HEADER TRANSCRIPTION 15-SEP-09 3JV6
TITLE CRYSTAL STRUCTURE OF THE DIMERIZATION DOMAINS P52 AND RELB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR RELB;
COMPND 3 CHAIN: A, C, E;
COMPND 4 FRAGMENT: DIMERIZATION DOMAIN (UNP RESIDUES 278-378);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NUCLEAR FACTOR NF-KAPPA-B P100 SUBUNIT;
COMPND 8 CHAIN: B, D, F;
COMPND 9 FRAGMENT: DIMERIZATION DOMAIN (UNP RESIDUES 225-331);
COMPND 10 SYNONYM: DNA-BINDING FACTOR KBF2, NUCLEAR FACTOR NF-KAPPA-B P52
COMPND 11 SUBUNIT;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RELB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: P52;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS NF-KB PROTEIN, HETERODIMER, RELB AND P52, ACTIVATOR, NUCLEUS,
KEYWDS 2 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, ANK REPEAT,
KEYWDS 3 DNA-BINDING, ISOPEPTIDE BOND
EXPDTA X-RAY DIFFRACTION
AUTHOR D.VU,D.B.HUANG,G.GHOSH
REVDAT 4 21-FEB-24 3JV6 1 REMARK SEQADV
REVDAT 3 04-SEP-13 3JV6 1 JRNL
REVDAT 2 27-MAR-13 3JV6 1 JRNL VERSN
REVDAT 1 24-NOV-10 3JV6 0
JRNL AUTH D.VU,D.B.HUANG,A.VEMU,G.GHOSH
JRNL TITL A STRUCTURAL BASIS FOR SELECTIVE DIMERIZATION BY NF-KAPPA B
JRNL TITL 2 RELB.
JRNL REF J.MOL.BIOL. V. 425 1934 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23485337
JRNL DOI 10.1016/J.JMB.2013.02.020
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 136706.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.3
REMARK 3 NUMBER OF REFLECTIONS : 26839
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 SET) : 0.205
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 35.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1561
REMARK 3 BIN R VALUE (WORKING SET) : 0.4450
REMARK 3 BIN FREE R VALUE : 0.4960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 85
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.054
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -33.02000
REMARK 3 B22 (A**2) : 67.79000
REMARK 3 B33 (A**2) : -34.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 1.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.870
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 44.26
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : AS.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : AS.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3JV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : NULL
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30666
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.55400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 63.16750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 70.57200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.49300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 63.16750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 70.57200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.49300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 63.16750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.57200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.49300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 63.16750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 70.57200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 84.49300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASP D 331
REMARK 465 GLU F 330
REMARK 465 ASP F 331
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 285 157.99 172.81
