HEADER TRANSCRIPTION 31-MAR-11 3RCW
TITLE CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BRD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: BR140-LIKE PROTEIN, BROMODOMAIN AND PHD FINGER-CONTAINING
COMPND 5 PROTEIN 2;
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 GENE: BRD1, BRL, BRPF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TRANSCRIPTION, BROMODOMAIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,T.KEATES,S.PICAUD,I.FELLETAR,A.C.W.PIKE,T.KROJER,
AUTHOR 2 F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 13-SEP-23 3RCW 1 REMARK SEQADV
REVDAT 3 31-JAN-18 3RCW 1 AUTHOR
REVDAT 2 11-APR-12 3RCW 1 JRNL VERSN
REVDAT 1 01-JUN-11 3RCW 0
JRNL AUTH P.FILIPPAKOPOULOS,S.PICAUD,M.MANGOS,T.KEATES,J.P.LAMBERT,
JRNL AUTH 2 D.BARSYTE-LOVEJOY,I.FELLETAR,R.VOLKMER,S.MULLER,T.PAWSON,
JRNL AUTH 3 A.C.GINGRAS,C.H.ARROWSMITH,S.KNAPP
JRNL TITL HISTONE RECOGNITION AND LARGE-SCALE STRUCTURAL ANALYSIS OF
JRNL TITL 2 THE HUMAN BROMODOMAIN FAMILY.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 149 214 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22464331
JRNL DOI 10.1016/J.CELL.2012.02.013
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 53137
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3765
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.23000
REMARK 3 B22 (A**2) : -1.75000
REMARK 3 B33 (A**2) : -2.03000
REMARK 3 B12 (A**2) : -0.70000
REMARK 3 B13 (A**2) : 0.95000
REMARK 3 B23 (A**2) : -1.30000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.215
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7388 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5050 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9994 ; 1.430 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12247 ; 0.902 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 905 ; 5.424 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 379 ;34.915 ;23.826
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1281 ;16.296 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;18.004 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1123 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8248 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1515 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4550 ; 4.442 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1804 ; 1.463 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7314 ; 6.238 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2838 ;10.258 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2677 ;12.608 ;11.000
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 : 8
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 562 A 678
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4429 10.4061 86.1506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0690 T22: 0.0740
REMARK 3 T33: 0.0807 T12: 0.0028
REMARK 3 T13: 0.0253 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 1.3281 L22: 1.5330
REMARK 3 L33: 0.4112 L12: 0.8993
REMARK 3 L13: -0.7813 L23: -0.5508
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: 0.1336 S13: -0.1737
REMARK 3 S21: -0.0942 S22: -0.0157 S23: -0.1373
REMARK 3 S31: -0.0351 S32: -0.0789 S33: 0.0327
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 563 B 680
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3383 -11.6656 78.3165
REMARK 3 T TENSOR
REMARK 3 T11: 0.1026 T22: 0.0683
REMARK 3 T33: 0.0782 T12: 0.0010
REMARK 3 T13: 0.0364 T23: -0.0293
REMARK 3 L TENSOR
REMARK 3 L11: -0.2054 L22: 1.8453
REMARK 3 L33: 1.5508 L12: 0.0649
REMARK 3 L13: 0.0648 L23: -1.0393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.0195 S13: -0.0255
REMARK 3 S21: 0.1589 S22: -0.0199 S23: 0.0841
REMARK 3 S31: -0.1729 S32: -0.0309 S33: 0.0027
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 565 C 675
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5877 -13.2509 129.6753
