HEADER TRANSCRIPTION 13-JUL-10 3NXB
TITLE CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN CECR2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAT EYE SYNDROME CRITICAL REGION PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BROMODOMAIN (UNP RESIDUES 424-538);
COMPND 5 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: CECR2, KIAA1740;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS STRUCTURAL GENOMICS CONSORTIUM, SGC, CECR2, CAT EYE SYNDROME
KEYWDS 2 CHROMOSOME REGION CANDIDATE 2, BROMODOMAIN, STRUCTURAL GENOMICS,
KEYWDS 3 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,S.PICAUD,T.KEATES,J.MUNIZ,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 3 31-JAN-18 3NXB 1 AUTHOR
REVDAT 2 11-APR-12 3NXB 1 JRNL VERSN
REVDAT 1 18-AUG-10 3NXB 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. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 22343
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1147
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) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1520
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.4480
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.5390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1639
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : 0.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.26000
REMARK 3 B23 (A**2) : 0.00000
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): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.461
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1720 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1235 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2298 ; 1.423 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3002 ; 0.905 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 201 ; 5.349 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;33.689 ;24.217
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 329 ;15.497 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;16.070 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 235 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1855 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 352 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 437 A 537
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6121 5.2381 16.7843
REMARK 3 T TENSOR
REMARK 3 T11: 0.0756 T22: 0.0556
REMARK 3 T33: 0.0504 T12: 0.0233
REMARK 3 T13: -0.0021 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 0.8978 L22: 0.5976
REMARK 3 L33: 0.6448 L12: -0.1118
REMARK 3 L13: 0.0408 L23: 0.1508
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.0275 S13: 0.0266
REMARK 3 S21: -0.0182 S22: 0.0658 S23: 0.0664
REMARK 3 S31: 0.0950 S32: 0.0512 S33: -0.0580
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 438 B 537
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5872 21.0119 1.0261
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: 0.0539
REMARK 3 T33: 0.1098 T12: -0.0131
REMARK 3 T13: -0.0037 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 1.4637 L22: 0.7943
REMARK 3 L33: 0.4785 L12: 0.4080
REMARK 3 L13: 0.0278 L23: 0.5730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: -0.0197 S13: -0.2992
REMARK 3 S21: -0.0827 S22: -0.0351 S23: -0.0544
REMARK 3 S31: -0.0953 S32: -0.0133 S33: 0.0145
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3NXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060395.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22346
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 29.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : 0.54100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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 PDB ENTRIES 2OSS, 2OUO, 2GRC, 2OO1,
REMARK 200 3DAI, 3D7C, 3DWY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 12% PEG 20,000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 6.5
