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Original site: 4YKW
Chemical substance (1) PDB-CCD (1) Gene (1) KEGG GENES (1) Protein sequence (4) UniProt (1) SWISS-PROT (1) PDBSTR (2) DNA sequence (1) EMBL (1) Protein domain (6) InterPro (5) PROSITE (1) All databases (13)
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HEADER CHAPERONE/INHIBITOR 04-MAR-15 4YKW
TITLE HEAT SHOCK PROTEIN 90 BOUND TO CS312
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 2-236;
COMPND 5 SYNONYM: HEAT SHOCK 86 KDA,HSP86,LIPOPOLYSACCHARIDE-ASSOCIATED
COMPND 6 PROTEIN 2,LPS-ASSOCIATED PROTEIN 2,RENAL CARCINOMA ANTIGEN NY-REN-38;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2
KEYWDS CHAPERONE, PROTEIN-INHIBITOR COMPLEX, HSP 90, CHAPERONE-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.N.KANG,J.A.STUCKEY
REVDAT 3 28-FEB-24 4YKW 1 REMARK
REVDAT 2 13-APR-16 4YKW 1 REMARK
REVDAT 1 09-MAR-16 4YKW 0
JRNL AUTH Y.N.KANG,J.A.STUCKEY
JRNL TITL STRUCTURE OF HEAT SHOCK PROTEIN 90 BOUND TO CS312
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 36735
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1834
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.73
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2891
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2134
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2751
REMARK 3 BIN R VALUE (WORKING SET) : 0.2139
REMARK 3 BIN FREE R VALUE : 0.2044
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.84
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19410
REMARK 3 B22 (A**2) : 0.04650
REMARK 3 B33 (A**2) : 0.14760
REMARK 3 B12 (A**2) : 0.17200
REMARK 3 B13 (A**2) : 1.27570
REMARK 3 B23 (A**2) : 0.30140
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.254
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.144
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.131
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.147
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.134
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3475 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4717 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1651 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 95 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 551 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3475 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 479 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4153 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.75
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.83
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|11 - 40}
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2982 1.9897 -4.7523
REMARK 3 T TENSOR
REMARK 3 T11: -0.0157 T22: -0.0418
REMARK 3 T33: 0.0325 T12: 0.0089
REMARK 3 T13: -0.0597 T23: -0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 0.9342 L22: 0.6634
REMARK 3 L33: 0.3111 L12: 0.7357
REMARK 3 L13: 0.1412 L23: -0.5971
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: -0.0176 S13: 0.0355
REMARK 3 S21: 0.0053 S22: -0.0074 S23: -0.0004
REMARK 3 S31: -0.0260 S32: 0.0087 S33: 0.0092
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|41 - 87}
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3038 -18.3696 -3.0648
REMARK 3 T TENSOR
REMARK 3 T11: -0.0657 T22: 0.0477
REMARK 3 T33: -0.0203 T12: -0.0050
REMARK 3 T13: -0.0005 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.3125 L22: 0.8211
REMARK 3 L33: 0.5978 L12: -0.3712