REMARK 3 T TENSOR
REMARK 3 T11: 0.0829 T22: 0.1304
REMARK 3 T33: 0.0296 T12: 0.0735
REMARK 3 T13: -0.0302 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.6922 L22: 1.5997
REMARK 3 L33: 0.7374 L12: 0.7938
REMARK 3 L13: -0.4804 L23: 0.2357
REMARK 3 S TENSOR
REMARK 3 S11: -0.0567 S12: 0.0792 S13: -0.0534
REMARK 3 S21: 0.0239 S22: -0.0601 S23: -0.0439
REMARK 3 S31: -0.0619 S32: -0.1371 S33: 0.1168
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 564 D 675
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1693 19.3142 60.0304
REMARK 3 T TENSOR
REMARK 3 T11: 0.0533 T22: 0.1046
REMARK 3 T33: 0.0784 T12: 0.0031
REMARK 3 T13: 0.0264 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: -0.0767 L22: 1.2265
REMARK 3 L33: 1.9121 L12: -0.0990
REMARK 3 L13: 0.0873 L23: 0.7902
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: -0.0009 S13: 0.0395
REMARK 3 S21: -0.1328 S22: 0.0150 S23: -0.0455
REMARK 3 S31: 0.0213 S32: 0.1051 S33: -0.0419
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 : E 563 E 678
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6925 5.3656 25.9458
REMARK 3 T TENSOR
REMARK 3 T11: 0.1900 T22: 0.1146
REMARK 3 T33: 0.0234 T12: -0.0386
REMARK 3 T13: 0.0305 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: -0.4170 L22: 1.0958
REMARK 3 L33: 1.3929 L12: -0.2970
REMARK 3 L13: 0.2919 L23: 0.4309
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: 0.1842 S13: 0.2539
REMARK 3 S21: 0.2126 S22: -0.2028 S23: -0.0626
REMARK 3 S31: 0.5263 S32: -0.0916 S33: 0.2030
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 : F 564 F 676
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2786 -17.1702 18.6729
REMARK 3 T TENSOR
REMARK 3 T11: 0.0652 T22: 0.0575
REMARK 3 T33: 0.0990 T12: -0.0167
REMARK 3 T13: -0.0350 T23: 0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 1.2727 L22: 2.8560
REMARK 3 L33: 0.7044 L12: -1.9629
REMARK 3 L13: 0.7306 L23: -0.5348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: 0.1010 S13: 0.1838
REMARK 3 S21: 0.2165 S22: -0.0963 S23: -0.1411
REMARK 3 S31: -0.0238 S32: 0.0338 S33: 0.1545
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 : G 564 G 675
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4011 -20.6135 105.4405
REMARK 3 T TENSOR
REMARK 3 T11: 0.0767 T22: 0.0740
REMARK 3 T33: 0.0836 T12: -0.0281
REMARK 3 T13: 0.0239 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.2715 L22: 1.0872
REMARK 3 L33: 0.5149 L12: -0.8037
REMARK 3 L13: -0.0170 L23: 0.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: -0.0760 S13: 0.0961
REMARK 3 S21: 0.0466 S22: 0.0678 S23: 0.0237
REMARK 3 S31: 0.0899 S32: -0.0342 S33: -0.0345
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 : H 566 H 673
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9064 -23.9733 43.8433
REMARK 3 T TENSOR
REMARK 3 T11: 0.0868 T22: 0.0969
REMARK 3 T33: 0.0068 T12: 0.0092
REMARK 3 T13: -0.0182 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: -0.2742 L22: 2.8942
REMARK 3 L33: 7.6839 L12: 0.7194
REMARK 3 L13: 1.2718 L23: 2.7277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: -0.0185 S13: -0.1305
REMARK 3 S21: -0.2069 S22: 0.3571 S23: -0.1311
REMARK 3 S31: -0.5879 S32: 0.0049 S33: -0.3736
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 3RCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064775.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
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) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53142
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 19.892
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : 0.41800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: ENSEMBLE OF 3HME, 2MB3, 2OSS, 2OIO, 2GRC, 2OO1,
REMARK 200 3DAI, 3D7C, 3DWY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32.5% PEG3350, 5% ETGLY, 0.1M ACETATE,