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 63.58000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.75500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.58000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.75500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 423
REMARK 465 MET A 424
REMARK 465 ARG A 425
REMARK 465 GLU A 426
REMARK 465 GLU A 427
REMARK 465 LYS A 428
REMARK 465 LYS A 429
REMARK 465 THR A 430
REMARK 465 LYS A 431
REMARK 465 ASP A 432
REMARK 465 LEU A 433
REMARK 465 PHE A 434
REMARK 465 GLU A 435
REMARK 465 LEU A 436
REMARK 465 HIS A 538
REMARK 465 SER B 423
REMARK 465 MET B 424
REMARK 465 ARG B 425
REMARK 465 GLU B 426
REMARK 465 GLU B 427
REMARK 465 LYS B 428
REMARK 465 LYS B 429
REMARK 465 THR B 430
REMARK 465 LYS B 431
REMARK 465 ASP B 432
REMARK 465 LEU B 433
REMARK 465 PHE B 434
REMARK 465 GLU B 435
REMARK 465 LEU B 436
REMARK 465 ASP B 437
REMARK 465 HIS B 538
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 437 CG OD1 OD2
REMARK 470 GLN A 473 CD OE1 NE2
REMARK 470 GLU A 516 CD OE1 OE2
REMARK 470 LYS A 537 CG CD CE NZ
REMARK 470 LYS B 454 CE NZ
REMARK 470 LYS B 537 CG CD CE NZ
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 MET B 503 CG - SD - CE ANGL. DEV. = -13.3 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 ALA B 468 67.30 -158.28
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 EDO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3
DBREF 3NXB A 424 538 UNP Q9BXF3 CECR2_HUMAN 424 538
DBREF 3NXB B 424 538 UNP Q9BXF3 CECR2_HUMAN 424 538
SEQADV 3NXB SER A 423 UNP Q9BXF3 EXPRESSION TAG
SEQADV 3NXB SER B 423 UNP Q9BXF3 EXPRESSION TAG
SEQRES 1 A 116 SER MET ARG GLU GLU LYS LYS THR LYS ASP LEU PHE GLU
SEQRES 2 A 116 LEU ASP ASP ASP PHE THR ALA MET TYR LYS VAL LEU ASP
SEQRES 3 A 116 VAL VAL LYS ALA HIS LYS ASP SER TRP PRO PHE LEU GLU
SEQRES 4 A 116 PRO VAL ASP GLU SER TYR ALA PRO ASN TYR TYR GLN ILE
SEQRES 5 A 116 ILE LYS ALA PRO MET ASP ILE SER SER MET GLU LYS LYS
SEQRES 6 A 116 LEU ASN GLY GLY LEU TYR CYS THR LYS GLU GLU PHE VAL
SEQRES 7 A 116 ASN ASP MET LYS THR MET PHE ARG ASN CYS ARG LYS TYR
SEQRES 8 A 116 ASN GLY GLU SER SER GLU TYR THR LYS MET SER ASP ASN
SEQRES 9 A 116 LEU GLU ARG CYS PHE HIS ARG ALA MET MET LYS HIS
SEQRES 1 B 116 SER MET ARG GLU GLU LYS LYS THR LYS ASP LEU PHE GLU
SEQRES 2 B 116 LEU ASP ASP ASP PHE THR ALA MET TYR LYS VAL LEU ASP
SEQRES 3 B 116 VAL VAL LYS ALA HIS LYS ASP SER TRP PRO PHE LEU GLU
SEQRES 4 B 116 PRO VAL ASP GLU SER TYR ALA PRO ASN TYR TYR GLN ILE
SEQRES 5 B 116 ILE LYS ALA PRO MET ASP ILE SER SER MET GLU LYS LYS
SEQRES 6 B 116 LEU ASN GLY GLY LEU TYR CYS THR LYS GLU GLU PHE VAL
SEQRES 7 B 116 ASN ASP MET LYS THR MET PHE ARG ASN CYS ARG LYS TYR
SEQRES 8 B 116 ASN GLY GLU SER SER GLU TYR THR LYS MET SER ASP ASN
SEQRES 9 B 116 LEU GLU ARG CYS PHE HIS ARG ALA MET MET LYS HIS
HET EDO A 1 8
HET EDO B 2 4
HET EDO B 3 8
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 HOH *209(H2 O)
HELIX 1 1 ASP A 438 HIS A 453 1 16
HELIX 2 2 SER A 456 LEU A 460 5 5
HELIX 3 3 ASN A 470 ILE A 475 1 6
HELIX 4 4 ASP A 480 GLY A 490 1 11
HELIX 5 5 THR A 495 GLY A 515 1 21
HELIX 6 6 SER A 518 LYS A 537 1 20
HELIX 7 7 ASP B 438 HIS B 453 1 16
HELIX 8 8 LYS B 454 LEU B 460 5 7
HELIX 9 9 ASP B 464 ALA B 468 5 5
HELIX 10 10 ASN B 470 ILE B 475 1 6
HELIX 11 11 ASP B 480 GLY B 490 1 11
HELIX 12 12 THR B 495 GLY B 515 1 21
HELIX 13 13 SER B 518 MET B 535 1 18
SITE 1 AC1 6 HOH A 173 HOH A 188 PRO A 458 VAL A 463
SITE 2 AC1 6 TYR A 467 ASN A 514
SITE 1 AC2 3 ASP B 439 MET B 443 THR B 495
SITE 1 AC3 8 HOH B 11 HOH B 72 HOH B 198 PRO B 458
SITE 2 AC3 8 VAL B 463 TYR B 513 ASN B 514 TYR B 520
CRYST1 127.160 45.510 45.590 90.00 105.67 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 0.007864 0.000000 0.002206 0.00000
SCALE2 0.000000 0.021973 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022781 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
