HEADER CHAPERONE 02-JUN-15 5BT1
TITLE HISTONE CHAPERONE HIF1 PLAYING WITH HISTONE H2A-H2B DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HAT1-INTERACTING FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H2A.1;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2B.1;
COMPND 11 CHAIN: D;
COMPND 12 SYNONYM: SUPPRESSOR OF TY PROTEIN 12;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: HIF1, YLL022C, L1205;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 12 S288C);
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 GENE: HTA1, H2A1, SPT11, YDR225W, YD9934.10;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 21 S288C);
SOURCE 22 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 23 ORGANISM_TAXID: 559292;
SOURCE 24 STRAIN: ATCC 204508 / S288C;
SOURCE 25 GENE: HTB1, H2B1, SPT12, YDR224C, YD9934.09C;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HISTONE CHAPERONE COMPLEX, TPR, NASP HOMOLOG, ASSEMBLY, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LIU,M.ZHANG,Y.GAO,M.TENG,L.NIU
REVDAT 3 18-OCT-17 5BT1 1 REMARK
REVDAT 2 27-SEP-17 5BT1 1 JRNL REMARK
REVDAT 1 26-OCT-16 5BT1 0
JRNL AUTH M.ZHANG,H.LIU,Y.GAO,Z.ZHU,Z.CHEN,P.ZHENG,L.XUE,J.LI,M.TENG,
JRNL AUTH 2 L.NIU
JRNL TITL STRUCTURAL INSIGHTS INTO THE ASSOCIATION OF HIF1 WITH
JRNL TITL 2 HISTONES H2A-H2B DIMER AND H3-H4 TETRAMER
JRNL REF STRUCTURE V. 24 1810 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27618665
JRNL DOI 10.1016/J.STR.2016.08.001
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 21504
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1162
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) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1591
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5270
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.49000
REMARK 3 B22 (A**2) : -0.32000
REMARK 3 B33 (A**2) : 0.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.66000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 2.644
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.349
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.264
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.950
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5350 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7222 ; 1.049 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 662 ; 4.681 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 262 ;41.213 ;24.771
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 974 ;19.088 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;21.287 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 821 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4017 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3330 ; 0.533 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5323 ; 1.007 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2020 ; 1.225 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1899 ; 2.174 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 15 A 346