REMARK 280 PH 4.8, VAPOR DIFFUSION, SITTING 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, 3, 4, 5, 6, 7, 8
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 554
REMARK 465 MET A 555
REMARK 465 GLU A 556
REMARK 465 GLN A 557
REMARK 465 VAL A 558
REMARK 465 ALA A 559
REMARK 465 MET A 560
REMARK 465 GLU A 561
REMARK 465 SER A 679
REMARK 465 GLY A 680
REMARK 465 MET A 681
REMARK 465 HIS A 682
REMARK 465 LEU A 683
REMARK 465 PRO A 684
REMARK 465 GLU A 685
REMARK 465 ARG A 686
REMARK 465 PRO A 687
REMARK 465 ALA A 688
REMARK 465 SER B 554
REMARK 465 MET B 555
REMARK 465 GLU B 556
REMARK 465 GLN B 557
REMARK 465 VAL B 558
REMARK 465 ALA B 559
REMARK 465 MET B 560
REMARK 465 GLU B 561
REMARK 465 LEU B 562
REMARK 465 MET B 681
REMARK 465 HIS B 682
REMARK 465 LEU B 683
REMARK 465 PRO B 684
REMARK 465 GLU B 685
REMARK 465 ARG B 686
REMARK 465 PRO B 687
REMARK 465 ALA B 688
REMARK 465 SER C 554
REMARK 465 MET C 555
REMARK 465 GLU C 556
REMARK 465 GLN C 557
REMARK 465 VAL C 558
REMARK 465 ALA C 559
REMARK 465 MET C 560
REMARK 465 GLU C 561
REMARK 465 LEU C 562
REMARK 465 ARG C 563
REMARK 465 LEU C 564
REMARK 465 GLU C 676
REMARK 465 GLU C 677
REMARK 465 ALA C 678
REMARK 465 SER C 679
REMARK 465 GLY C 680
REMARK 465 MET C 681
REMARK 465 HIS C 682
REMARK 465 LEU C 683
REMARK 465 PRO C 684
REMARK 465 GLU C 685
REMARK 465 ARG C 686
REMARK 465 PRO C 687
REMARK 465 ALA C 688
REMARK 465 SER D 554
REMARK 465 MET D 555
REMARK 465 GLU D 556
REMARK 465 GLN D 557
REMARK 465 VAL D 558
REMARK 465 ALA D 559
REMARK 465 MET D 560
REMARK 465 GLU D 561
REMARK 465 LEU D 562
REMARK 465 ARG D 563
REMARK 465 GLU D 676
REMARK 465 GLU D 677
REMARK 465 ALA D 678
REMARK 465 SER D 679
REMARK 465 GLY D 680
REMARK 465 MET D 681
REMARK 465 HIS D 682
REMARK 465 LEU D 683
REMARK 465 PRO D 684
REMARK 465 GLU D 685
REMARK 465 ARG D 686
REMARK 465 PRO D 687
REMARK 465 ALA D 688
REMARK 465 SER E 554
REMARK 465 MET E 555
REMARK 465 GLU E 556
REMARK 465 GLN E 557
REMARK 465 VAL E 558
REMARK 465 ALA E 559
REMARK 465 MET E 560
REMARK 465 GLU E 561
REMARK 465 LEU E 562
REMARK 465 SER E 679
REMARK 465 GLY E 680
REMARK 465 MET E 681
REMARK 465 HIS E 682
REMARK 465 LEU E 683
REMARK 465 PRO E 684
REMARK 465 GLU E 685
REMARK 465 ARG E 686
REMARK 465 PRO E 687
REMARK 465 ALA E 688
REMARK 465 SER F 554
REMARK 465 MET F 555
REMARK 465 GLU F 556
REMARK 465 GLN F 557
REMARK 465 VAL F 558
REMARK 465 ALA F 559
REMARK 465 MET F 560
REMARK 465 GLU F 561
REMARK 465 LEU F 562
REMARK 465 ARG F 563
REMARK 465 GLU F 677
REMARK 465 ALA F 678
REMARK 465 SER F 679
REMARK 465 GLY F 680
REMARK 465 MET F 681
REMARK 465 HIS F 682
REMARK 465 LEU F 683
REMARK 465 PRO F 684
REMARK 465 GLU F 685
REMARK 465 ARG F 686
REMARK 465 PRO F 687
REMARK 465 ALA F 688
REMARK 465 SER G 554
REMARK 465 MET G 555
REMARK 465 GLU G 556
REMARK 465 GLN G 557
REMARK 465 VAL G 558
REMARK 465 ALA G 559
REMARK 465 MET G 560
REMARK 465 GLU G 561
REMARK 465 LEU G 562
REMARK 465 ARG G 563
REMARK 465 GLU G 676
REMARK 465 GLU G 677
REMARK 465 ALA G 678
REMARK 465 SER G 679
REMARK 465 GLY G 680
REMARK 465 MET G 681
REMARK 465 HIS G 682
REMARK 465 LEU G 683
REMARK 465 PRO G 684
REMARK 465 GLU G 685
REMARK 465 ARG G 686
REMARK 465 PRO G 687
REMARK 465 ALA G 688
REMARK 465 SER H 554
REMARK 465 MET H 555
REMARK 465 GLU H 556
REMARK 465 GLN H 557
REMARK 465 VAL H 558
REMARK 465 ALA H 559
REMARK 465 MET H 560
REMARK 465 GLU H 561
REMARK 465 LEU H 562
REMARK 465 ARG H 563
REMARK 465 LEU H 564
REMARK 465 THR H 565
REMARK 465 GLY H 674
REMARK 465 LEU H 675
REMARK 465 GLU H 676
REMARK 465 GLU H 677
REMARK 465 ALA H 678
REMARK 465 SER H 679
REMARK 465 GLY H 680
REMARK 465 MET H 681
REMARK 465 HIS H 682
REMARK 465 LEU H 683
REMARK 465 PRO H 684
REMARK 465 GLU H 685
REMARK 465 ARG H 686
REMARK 465 PRO H 687
REMARK 465 ALA H 688