REMARK 500 LYS A 305 126.05 -33.91
REMARK 500 ASP A 310 58.40 -162.27
REMARK 500 GLU A 321 105.02 178.24
REMARK 500 PRO A 377 170.31 -57.27
REMARK 500 ASP B 234 -63.74 -19.48
REMARK 500 LYS B 252 108.53 -24.69
REMARK 500 LYS B 255 -40.94 -28.14
REMARK 500 ASP B 265 12.68 -63.96
REMARK 500 ASP B 266 -166.30 -73.39
REMARK 500 PHE B 276 146.73 -173.35
REMARK 500 LYS B 283 38.78 34.31
REMARK 500 LYS B 298 44.56 -95.25
REMARK 500 PRO B 302 103.04 -47.84
REMARK 500 VAL B 328 102.46 -56.87
REMARK 500 GLU B 330 -174.84 -58.50
REMARK 500 ARG C 285 158.25 177.23
REMARK 500 LYS C 305 130.42 -38.95
REMARK 500 ASP C 310 55.90 -162.45
REMARK 500 GLU C 321 102.88 174.03
REMARK 500 PRO C 377 -178.93 -59.48
REMARK 500 ASP D 234 -77.16 -40.56
REMARK 500 LYS D 252 130.73 -30.75
REMARK 500 LYS D 255 -47.38 -27.41
REMARK 500 TYR D 263 149.07 178.89
REMARK 500 ASP D 266 -146.91 -158.14
REMARK 500 ASP D 280 5.78 -57.42
REMARK 500 LYS D 283 53.20 31.66
REMARK 500 GLN D 284 -18.48 68.25
REMARK 500 ARG D 313 -81.85 -71.91
REMARK 500 LYS E 305 126.56 -33.95
REMARK 500 ASP E 310 56.96 -162.93
REMARK 500 GLU E 321 99.54 176.31
REMARK 500 PRO E 377 -178.58 -66.02
REMARK 500 ASP F 234 -67.50 -17.86
REMARK 500 LYS F 252 110.47 -26.48
REMARK 500 LYS F 255 -39.62 -30.28
REMARK 500 ASP F 266 -154.69 -152.79
REMARK 500 PHE F 276 148.82 -173.31
REMARK 500 GLN F 284 -2.06 70.88
REMARK 500 LYS F 298 39.49 -90.28
REMARK 500 PRO F 302 103.01 -49.17
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 SO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 609
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JTC RELATED DB: PDB
REMARK 900 RELATED ID: 3JUZ RELATED DB: PDB
REMARK 900 RELATED ID: 3JV0 RELATED DB: PDB
REMARK 900 RELATED ID: 3JV4 RELATED DB: PDB
REMARK 900 RELATED ID: 3JV5 RELATED DB: PDB
DBREF 3JV6 A 278 378 UNP Q04863 RELB_MOUSE 278 378
DBREF 3JV6 B 225 331 UNP Q9WTK5 NFKB2_MOUSE 225 331
DBREF 3JV6 C 278 378 UNP Q04863 RELB_MOUSE 278 378
DBREF 3JV6 D 225 331 UNP Q9WTK5 NFKB2_MOUSE 225 331
DBREF 3JV6 E 278 378 UNP Q04863 RELB_MOUSE 278 378
DBREF 3JV6 F 225 331 UNP Q9WTK5 NFKB2_MOUSE 225 331
SEQADV 3JV6 VAL B 328 UNP Q9WTK5 LEU 328 CONFLICT
SEQADV 3JV6 VAL D 328 UNP Q9WTK5 LEU 328 CONFLICT
SEQADV 3JV6 VAL F 328 UNP Q9WTK5 LEU 328 CONFLICT
SEQRES 1 A 101 THR SER GLU LEU ARG ILE CYS ARG ILE ASN LYS GLU SER
SEQRES 2 A 101 GLY PRO CYS THR GLY GLY GLU GLU LEU TYR LEU LEU CYS
SEQRES 3 A 101 ASP LYS VAL GLN LYS GLU ASP ILE SER VAL VAL PHE SER
SEQRES 4 A 101 THR ALA SER TRP GLU GLY ARG ALA ASP PHE SER GLN ALA
SEQRES 5 A 101 ASP VAL HIS ARG GLN ILE ALA ILE VAL PHE LYS THR PRO
SEQRES 6 A 101 PRO TYR GLU ASP LEU GLU ILE SER GLU PRO VAL THR VAL
SEQRES 7 A 101 ASN VAL PHE LEU GLN ARG LEU THR ASP GLY VAL CYS SER
SEQRES 8 A 101 GLU PRO LEU PRO PHE THR TYR LEU PRO ARG
SEQRES 1 B 107 ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA
SEQRES 2 B 107 GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS
SEQRES 3 B 107 ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR
SEQRES 4 B 107 GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE
SEQRES 5 B 107 SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE
SEQRES 6 B 107 ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO
SEQRES 7 B 107 VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY
SEQRES 8 B 107 ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO VAL
SEQRES 9 B 107 VAL GLU ASP
SEQRES 1 C 101 THR SER GLU LEU ARG ILE CYS ARG ILE ASN LYS GLU SER