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6734 -4.1717 -63.4318
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.1012
REMARK 3 T33: 0.1156 T12: 0.0035
REMARK 3 T13: 0.0281 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.4381 L22: 1.8289
REMARK 3 L33: 0.4054 L12: 0.8305
REMARK 3 L13: 0.1576 L23: 0.4070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0596 S12: -0.0770 S13: -0.0051
REMARK 3 S21: -0.0494 S22: -0.1173 S23: -0.0400
REMARK 3 S31: 0.0105 S32: 0.0248 S33: 0.0577
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 17 B 345
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6583 -1.5173 -19.1718
REMARK 3 T TENSOR
REMARK 3 T11: 0.1218 T22: 0.0956
REMARK 3 T33: 0.1259 T12: -0.0384
REMARK 3 T13: 0.0098 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.3497 L22: 1.7246
REMARK 3 L33: 0.7952 L12: 0.0980
REMARK 3 L13: -0.1198 L23: -1.1339
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: -0.0066 S13: 0.0138
REMARK 3 S21: 0.0464 S22: -0.0116 S23: 0.0688
REMARK 3 S31: -0.0201 S32: 0.0294 S33: 0.0225
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 16 C 100
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7169 5.8583 -35.5902
REMARK 3 T TENSOR
REMARK 3 T11: 0.1171 T22: 0.1472
REMARK 3 T33: 0.1116 T12: -0.0541
REMARK 3 T13: -0.0352 T23: 0.1030
REMARK 3 L TENSOR
REMARK 3 L11: 2.0705 L22: 3.0256
REMARK 3 L33: 1.3583 L12: -0.2615
REMARK 3 L13: -0.7160 L23: -1.5927
REMARK 3 S TENSOR
REMARK 3 S11: -0.1240 S12: -0.1231 S13: -0.2801
REMARK 3 S21: 0.0431 S22: 0.0262 S23: 0.1666
REMARK 3 S31: -0.1058 S32: 0.1336 S33: 0.0978
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 37 D 126
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0209 9.8439 -38.1260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0498 T22: 0.1277
REMARK 3 T33: 0.1504 T12: -0.0455
REMARK 3 T13: -0.0022 T23: 0.0834
REMARK 3 L TENSOR
REMARK 3 L11: 1.7865 L22: 2.8296
REMARK 3 L33: 2.0138 L12: 0.2751
REMARK 3 L13: -0.2411 L23: -2.2894
REMARK 3 S TENSOR
REMARK 3 S11: -0.1616 S12: -0.1248 S13: -0.1596
REMARK 3 S21: 0.0655 S22: -0.0801 S23: -0.1094
REMARK 3 S31: -0.0885 S32: 0.1861 S33: 0.2417
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 5BT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210453.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-14
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22738
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.62600
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: 4NQ0
REMARK 200
REMARK 200 REMARK: ROD-SHAPED CRYSTALS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 22.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MAGNESIUM FORMATE DIHYDRATE, 15%
REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 51.33650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.18150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.33650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.18150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 MET A 1
REMARK 465 LYS A 2