REMARK 3 L13: 0.0926 L23: -0.0283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: -0.0478 S13: -0.0090
REMARK 3 S21: 0.0050 S22: 0.0157 S23: -0.0241
REMARK 3 S31: -0.0338 S32: -0.0733 S33: 0.0075
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|88 - 111}
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8475 -7.3544 -2.9678
REMARK 3 T TENSOR
REMARK 3 T11: -0.0295 T22: 0.0243
REMARK 3 T33: 0.0148 T12: 0.0289
REMARK 3 T13: 0.0075 T23: -0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.2468 L22: 0.4969
REMARK 3 L33: -0.1537 L12: -0.0092
REMARK 3 L13: -0.3534 L23: 0.1506
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: -0.0233 S13: 0.0113
REMARK 3 S21: 0.0035 S22: -0.0057 S23: 0.0040
REMARK 3 S31: -0.0371 S32: -0.0205 S33: 0.0147
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|112 - 127}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2587 -3.3063 9.9965
REMARK 3 T TENSOR
REMARK 3 T11: -0.0137 T22: 0.0399
REMARK 3 T33: -0.0247 T12: -0.0245
REMARK 3 T13: -0.0217 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.0635 L22: -0.0366
REMARK 3 L33: 0.1358 L12: 0.0566
REMARK 3 L13: 0.0435 L23: 0.0282
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: -0.0021 S13: 0.0009
REMARK 3 S21: 0.0021 S22: -0.0047 S23: -0.0011
REMARK 3 S31: -0.0020 S32: 0.0008 S33: 0.0039
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|128 - 169}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0893 -6.0961 -3.7060
REMARK 3 T TENSOR
REMARK 3 T11: -0.0295 T22: 0.0040
REMARK 3 T33: 0.0110 T12: -0.0011
REMARK 3 T13: -0.0352 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.0335 L22: 0.7693
REMARK 3 L33: 0.4970 L12: -0.3727
REMARK 3 L13: 0.0205 L23: 0.0306
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.0176 S13: 0.0213
REMARK 3 S21: 0.0235 S22: -0.0005 S23: 0.0080
REMARK 3 S31: -0.0622 S32: -0.0188 S33: 0.0010
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|170 - 223}
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8333 -15.4676 -8.5069
REMARK 3 T TENSOR
REMARK 3 T11: -0.0576 T22: -0.0150
REMARK 3 T33: 0.0244 T12: -0.0055
REMARK 3 T13: 0.0116 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 1.4082 L22: 0.5809
REMARK 3 L33: 0.6816 L12: -0.1447
REMARK 3 L13: 0.3149 L23: 0.2395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0380 S12: -0.0252 S13: -0.0278
REMARK 3 S21: -0.0900 S22: -0.0186 S23: -0.0581
REMARK 3 S31: -0.0346 S32: -0.0084 S33: 0.0566
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {B|11 - 36}
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1059 -26.4737 26.7506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0187 T22: -0.0366
REMARK 3 T33: 0.0112 T12: -0.0326
REMARK 3 T13: -0.0018 T23: -0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 0.6488 L22: 0.8907
REMARK 3 L33: -0.1427 L12: 0.6932
REMARK 3 L13: -0.3780 L23: 0.0540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: 0.0128 S13: -0.0017
REMARK 3 S21: -0.0467 S22: 0.0240 S23: 0.0082
REMARK 3 S31: 0.0062 S32: -0.0046 S33: -0.0051
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {B|37 - 56}
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0872 -17.3715 22.8363
REMARK 3 T TENSOR
REMARK 3 T11: 0.0529 T22: 0.0013
REMARK 3 T33: -0.0508 T12: -0.0349
REMARK 3 T13: 0.0582 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: -0.1443 L22: 0.1746
REMARK 3 L33: 0.0679 L12: -0.2139
REMARK 3 L13: 0.0947 L23: -0.0377
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: 0.0129 S13: -0.0180
REMARK 3 S21: -0.0180 S22: 0.0095 S23: -0.0117
