9 AA9 PRO B 106 SER B 126 1 21
HELIX 10 AB1 ARG C 18 GLY C 23 1 6
HELIX 11 AB2 PRO C 27 GLY C 38 1 12
HELIX 12 AB3 SER C 46 ASN C 74 1 29
HELIX 13 AB4 ILE C 80 ASN C 90 1 11
HELIX 14 AB5 ASP C 91 LEU C 98 1 8
HELIX 15 AB6 TYR D 40 HIS D 52 1 13
HELIX 16 AB7 SER D 58 ASN D 87 1 30
HELIX 17 AB8 SER D 93 LEU D 105 1 13
HELIX 18 AB9 PRO D 106 SER D 126 1 21
HELIX 19 AC1 ARG E 18 ALA E 22 1 5
HELIX 20 AC2 PRO E 27 GLY E 38 1 12
HELIX 21 AC3 SER E 46 ASN E 74 1 29
HELIX 22 AC4 ILE E 80 ASP E 91 1 12
HELIX 23 AC5 ASP E 91 GLY E 99 1 9
HELIX 24 AC6 TYR F 40 HIS F 52 1 13
HELIX 25 AC7 SER F 58 ASN F 87 1 30
HELIX 26 AC8 SER F 93 LEU F 105 1 13
HELIX 27 AC9 PRO F 106 SER F 125 1 20
HELIX 28 AD1 ARG G 18 GLY G 23 1 6
HELIX 29 AD2 PRO G 27 ARG G 37 1 11
HELIX 30 AD3 SER G 46 ARG G 72 1 27
HELIX 31 AD4 ILE G 80 ASN G 90 1 11
HELIX 32 AD5 ASP G 91 LEU G 98 1 8
HELIX 33 AD6 TYR H 40 HIS H 52 1 13
HELIX 34 AD7 SER H 58 ASN H 87 1 30
HELIX 35 AD8 SER H 93 LEU H 105 1 13
HELIX 36 AD9 PRO H 106 SER H 125 1 20
SHEET 1 AA1 2 ARG A 43 ILE A 44 0
SHEET 2 AA1 2 THR B 91 ILE B 92 1 O ILE B 92 N ARG A 43
SHEET 1 AA2 2 ARG A 78 ILE A 79 0
SHEET 2 AA2 2 GLY B 56 ILE B 57 1 O GLY B 56 N ILE A 79
SHEET 1 AA3 2 ARG C 43 ILE C 44 0
SHEET 2 AA3 2 THR D 91 ILE D 92 1 O ILE D 92 N ARG C 43
SHEET 1 AA4 2 ARG C 78 ILE C 79 0
SHEET 2 AA4 2 GLY D 56 ILE D 57 1 O GLY D 56 N ILE C 79
SHEET 1 AA5 2 ARG E 43 ILE E 44 0
SHEET 2 AA5 2 THR F 91 ILE F 92 1 O ILE F 92 N ARG E 43
SHEET 1 AA6 2 ARG E 78 ILE E 79 0
SHEET 2 AA6 2 GLY F 56 ILE F 57 1 O GLY F 56 N ILE E 79
SHEET 1 AA7 2 ARG G 43 ILE G 44 0
SHEET 2 AA7 2 THR H 91 ILE H 92 1 O ILE H 92 N ARG G 43
SHEET 1 AA8 2 ARG G 78 ILE G 79 0
SHEET 2 AA8 2 GLY H 56 ILE H 57 1 O GLY H 56 N ILE G 79
CISPEP 1 SER H 33 LYS H 34 0 26.30
SITE 1 AC1 4 THR A 77 ARG A 78 GLY B 56 ASN C 95
SITE 1 AC2 4 THR E 77 ARG E 78 GLY F 56 ASN G 95
CRYST1 109.667 109.667 187.470 90.00 90.00 120.00 H 3 36
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 0.009119 0.005265 0.000000 0.00000
SCALE2 0.000000 0.010529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005334 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