REMARK 465 LEU A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 ASP A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 ASN A 11
REMARK 465 GLY A 12
REMARK 465 THR A 13
REMARK 465 SER A 14
REMARK 465 GLY A 80
REMARK 465 ASN A 81
REMARK 465 LEU A 82
REMARK 465 PHE A 83
REMARK 465 GLY A 84
REMARK 465 ASP A 85
REMARK 465 ALA A 86
REMARK 465 LEU A 87
REMARK 465 LEU A 88
REMARK 465 ALA A 89
REMARK 465 GLY A 90
REMARK 465 ASP A 91
REMARK 465 ASP A 92
REMARK 465 GLY A 93
REMARK 465 SER A 94
REMARK 465 GLY A 95
REMARK 465 SER A 96
REMARK 465 GLU A 97
REMARK 465 SER A 98
REMARK 465 GLU A 99
REMARK 465 SER A 100
REMARK 465 GLU A 101
REMARK 465 PRO A 102
REMARK 465 GLU A 103
REMARK 465 SER A 104
REMARK 465 ASP A 105
REMARK 465 VAL A 106
REMARK 465 SER A 107
REMARK 465 ASN A 108
REMARK 465 GLY A 109
REMARK 465 GLU A 110
REMARK 465 GLU A 111
REMARK 465 GLY A 112
REMARK 465 ASN A 113
REMARK 465 GLU A 114
REMARK 465 ASN A 115
REMARK 465 GLY A 116
REMARK 465 GLN A 117
REMARK 465 THR A 118
REMARK 465 GLU A 119
REMARK 465 ILE A 120
REMARK 465 PRO A 121
REMARK 465 ASN A 122
REMARK 465 SER A 123
REMARK 465 ARG A 124
REMARK 465 MET A 125
REMARK 465 PHE A 126
REMARK 465 GLN A 127
REMARK 465 PHE A 128
REMARK 465 ASP A 129
REMARK 465 GLN A 130
REMARK 465 GLU A 131
REMARK 465 GLU A 132
REMARK 465 GLU A 133
REMARK 465 ASP A 134
REMARK 465 LEU A 135
REMARK 465 THR A 136
REMARK 465 GLY A 137
REMARK 465 ASP A 138
REMARK 465 VAL A 139
REMARK 465 ASP A 140
REMARK 465 SER A 141
REMARK 465 GLY A 142
REMARK 465 ASP A 143
REMARK 465 SER A 144
REMARK 465 GLU A 145
REMARK 465 ASP A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
REMARK 465 GLU A 149
REMARK 465 GLY A 150
REMARK 465 SER A 151
REMARK 465 GLU A 152
REMARK 465 GLU A 153
REMARK 465 GLU A 154
REMARK 465 GLU A 155
REMARK 465 GLU A 156
REMARK 465 ASN A 157
REMARK 465 VAL A 158
REMARK 465 GLU A 159
REMARK 465 LYS A 160
REMARK 465 GLU A 161
REMARK 465 GLU A 162
REMARK 465 GLU A 163
REMARK 465 ARG A 164
REMARK 465 LEU A 165
REMARK 465 ALA A 166
REMARK 465 LEU A 167
REMARK 465 GLY A 347
REMARK 465 SER A 348
REMARK 465 LYS A 349
REMARK 465 ARG A 350
REMARK 465 PRO A 351
REMARK 465 LEU A 352
REMARK 465 SER A 353
REMARK 465 GLN A 354
REMARK 465 PRO A 355
REMARK 465 THR A 356
REMARK 465 THR A 357
REMARK 465 SER A 358
REMARK 465 ILE A 359
REMARK 465 GLY A 360
REMARK 465 PHE A 361
REMARK 465 PRO A 362
REMARK 465 ALA A 363
REMARK 465 LEU A 364
REMARK 465 GLU A 365
REMARK 465 LYS A 366
REMARK 465 PRO A 367
REMARK 465 LEU A 368
REMARK 465 GLY A 369
REMARK 465 ASP A 370
REMARK 465 PHE A 371
REMARK 465 ASN A 372
REMARK 465 ASP A 373
REMARK 465 LEU A 374
REMARK 465 SER A 375
REMARK 465 GLN A 376
REMARK 465 LEU A 377
REMARK 465 VAL A 378
REMARK 465 LYS A 379
REMARK 465 LYS A 380
REMARK 465 LYS A 381
REMARK 465 PRO A 382
REMARK 465 ARG A 383
REMARK 465 ARG A 384
REMARK 465 HIS A 385
REMARK 465 LEU A 386
REMARK 465 GLU A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 HIS A 393
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 LEU B 3
REMARK 465 ARG B 4