REMARK 3 S31: -0.0134 S32: 0.0191 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {B|57 - 90}
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7706 -3.6596 27.0759
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: -0.0377
REMARK 3 T33: 0.0024 T12: 0.0067
REMARK 3 T13: -0.0005 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.5169 L22: 0.3257
REMARK 3 L33: -0.0308 L12: 0.5254
REMARK 3 L13: -0.3347 L23: -0.0083
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.0052 S13: 0.0278
REMARK 3 S21: -0.0207 S22: -0.0031 S23: 0.0400
REMARK 3 S31: 0.0008 S32: -0.0052 S33: 0.0167
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {B|91 - 127}
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8814 -19.2212 17.7921
REMARK 3 T TENSOR
REMARK 3 T11: 0.0154 T22: 0.0170
REMARK 3 T33: 0.0009 T12: -0.0292
REMARK 3 T13: -0.0475 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: -0.0931 L22: 0.0158
REMARK 3 L33: 0.0772 L12: -0.0632
REMARK 3 L13: 0.3005 L23: -0.1437
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0428 S13: 0.0044
REMARK 3 S21: -0.0282 S22: -0.0003 S23: -0.0022
REMARK 3 S31: 0.0152 S32: 0.0012 S33: 0.0027
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {B|128 - 207}
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3798 -17.3131 29.5652
REMARK 3 T TENSOR
REMARK 3 T11: -0.0287 T22: -0.0585
REMARK 3 T33: -0.0039 T12: 0.0026
REMARK 3 T13: 0.0005 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.9420 L22: 1.7062
REMARK 3 L33: 0.2463 L12: 1.8107
REMARK 3 L13: -0.2989 L23: 0.2145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0536 S12: 0.0278 S13: 0.0173
REMARK 3 S21: -0.1644 S22: 0.0165 S23: -0.0065
REMARK 3 S31: 0.0620 S32: -0.0188 S33: 0.0371
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {B|208 - 223}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3017 -6.7350 27.9210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0094 T22: 0.0026
REMARK 3 T33: -0.0097 T12: 0.0044
REMARK 3 T13: 0.0104 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.2469 L22: 0.0321
REMARK 3 L33: 0.0228 L12: 0.1143
REMARK 3 L13: 0.0316 L23: -0.0486
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0045 S13: -0.0008
REMARK 3 S21: -0.0041 S22: 0.0057 S23: -0.0082
REMARK 3 S31: -0.0005 S32: 0.0066 S33: -0.0036
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207624.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36735
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.49500
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: NULL
REMARK 200 STARTING MODEL: IN-HOUSE APO STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 1000, 0.1 M TRIS PH 7.0, CRYO
REMARK 280 CONDITIONS: 35% PEG 4000, 10% GLYCEROL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -1
REMARK 465 ASN A 0
REMARK 465 ALA A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 THR A 5
REMARK 465 GLN A 6
REMARK 465 THR A 7
REMARK 465 GLN A 8
REMARK 465 ASP A 9
REMARK 465 GLN A 10
REMARK 465 LYS A 224
REMARK 465 GLU A 225
REMARK 465 ARG A 226
REMARK 465 ASP A 227
REMARK 465 LYS A 228
REMARK 465 GLU A 229
REMARK 465 VAL A 230
REMARK 465 SER A 231
REMARK 465 ASP A 232
REMARK 465 ASP A 233
REMARK 465 GLU A 234
REMARK 465 ALA A 235
REMARK 465 GLU A 236
REMARK 465 SER B -1
REMARK 465 ASN B 0
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 THR B 5
REMARK 465 GLN B 6
REMARK 465 THR B 7
REMARK 465 GLN B 8
REMARK 465 ASP B 9
REMARK 465 GLN B 10
REMARK 465 LYS B 224
REMARK 465 GLU B 225
REMARK 465 ARG B 226
REMARK 465 ASP B 227
REMARK 465 LYS B 228
REMARK 465 GLU B 229