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 563 NE CZ NH1 NH2
REMARK 470 ARG A 644 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 654 NE CZ NH1 NH2
REMARK 470 ARG A 667 NE CZ NH1 NH2
REMARK 470 ARG B 563 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 622 CE NZ
REMARK 470 ARG B 644 NE CZ NH1 NH2
REMARK 470 ASP B 645 CG OD1 OD2
REMARK 470 ARG B 667 NE CZ NH1 NH2
REMARK 470 LYS C 594 CE NZ
REMARK 470 LYS C 604 CE NZ
REMARK 470 GLN C 619 CG CD OE1 NE2
REMARK 470 LYS C 622 CE NZ
REMARK 470 ARG C 644 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 654 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 564 CG CD1 CD2
REMARK 470 THR D 565 OG1 CG2
REMARK 470 LYS D 594 CD CE NZ
REMARK 470 LYS D 604 CE NZ
REMARK 470 ARG E 563 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 595 CG CD OE1 OE2
REMARK 470 ARG E 644 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 645 CG OD1 OD2
REMARK 470 ARG E 650 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 654 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 667 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 668 NE CZ NH1 NH2
REMARK 470 LYS F 604 CE NZ
REMARK 470 LYS F 614 CE NZ
REMARK 470 LYS F 622 CE NZ
REMARK 470 LYS F 640 CE NZ
REMARK 470 ARG F 644 CG CD NE CZ NH1 NH2
REMARK 470 ASP F 645 CG OD1 OD2
REMARK 470 ARG F 650 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 654 NE CZ NH1 NH2
REMARK 470 GLN F 665 CG CD OE1 NE2
REMARK 470 ARG F 667 NE CZ NH1 NH2
REMARK 470 ARG F 668 NE CZ NH1 NH2
REMARK 470 LEU F 675 CG CD1 CD2
REMARK 470 GLU F 676 CG CD OE1 OE2
REMARK 470 LEU G 564 CG CD1 CD2
REMARK 470 LYS G 594 CG CD CE NZ
REMARK 470 GLU G 595 CG CD OE1 OE2
REMARK 470 LYS G 604 CG CD CE NZ
REMARK 470 LYS G 622 CE NZ
REMARK 470 LYS G 640 CD CE NZ
REMARK 470 ARG G 644 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 567 CG CD1 CD2
REMARK 470 ARG H 585 NE CZ NH1 NH2
REMARK 470 LYS H 614 CD CE NZ
REMARK 470 GLN H 619 CG CD OE1 NE2
REMARK 470 LYS H 640 CG CD CE NZ
REMARK 470 ARG H 644 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 645 CG OD1 OD2
REMARK 470 THR H 646 OG1 CG2
REMARK 470 VAL H 647 CG1 CG2
REMARK 470 ARG H 654 CG CD NE CZ NH1 NH2
REMARK 470 ILE H 673 CG1 CG2 CD1
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 OAB MB3 C 1 O HOH C 132 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 170 O HOH E 150 1556 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 615 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 615 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG H 668 NE - CZ - NH2 ANGL. DEV. = 3.4 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 ARG A 563 70.14 -103.77
REMARK 500 ASP A 582 53.90 -114.38
REMARK 500 GLN B 619 50.50 36.12
REMARK 500 ASP D 645 42.56 -90.43
REMARK 500 GLU E 677 73.92 -68.09
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 MB3 C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 2
DBREF 3RCW A 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW B 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW C 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW D 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW E 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW F 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW G 556 688 UNP O95696 BRD1_HUMAN 556 688
DBREF 3RCW H 556 688 UNP O95696 BRD1_HUMAN 556 688
SEQADV 3RCW SER A 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET A 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER B 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET B 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER C 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET C 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER D 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET D 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER E 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET E 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER F 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET F 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER G 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET G 555 UNP O95696 EXPRESSION TAG