REMARK 465 ALA B 5
REMARK 465 GLU B 6
REMARK 465 ASP B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 ASN B 11
REMARK 465 GLY B 12
REMARK 465 THR B 13
REMARK 465 SER B 14
REMARK 465 ARG B 15
REMARK 465 HIS B 16
REMARK 465 GLY B 84
REMARK 465 ASP B 85
REMARK 465 ALA B 86
REMARK 465 LEU B 87
REMARK 465 LEU B 88
REMARK 465 ALA B 89
REMARK 465 GLY B 90
REMARK 465 ASP B 91
REMARK 465 ASP B 92
REMARK 465 GLY B 93
REMARK 465 SER B 94
REMARK 465 GLY B 95
REMARK 465 SER B 96
REMARK 465 GLU B 97
REMARK 465 SER B 98
REMARK 465 GLU B 99
REMARK 465 SER B 100
REMARK 465 GLU B 101
REMARK 465 PRO B 102
REMARK 465 GLU B 103
REMARK 465 SER B 104
REMARK 465 ASP B 105
REMARK 465 VAL B 106
REMARK 465 SER B 107
REMARK 465 ASN B 108
REMARK 465 GLY B 109
REMARK 465 GLU B 110
REMARK 465 GLU B 111
REMARK 465 GLY B 112
REMARK 465 ASN B 113
REMARK 465 GLU B 114
REMARK 465 ASN B 115
REMARK 465 GLY B 116
REMARK 465 GLN B 117
REMARK 465 THR B 118
REMARK 465 GLU B 119
REMARK 465 ILE B 120
REMARK 465 PRO B 121
REMARK 465 ASN B 122
REMARK 465 SER B 123
REMARK 465 ARG B 124
REMARK 465 MET B 125
REMARK 465 PHE B 126
REMARK 465 GLN B 127
REMARK 465 PHE B 128
REMARK 465 ASP B 129
REMARK 465 GLN B 130
REMARK 465 GLU B 131
REMARK 465 GLU B 132
REMARK 465 GLU B 133
REMARK 465 ASP B 134
REMARK 465 LEU B 135
REMARK 465 THR B 136
REMARK 465 GLY B 137
REMARK 465 ASP B 138
REMARK 465 VAL B 139
REMARK 465 ASP B 140
REMARK 465 SER B 141
REMARK 465 GLY B 142
REMARK 465 ASP B 143
REMARK 465 SER B 144
REMARK 465 GLU B 145
REMARK 465 ASP B 146
REMARK 465 SER B 147
REMARK 465 GLY B 148
REMARK 465 GLU B 149
REMARK 465 GLY B 150
REMARK 465 SER B 151
REMARK 465 GLU B 152
REMARK 465 GLU B 153
REMARK 465 GLU B 154
REMARK 465 GLU B 155
REMARK 465 GLU B 156
REMARK 465 ASN B 157
REMARK 465 VAL B 158
REMARK 465 GLU B 159
REMARK 465 LYS B 160
REMARK 465 GLU B 161
REMARK 465 GLU B 162
REMARK 465 GLU B 163
REMARK 465 HIS B 346
REMARK 465 GLY B 347
REMARK 465 SER B 348
REMARK 465 LYS B 349
REMARK 465 ARG B 350
REMARK 465 PRO B 351
REMARK 465 LEU B 352
REMARK 465 SER B 353
REMARK 465 GLN B 354
REMARK 465 PRO B 355
REMARK 465 THR B 356
REMARK 465 THR B 357
REMARK 465 SER B 358
REMARK 465 ILE B 359
REMARK 465 GLY B 360
REMARK 465 PHE B 361
REMARK 465 PRO B 362
REMARK 465 ALA B 363
REMARK 465 LEU B 364
REMARK 465 GLU B 365
REMARK 465 LYS B 366
REMARK 465 PRO B 367
REMARK 465 LEU B 368
REMARK 465 GLY B 369
REMARK 465 ASP B 370
REMARK 465 PHE B 371
REMARK 465 ASN B 372
REMARK 465 ASP B 373
REMARK 465 LEU B 374
REMARK 465 SER B 375
REMARK 465 GLN B 376
REMARK 465 LEU B 377
REMARK 465 VAL B 378
REMARK 465 LYS B 379
REMARK 465 LYS B 380
REMARK 465 LYS B 381
REMARK 465 PRO B 382
REMARK 465 ARG B 383
REMARK 465 ARG B 384
REMARK 465 HIS B 385
REMARK 465 LEU B 386
REMARK 465 GLU B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 HIS B 392
REMARK 465 HIS B 393
REMARK 465 MET C -11
REMARK 465 GLY C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
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 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 -11