REMARK 465 VAL B 230
REMARK 465 SER B 231
REMARK 465 ASP B 232
REMARK 465 ASP B 233
REMARK 465 GLU B 234
REMARK 465 ALA B 235
REMARK 465 GLU B 236
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 PHE A 37 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 130 CG SD CE
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 GLU B 25 CG CD OE1 OE2
REMARK 470 PHE B 118 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 119 CG SD CE
REMARK 470 ILE B 131 CG1 CG2 CD1
REMARK 470 GLN B 133 CG CD OE1 NE2
REMARK 470 PHE B 134 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 212 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ILE B 131 C - N - CA ANGL. DEV. = 18.5 DEGREES
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 TYR A 38 115.95 -19.58
REMARK 500 MET A 130 6.30 -69.48
REMARK 500 ALA A 166 -135.57 65.41
REMARK 500 ARG A 182 142.87 -172.16
REMARK 500 PHE A 213 51.90 -112.36
REMARK 500 LEU B 107 51.46 -116.73
REMARK 500 ILE B 131 44.77 117.71
REMARK 500 VAL B 136 -35.88 -39.90
REMARK 500 ALA B 166 -134.90 72.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ES A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4ES B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YKQ RELATED DB: PDB
REMARK 900 RELATED ID: 4YKR RELATED DB: PDB
REMARK 900 RELATED ID: 4YKT RELATED DB: PDB
REMARK 900 RELATED ID: 4YKU RELATED DB: PDB
REMARK 900 RELATED ID: 4YKX RELATED DB: PDB
REMARK 900 RELATED ID: 4YKY RELATED DB: PDB
REMARK 900 RELATED ID: 4YKZ RELATED DB: PDB
DBREF 4YKW A 2 236 UNP P07900 HS90A_HUMAN 2 236
DBREF 4YKW B 2 236 UNP P07900 HS90A_HUMAN 2 236
SEQADV 4YKW SER A -1 UNP P07900 EXPRESSION TAG
SEQADV 4YKW ASN A 0 UNP P07900 EXPRESSION TAG
SEQADV 4YKW ALA A 1 UNP P07900 EXPRESSION TAG
SEQADV 4YKW SER B -1 UNP P07900 EXPRESSION TAG
SEQADV 4YKW ASN B 0 UNP P07900 EXPRESSION TAG
SEQADV 4YKW ALA B 1 UNP P07900 EXPRESSION TAG
SEQRES 1 A 238 SER ASN ALA PRO GLU GLU THR GLN THR GLN ASP GLN PRO
SEQRES 2 A 238 MET GLU GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA
SEQRES 3 A 238 GLU ILE ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE
SEQRES 4 A 238 TYR SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER
SEQRES 5 A 238 ASN SER SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER
SEQRES 6 A 238 LEU THR ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU
SEQRES 7 A 238 HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU
SEQRES 8 A 238 THR ILE VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP
SEQRES 9 A 238 LEU ILE ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR
SEQRES 10 A 238 LYS ALA PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE
SEQRES 11 A 238 SER MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA
SEQRES 12 A 238 TYR LEU VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS
SEQRES 13 A 238 ASN ASP ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY
SEQRES 14 A 238 GLY SER PHE THR VAL ARG THR ASP THR GLY GLU PRO MET
SEQRES 15 A 238 GLY ARG GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP
SEQRES 16 A 238 GLN THR GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE
SEQRES 17 A 238 VAL LYS LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR
SEQRES 18 A 238 LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP
SEQRES 19 A 238 ASP GLU ALA GLU
SEQRES 1 B 238 SER ASN ALA PRO GLU GLU THR GLN THR GLN ASP GLN PRO
SEQRES 2 B 238 MET GLU GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA
SEQRES 3 B 238 GLU ILE ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE
SEQRES 4 B 238 TYR SER ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER
SEQRES 5 B 238 ASN SER SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER
SEQRES 6 B 238 LEU THR ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU
SEQRES 7 B 238 HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU
SEQRES 8 B 238 THR ILE VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP
SEQRES 9 B 238 LEU ILE ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR
SEQRES 10 B 238 LYS ALA PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE
SEQRES 11 B 238 SER MET ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA
SEQRES 12 B 238 TYR LEU VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS
SEQRES 13 B 238 ASN ASP ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY
SEQRES 14 B 238 GLY SER PHE THR VAL ARG THR ASP THR GLY GLU PRO MET
SEQRES 15 B 238 GLY ARG GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP
SEQRES 16 B 238 GLN THR GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE
SEQRES 17 B 238 VAL LYS LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR
SEQRES 18 B 238 LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP
SEQRES 19 B 238 ASP GLU ALA GLU
HET 4ES A 301 27
HET 4ES B 301 27
HETNAM 4ES 4-(2-CHLORO-4-NITROPHENYL)-6-METHYLPYRIMIDIN-2-AMINE
FORMUL 3 4ES 2(C11 H9 CL N4 O2)
FORMUL 5 HOH *215(H2 O)
HELIX 1 AA1 GLN A 23 THR A 36 1 14
HELIX 2 AA2 ASN A 40 GLU A 42 5 3
HELIX 3 AA3 ILE A 43 ASP A 66 1 24
HELIX 4 AA4 PRO A 67 ASP A 71 5 5
HELIX 5 AA5 THR A 99 LEU A 107 1 9
HELIX 6 AA6 GLY A 114 GLY A 125 1 12
HELIX 7 AA7 ASP A 127 GLY A 132 5 6
HELIX 8 AA8 PHE A 134 LEU A 143 5 10
HELIX 9 AA9 GLU A 192 LEU A 198 5 7
HELIX 10 AB1 GLU A 199 SER A 211 1 13
HELIX 11 AB2 GLN B 23 THR B 36 1 14
HELIX 12 AB3 GLU B 42 LEU B 64 1 23
HELIX 13 AB4 ASP B 66 ASP B 71 5 6
HELIX 14 AB5 THR B 99 LEU B 107 1 9
HELIX 15 AB6 GLY B 114 GLN B 123 1 10
HELIX 16 AB7 PHE B 134 LEU B 143 5 10
HELIX 17 AB8 GLU B 192 LEU B 198 5 7
HELIX 18 AB9 GLU B 199 SER B 211 1 13
SHEET 1 AA1 8 GLU A 18 ALA A 21 0
SHEET 2 AA1 8 SER A 169 THR A 174 -1 O PHE A 170 N PHE A 20
SHEET 3 AA1 8 GLN A 159 SER A 164 -1 N ALA A 161 O ARG A 173
SHEET 4 AA1 8 ALA A 145 LYS A 153 -1 N VAL A 150 O TRP A 162
SHEET 5 AA1 8 GLY A 183 LEU A 190 -1 O ILE A 187 N THR A 149
SHEET 6 AA1 8 THR A 88 ASP A 93 -1 N LEU A 89 O LEU A 188
SHEET 7 AA1 8 ILE A 78 ASN A 83 -1 N ASN A 79 O VAL A 92
SHEET 8 AA1 8 ILE A 218 LEU A 220 1 O THR A 219 N LEU A 80
SHEET 1 AA2 8 GLU B 18 ALA B 21 0
SHEET 2 AA2 8 SER B 169 THR B 174 -1 O PHE B 170 N PHE B 20
SHEET 3 AA2 8 GLN B 159 SER B 164 -1 N ALA B 161 O ARG B 173
SHEET 4 AA2 8 ALA B 145 LYS B 153 -1 N VAL B 150 O TRP B 162
SHEET 5 AA2 8 GLY B 183 LEU B 190 -1 O ILE B 187 N THR B 149
SHEET 6 AA2 8 THR B 88 ASP B 93 -1 N LEU B 89 O LEU B 188
SHEET 7 AA2 8 ILE B 78 ASN B 83 -1 N ILE B 81 O THR B 90
SHEET 8 AA2 8 ILE B 218 LEU B 220 1 O THR B 219 N LEU B 80
SITE 1 AC1 13 ALA A 55 ASP A 93 GLY A 97 MET A 98
SITE 2 AC1 13 ASN A 106 LEU A 107 GLY A 135 VAL A 136
SITE 3 AC1 13 PHE A 138 TYR A 139 THR A 184 HOH A 445
SITE 4 AC1 13 HOH A 478
SITE 1 AC2 13 ALA B 55 ASP B 93 GLY B 97 MET B 98
SITE 2 AC2 13 ASN B 106 LEU B 107 GLY B 135 VAL B 136
SITE 3 AC2 13 PHE B 138 TYR B 139 THR B 184 HOH B 414
SITE 4 AC2 13 HOH B 454
CRYST1 43.928 51.853 56.703 68.43 86.65 71.50 P 1 2
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 0.022765 -0.007617 0.001588 0.00000
SCALE2 0.000000 0.020336 -0.008067 0.00000
SCALE3 0.000000 0.000000 0.019005 0.00000
(ATOM LINES ARE NOT SHOWN.)
END