SEQADV 3RCW SER H 554 UNP O95696 EXPRESSION TAG
SEQADV 3RCW MET H 555 UNP O95696 EXPRESSION TAG
SEQRES 1 A 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 A 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 A 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 A 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 A 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 A 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 A 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 A 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 A 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 A 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 A 135 PRO GLU ARG PRO ALA
SEQRES 1 B 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 B 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 B 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 B 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 B 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 B 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 B 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 B 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 B 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 B 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 B 135 PRO GLU ARG PRO ALA
SEQRES 1 C 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 C 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 C 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 C 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 C 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 C 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 C 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 C 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 C 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 C 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 C 135 PRO GLU ARG PRO ALA
SEQRES 1 D 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 D 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 D 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 D 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 D 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 D 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 D 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 D 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 D 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 D 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 D 135 PRO GLU ARG PRO ALA
SEQRES 1 E 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 E 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 E 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 E 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 E 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 E 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 E 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 E 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 E 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 E 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 E 135 PRO GLU ARG PRO ALA
SEQRES 1 F 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 F 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 F 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 F 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 F 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 F 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 F 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 F 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 F 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 F 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 F 135 PRO GLU ARG PRO ALA
SEQRES 1 G 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 G 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 G 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 G 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 G 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 G 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 G 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 G 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 G 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 G 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 G 135 PRO GLU ARG PRO ALA
SEQRES 1 H 135 SER MET GLU GLN VAL ALA MET GLU LEU ARG LEU THR PRO
SEQRES 2 H 135 LEU THR VAL LEU LEU ARG SER VAL LEU ASP GLN LEU GLN
SEQRES 3 H 135 ASP LYS ASP PRO ALA ARG ILE PHE ALA GLN PRO VAL SER
SEQRES 4 H 135 LEU LYS GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS HIS
SEQRES 5 H 135 PRO MET ASP PHE ALA THR MET ARG LYS ARG LEU GLU ALA
SEQRES 6 H 135 GLN GLY TYR LYS ASN LEU HIS GLU PHE GLU GLU ASP PHE
SEQRES 7 H 135 ASP LEU ILE ILE ASP ASN CYS MET LYS TYR ASN ALA ARG
SEQRES 8 H 135 ASP THR VAL PHE TYR ARG ALA ALA VAL ARG LEU ARG ASP
SEQRES 9 H 135 GLN GLY GLY VAL VAL LEU ARG GLN ALA ARG ARG GLU VAL
SEQRES 10 H 135 ASP SER ILE GLY LEU GLU GLU ALA SER GLY MET HIS LEU
SEQRES 11 H 135 PRO GLU ARG PRO ALA
HET MB3 C 1 7
HET ACT D 1 4
HET EDO F 2 4
HET EDO G 1 4
HET ACT H 2 4
HETNAM MB3 1-METHYLPYRROLIDIN-2-ONE
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 MB3 C5 H9 N O
FORMUL 10 ACT 2(C2 H3 O2 1-)
FORMUL 11 EDO 2(C2 H6 O2)
FORMUL 14 HOH *166(H2 O)
HELIX 1 1 THR A 565 LYS A 581 1 17
HELIX 2 2 ASP A 598 ILE A 603 1 6
HELIX 3 3 ASP A 608 ALA A 618 1 11
HELIX 4 4 ASN A 623 ASN A 642 1 20
HELIX 5 5 THR A 646 GLU A 677 1 32
HELIX 6 6 THR B 565 LYS B 581 1 17
HELIX 7 7 ASP B 598 HIS B 602 5 5
HELIX 8 8 ASP B 608 ALA B 618 1 11
HELIX 9 9 ASN B 623 ASN B 642 1 20
HELIX 10 10 THR B 646 LEU B 675 1 30
HELIX 11 11 GLU B 676 GLY B 680 5 5
HELIX 12 12 THR C 565 LYS C 581 1 17
HELIX 13 13 ASP C 598 ILE C 603 1 6
HELIX 14 14 ASP C 608 ALA C 618 1 11
HELIX 15 15 ASN C 623 ASN C 642 1 20
HELIX 16 16 THR C 646 GLY C 674 1 29
HELIX 17 17 LEU D 564 ASP D 580 1 17
HELIX 18 18 ASP D 598 ILE D 603 1 6
HELIX 19 19 ASP D 608 ALA D 618 1 11
HELIX 20 20 ASN D 623 ASN D 642 1 20
HELIX 21 21 THR D 646 LEU D 675 1 30
HELIX 22 22 THR E 565 LYS E 581 1 17
HELIX 23 23 ASP E 598 ILE E 603 1 6
HELIX 24 24 ASP E 608 ALA E 618 1 11
HELIX 25 25 ASN E 623 ASN E 642 1 20
HELIX 26 26 THR E 646 GLU E 677 1 32
HELIX 27 27 THR F 565 ASP F 580 1 16
HELIX 28 28 ASP F 598 ILE F 603 1 6
HELIX 29 29 ASP F 608 ALA F 618 1 11
HELIX 30 30 ASN F 623 ASN F 642 1 20
HELIX 31 31 THR F 646 GLU F 676 1 31
HELIX 32 32 THR G 565 LYS G 581 1 17
HELIX 33 33 ASP G 598 ILE G 603 1 6
HELIX 34 34 ASP G 608 ALA G 618 1 11
HELIX 35 35 ASN G 623 ASN G 642 1 20
HELIX 36 36 THR G 646 GLY G 674 1 29
HELIX 37 37 PRO H 566 ASP H 580 1 15
HELIX 38 38 ASP H 598 ILE H 603 1 6
HELIX 39 39 ASP H 608 GLU H 617 1 10
HELIX 40 40 ASN H 623 ASN H 642 1 20
HELIX 41 41 THR H 646 ILE H 673 1 28
CISPEP 1 GLU A 677 ALA A 678 0 2.04
SITE 1 AC1 7 HOH C 132 ILE C 586 PHE C 587 VAL C 591
SITE 2 AC1 7 CYS C 638 ASN C 642 PHE C 648
SITE 1 AC2 4 ARG D 615 GLU D 626 GLU D 629 TYR H 649
SITE 1 AC3 5 SER E 573 GLN E 577 LEU F 570 SER F 573
SITE 2 AC3 5 GLN F 577
SITE 1 AC4 5 ASN G 623 LEU G 624 HIS G 625 ARG G 667
SITE 2 AC4 5 VAL G 670
SITE 1 AC5 3 PRO H 590 VAL H 591 PRO H 606
CRYST1 43.137 51.245 130.626 100.61 90.75 93.89 P 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 0.023182 0.001576 0.000606 0.00000
SCALE2 0.000000 0.019559 0.003690 0.00000
SCALE3 0.000000 0.000000 0.007791 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