REMARK 465 GLY D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 SER D 1
REMARK 465 ALA D 2
REMARK 465 LYS D 3
REMARK 465 ALA D 4
REMARK 465 GLU D 5
REMARK 465 LYS D 6
REMARK 465 LYS D 7
REMARK 465 PRO D 8
REMARK 465 ALA D 9
REMARK 465 SER D 10
REMARK 465 LYS D 11
REMARK 465 ALA D 12
REMARK 465 PRO D 13
REMARK 465 ALA D 14
REMARK 465 GLU D 15
REMARK 465 LYS D 16
REMARK 465 LYS D 17
REMARK 465 PRO D 18
REMARK 465 ALA D 19
REMARK 465 ALA D 20
REMARK 465 LYS D 21
REMARK 465 LYS D 22
REMARK 465 THR D 23
REMARK 465 SER D 24
REMARK 465 THR D 25
REMARK 465 SER D 26
REMARK 465 THR D 27
REMARK 465 ASP D 28
REMARK 465 GLY D 29
REMARK 465 LYS D 30
REMARK 465 LYS D 31
REMARK 465 ARG D 32
REMARK 465 SER D 33
REMARK 465 LYS D 34
REMARK 465 ALA D 35
REMARK 465 ARG D 36
REMARK 465 SER D 127
REMARK 465 THR D 128
REMARK 465 GLN D 129
REMARK 465 ALA D 130
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 ARG A 15 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 16 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 168 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 181 CG OD1 OD2
REMARK 470 GLU A 204 CG CD OE1 OE2
REMARK 470 ARG A 254 CZ NH1 NH2
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 GLN A 344 CG CD OE1 NE2
REMARK 470 GLN A 345 CG CD OE1 NE2
REMARK 470 HIS A 346 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 17 CG CD CE NZ
REMARK 470 VAL B 18 CG1 CG2
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 SER B 79 OG
REMARK 470 LYS B 270 CG CD CE NZ
REMARK 470 GLN B 274 CG CD OE1 NE2
REMARK 470 GLU B 324 CD OE1 OE2
REMARK 470 GLN B 345 CG CD OE1 NE2
REMARK 470 GLU C 65 CD OE1 OE2
REMARK 470 LYS C 75 CG CD CE NZ
REMARK 470 ARG C 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 88 CG CD CE NZ
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 A 17 90.70 -165.83
REMARK 500 LYS A 36 17.58 59.84
REMARK 500 ASN A 200 -137.61 59.46
REMARK 500 ASP A 322 40.81 -108.07
REMARK 500 ASN A 343 35.92 -77.81
REMARK 500 GLN A 345 -8.01 66.58
REMARK 500 ASN B 200 -128.02 50.07
REMARK 500 MET B 251 71.54 -100.09
REMARK 500 THR D 51 -63.07 -96.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NQ0 RELATED DB: PDB
REMARK 900 FREE HIF1 WITHOUT HISTONE BINDING
DBREF 5BT1 A 1 385 UNP Q12373 HIF1_YEAST 1 385
DBREF 5BT1 B 1 385 UNP Q12373 HIF1_YEAST 1 385
DBREF 5BT1 C 0 131 UNP P04911 H2A1_YEAST 1 132
DBREF 5BT1 D 0 130 UNP P02293 H2B1_YEAST 1 131
SEQADV 5BT1 LEU A 386 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 GLU A 387 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS A 388 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS A 389 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS A 390 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS A 391 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS A 392 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS A 393 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 LEU B 386 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 GLU B 387 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS B 388 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS B 389 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS B 390 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS B 391 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS B 392 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 HIS B 393 UNP Q12373 EXPRESSION TAG
SEQADV 5BT1 MET C -11 UNP P04911 INITIATING METHIONINE
SEQADV 5BT1 GLY C -10 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -9 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -8 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -7 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -6 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -5 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -4 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 GLY C -3 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 SER C -2 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 HIS C -1 UNP P04911 EXPRESSION TAG
SEQADV 5BT1 MET D -11 UNP P02293 INITIATING METHIONINE
SEQADV 5BT1 GLY D -10 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -9 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -8 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -7 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -6 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -5 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -4 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 GLY D -3 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 SER D -2 UNP P02293 EXPRESSION TAG
SEQADV 5BT1 HIS D -1 UNP P02293 EXPRESSION TAG
SEQRES 1 A 393 MET LYS LEU ARG ALA GLU ASP VAL LEU ALA ASN GLY THR
SEQRES 2 A 393 SER ARG HIS LYS VAL GLN ILE ASP MET GLU ARG GLN VAL
SEQRES 3 A 393 GLN ILE ALA LYS ASP LEU LEU ALA GLN LYS LYS PHE LEU
SEQRES 4 A 393 GLU ALA ALA LYS ARG CYS GLN GLN THR LEU ASP SER LEU
SEQRES 5 A 393 PRO LYS ASP GLY LEU LEU PRO ASP PRO GLU LEU PHE THR
SEQRES 6 A 393 ILE PHE ALA GLN ALA VAL TYR ASN MET GLU VAL GLN ASN
SEQRES 7 A 393 SER GLY ASN LEU PHE GLY ASP ALA LEU LEU ALA GLY ASP
SEQRES 8 A 393 ASP GLY SER GLY SER GLU SER GLU SER GLU PRO GLU SER
SEQRES 9 A 393 ASP VAL SER ASN GLY GLU GLU GLY ASN GLU ASN GLY GLN
SEQRES 10 A 393 THR GLU ILE PRO ASN SER ARG MET PHE GLN PHE ASP GLN
SEQRES 11 A 393 GLU GLU GLU ASP LEU THR GLY ASP VAL ASP SER GLY ASP
SEQRES 12 A 393 SER GLU ASP SER GLY GLU GLY SER GLU GLU GLU GLU GLU
SEQRES 13 A 393 ASN VAL GLU LYS GLU GLU GLU ARG LEU ALA LEU HIS GLU
SEQRES 14 A 393 LEU ALA ASN PHE SER PRO ALA ASN GLU HIS ASP ASP GLU
SEQRES 15 A 393 ILE GLU ASP VAL SER GLN LEU ARG LYS SER GLY PHE HIS
SEQRES 16 A 393 ILE TYR PHE GLU ASN ASP LEU TYR GLU ASN ALA LEU ASP
SEQRES 17 A 393 LEU LEU ALA GLN ALA LEU MET LEU LEU GLY ARG PRO THR
SEQRES 18 A 393 ALA ASP GLY GLN SER LEU THR GLU ASN SER ARG LEU ARG
SEQRES 19 A 393 ILE GLY ASP VAL TYR ILE LEU MET GLY ASP ILE GLU ARG
SEQRES 20 A 393 GLU ALA GLU MET PHE SER ARG ALA ILE HIS HIS TYR LEU
SEQRES 21 A 393 LYS ALA LEU GLY TYR TYR LYS THR LEU LYS PRO ALA GLU
SEQRES 22 A 393 GLN VAL THR GLU LYS VAL ILE GLN ALA GLU PHE LEU VAL
SEQRES 23 A 393 CYS ASP ALA LEU ARG TRP VAL ASP GLN VAL PRO ALA LYS
SEQRES 24 A 393 ASP LYS LEU LYS ARG PHE LYS HIS ALA LYS ALA LEU LEU
SEQRES 25 A 393 GLU LYS HIS MET THR THR ARG PRO LYS ASP SER GLU LEU
SEQRES 26 A 393 GLN GLN ALA ARG LEU ALA GLN ILE GLN ASP ASP ILE ASP
SEQRES 27 A 393 GLU VAL GLN GLU ASN GLN GLN HIS GLY SER LYS ARG PRO
SEQRES 28 A 393 LEU SER GLN PRO THR THR SER ILE GLY PHE PRO ALA LEU
SEQRES 29 A 393 GLU LYS PRO LEU GLY ASP PHE ASN ASP LEU SER GLN LEU
SEQRES 30 A 393 VAL LYS LYS LYS PRO ARG ARG HIS LEU GLU HIS HIS HIS
SEQRES 31 A 393 HIS HIS HIS
SEQRES 1 B 393 MET LYS LEU ARG ALA GLU ASP VAL LEU ALA ASN GLY THR
SEQRES 2 B 393 SER ARG HIS LYS VAL GLN ILE ASP MET GLU ARG GLN VAL
SEQRES 3 B 393 GLN ILE ALA LYS ASP LEU LEU ALA GLN LYS LYS PHE LEU
SEQRES 4 B 393 GLU ALA ALA LYS ARG CYS GLN GLN THR LEU ASP SER LEU
SEQRES 5 B 393 PRO LYS ASP GLY LEU LEU PRO ASP PRO GLU LEU PHE THR
SEQRES 6 B 393 ILE PHE ALA GLN ALA VAL TYR ASN MET GLU VAL GLN ASN
SEQRES 7 B 393 SER GLY ASN LEU PHE GLY ASP ALA LEU LEU ALA GLY ASP
SEQRES 8 B 393 ASP GLY SER GLY SER GLU SER GLU SER GLU PRO GLU SER
SEQRES 9 B 393 ASP VAL SER ASN GLY GLU GLU GLY ASN GLU ASN GLY GLN
SEQRES 10 B 393 THR GLU ILE PRO ASN SER ARG MET PHE GLN PHE ASP GLN
SEQRES 11 B 393 GLU GLU GLU ASP LEU THR GLY ASP VAL ASP SER GLY ASP
SEQRES 12 B 393 SER GLU ASP SER GLY GLU GLY SER GLU GLU GLU GLU GLU
SEQRES 13 B 393 ASN VAL GLU LYS GLU GLU GLU ARG LEU ALA LEU HIS GLU
SEQRES 14 B 393 LEU ALA ASN PHE SER PRO ALA ASN GLU HIS ASP ASP GLU
SEQRES 15 B 393 ILE GLU ASP VAL SER GLN LEU ARG LYS SER GLY PHE HIS
SEQRES 16 B 393 ILE TYR PHE GLU ASN ASP LEU TYR GLU ASN ALA LEU ASP
SEQRES 17 B 393 LEU LEU ALA GLN ALA LEU MET LEU LEU GLY ARG PRO THR
SEQRES 18 B 393 ALA ASP GLY GLN SER LEU THR GLU ASN SER ARG LEU ARG
SEQRES 19 B 393 ILE GLY ASP VAL TYR ILE LEU MET GLY ASP ILE GLU ARG
SEQRES 20 B 393 GLU ALA GLU MET PHE SER ARG ALA ILE HIS HIS TYR LEU
SEQRES 21 B 393 LYS ALA LEU GLY TYR TYR LYS THR LEU LYS PRO ALA GLU
SEQRES 22 B 393 GLN VAL THR GLU LYS VAL ILE GLN ALA GLU PHE LEU VAL
SEQRES 23 B 393 CYS ASP ALA LEU ARG TRP VAL ASP GLN VAL PRO ALA LYS
SEQRES 24 B 393 ASP LYS LEU LYS ARG PHE LYS HIS ALA LYS ALA LEU LEU
SEQRES 25 B 393 GLU LYS HIS MET THR THR ARG PRO LYS ASP SER GLU LEU
SEQRES 26 B 393 GLN GLN ALA ARG LEU ALA GLN ILE GLN ASP ASP ILE ASP
SEQRES 27 B 393 GLU VAL GLN GLU ASN GLN GLN HIS GLY SER LYS ARG PRO
SEQRES 28 B 393 LEU SER GLN PRO THR THR SER ILE GLY PHE PRO ALA LEU
SEQRES 29 B 393 GLU LYS PRO LEU GLY ASP PHE ASN ASP LEU SER GLN LEU
SEQRES 30 B 393 VAL LYS LYS LYS PRO ARG ARG HIS LEU GLU HIS HIS HIS
SEQRES 31 B 393 HIS HIS HIS
SEQRES 1 C 143 MET GLY HIS HIS HIS HIS HIS HIS GLY SER HIS MET SER
SEQRES 2 C 143 GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA LYS ALA
SEQRES 3 C 143 SER GLN SER ARG SER ALA LYS ALA GLY LEU THR PHE PRO
SEQRES 4 C 143 VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY ASN TYR
SEQRES 5 C 143 ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR LEU THR
SEQRES 6 C 143 ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU GLU LEU
SEQRES 7 C 143 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 8 C 143 ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP ASP
SEQRES 9 C 143 GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE ALA GLN
SEQRES 10 C 143 GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU LEU PRO
SEQRES 11 C 143 LYS LYS SER ALA LYS ALA THR LYS ALA SER GLN GLU LEU
SEQRES 1 D 142 MET GLY HIS HIS HIS HIS HIS HIS GLY SER HIS MET SER
SEQRES 2 D 142 ALA LYS ALA GLU LYS LYS PRO ALA SER LYS ALA PRO ALA
SEQRES 3 D 142 GLU LYS LYS PRO ALA ALA LYS LYS THR SER THR SER THR
SEQRES 4 D 142 ASP GLY LYS LYS ARG SER LYS ALA ARG LYS GLU THR TYR
SEQRES 5 D 142 SER SER TYR ILE TYR LYS VAL LEU LYS GLN THR HIS PRO
SEQRES 6 D 142 ASP THR GLY ILE SER GLN LYS SER MET SER ILE LEU ASN
SEQRES 7 D 142 SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA THR GLU
SEQRES 8 D 142 ALA SER LYS LEU ALA ALA TYR ASN LYS LYS SER THR ILE
SEQRES 9 D 142 SER ALA ARG GLU ILE GLN THR ALA VAL ARG LEU ILE LEU
SEQRES 10 D 142 PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR
SEQRES 11 D 142 ARG ALA VAL THR LYS TYR SER SER SER THR GLN ALA
FORMUL 5 HOH *47(H2 O)
HELIX 1 AA1 ASP A 21 GLN A 35 1 15
HELIX 2 AA2 LYS A 37 LEU A 52 1 16
HELIX 3 AA3 PRO A 61 ASN A 78 1 18
HELIX 4 AA4 ASP A 185 LEU A 189 5 5
HELIX 5 AA5 GLY A 193 GLU A 199 5 7
HELIX 6 AA6 ASP A 201 GLY A 218 1 18
HELIX 7 AA7 THR A 228 GLU A 250 1 23
HELIX 8 AA8 MET A 251 LYS A 267 1 17
HELIX 9 AA9 ALA A 272 ARG A 291 1 20
HELIX 10 AB1 PRO A 297 THR A 317 1 21
HELIX 11 AB2 ASP A 322 ASN A 343 1 22
HELIX 12 AB3 ASP B 21 GLN B 35 1 15
HELIX 13 AB4 LYS B 37 LEU B 52 1 16
HELIX 14 AB5 PRO B 61 GLY B 80 1 20
HELIX 15 AB6 ALA B 166 ASN B 172 1 7
HELIX 16 AB7 ASP B 185 LEU B 189 5 5
HELIX 17 AB8 GLY B 193 GLU B 199 5 7
HELIX 18 AB9 ASP B 201 GLY B 218 1 18
HELIX 19 AC1 THR B 228 ALA B 249 1 22
HELIX 20 AC2 MET B 251 LYS B 267 1 17
HELIX 21 AC3 ALA B 272 LEU B 290 1 19
HELIX 22 AC4 ARG B 291 VAL B 293 5 3
HELIX 23 AC5 PRO B 297 THR B 317 1 21
HELIX 24 AC6 ASP B 322 ASN B 343 1 22
HELIX 25 AC7 SER C 17 GLY C 23 1 7
HELIX 26 AC8 PRO C 27 ARG C 37 1 11
HELIX 27 AC9 SER C 46 ASN C 74 1 29
HELIX 28 AD1 ILE C 80 ASN C 90 1 11
HELIX 29 AD2 ASP C 91 GLY C 99 1 9
HELIX 30 AD3 TYR D 40 HIS D 52 1 13
HELIX 31 AD4 SER D 58 ASN D 87 1 30
HELIX 32 AD5 SER D 93 LEU D 105 1 13
HELIX 33 AD6 PRO D 106 SER D 126 1 21
SHEET 1 AA1 2 ARG C 43 ILE C 44 0
SHEET 2 AA1 2 THR D 91 ILE D 92 1 O ILE D 92 N ARG C 43
SHEET 1 AA2 2 ARG C 78 ILE C 79 0
SHEET 2 AA2 2 GLY D 56 ILE D 57 1 O GLY D 56 N ILE C 79
CRYST1 102.673 48.363 160.706 90.00 107.05 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009740 0.000000 0.002986 0.00000
SCALE2 0.000000 0.020677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006508 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