SEQRES 2 C 101 GLY PRO CYS THR GLY GLY GLU GLU LEU TYR LEU LEU CYS
SEQRES 3 C 101 ASP LYS VAL GLN LYS GLU ASP ILE SER VAL VAL PHE SER
SEQRES 4 C 101 THR ALA SER TRP GLU GLY ARG ALA ASP PHE SER GLN ALA
SEQRES 5 C 101 ASP VAL HIS ARG GLN ILE ALA ILE VAL PHE LYS THR PRO
SEQRES 6 C 101 PRO TYR GLU ASP LEU GLU ILE SER GLU PRO VAL THR VAL
SEQRES 7 C 101 ASN VAL PHE LEU GLN ARG LEU THR ASP GLY VAL CYS SER
SEQRES 8 C 101 GLU PRO LEU PRO PHE THR TYR LEU PRO ARG
SEQRES 1 D 107 ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA
SEQRES 2 D 107 GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS
SEQRES 3 D 107 ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR
SEQRES 4 D 107 GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE
SEQRES 5 D 107 SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE
SEQRES 6 D 107 ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO
SEQRES 7 D 107 VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY
SEQRES 8 D 107 ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO VAL
SEQRES 9 D 107 VAL GLU ASP
SEQRES 1 E 101 THR SER GLU LEU ARG ILE CYS ARG ILE ASN LYS GLU SER
SEQRES 2 E 101 GLY PRO CYS THR GLY GLY GLU GLU LEU TYR LEU LEU CYS
SEQRES 3 E 101 ASP LYS VAL GLN LYS GLU ASP ILE SER VAL VAL PHE SER
SEQRES 4 E 101 THR ALA SER TRP GLU GLY ARG ALA ASP PHE SER GLN ALA
SEQRES 5 E 101 ASP VAL HIS ARG GLN ILE ALA ILE VAL PHE LYS THR PRO
SEQRES 6 E 101 PRO TYR GLU ASP LEU GLU ILE SER GLU PRO VAL THR VAL
SEQRES 7 E 101 ASN VAL PHE LEU GLN ARG LEU THR ASP GLY VAL CYS SER
SEQRES 8 E 101 GLU PRO LEU PRO PHE THR TYR LEU PRO ARG
SEQRES 1 F 107 ALA SER ASN LEU LYS ILE SER ARG MET ASP LYS THR ALA
SEQRES 2 F 107 GLY SER VAL ARG GLY GLY ASP GLU VAL TYR LEU LEU CYS
SEQRES 3 F 107 ASP LYS VAL GLN LYS ASP ASP ILE GLU VAL ARG PHE TYR
SEQRES 4 F 107 GLU ASP ASP GLU ASN GLY TRP GLN ALA PHE GLY ASP PHE
SEQRES 5 F 107 SER PRO THR ASP VAL HIS LYS GLN TYR ALA ILE VAL PHE
SEQRES 6 F 107 ARG THR PRO PRO TYR HIS LYS MET LYS ILE GLU ARG PRO
SEQRES 7 F 107 VAL THR VAL PHE LEU GLN LEU LYS ARG LYS ARG GLY GLY
SEQRES 8 F 107 ASP VAL SER ASP SER LYS GLN PHE THR TYR TYR PRO VAL
SEQRES 9 F 107 VAL GLU ASP
HET SO4 A 606 5
HET SO4 B 601 5
HET SO4 B 607 5
HET SO4 C 605 5
HET SO4 D 603 5
HET SO4 D 608 5
HET SO4 E 604 5
HET SO4 F 602 5
HET SO4 F 609 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 9(O4 S 2-)
FORMUL 16 HOH *146(H2 O)
HELIX 1 1 SER A 327 GLN A 334 5 8
HELIX 2 2 SER B 277 THR B 279 5 3
HELIX 3 3 SER C 327 GLN C 334 5 8
HELIX 4 4 SER E 327 GLN E 334 5 8
HELIX 5 5 SER F 277 THR F 279 5 3
SHEET 1 A 3 ILE A 283 ILE A 286 0
SHEET 2 A 3 GLU A 298 CYS A 303 -1 O LEU A 302 N CYS A 284
SHEET 3 A 3 ALA A 336 LYS A 340 -1 O PHE A 339 N LEU A 299
SHEET 1 B 5 SER A 290 PRO A 292 0
SHEET 2 B 5 LEU A 371 LEU A 376 1 O LEU A 376 N GLY A 291
SHEET 3 B 5 VAL A 353 GLN A 360 -1 N VAL A 355 O PHE A 373
SHEET 4 B 5 SER A 312 SER A 316 -1 N SER A 316 O ASN A 356
SHEET 5 B 5 GLU A 321 ARG A 323 -1 O GLY A 322 N PHE A 315
SHEET 1 C 4 ILE B 230 MET B 233 0
SHEET 2 C 4 GLU B 245 CYS B 250 -1 O LEU B 249 N ARG B 232
SHEET 3 C 4 ALA B 286 ARG B 290 -1 O ILE B 287 N LEU B 248
SHEET 4 C 4 VAL B 281 HIS B 282 -1 N HIS B 282 O ALA B 286
SHEET 1 D 5 ALA B 237 SER B 239 0
SHEET 2 D 5 LYS B 321 TYR B 326 1 O TYR B 326 N GLY B 238
SHEET 3 D 5 VAL B 303 ARG B 311 -1 N VAL B 303 O TYR B 325
SHEET 4 D 5 ILE B 258 TYR B 263 -1 N TYR B 263 O PHE B 306
SHEET 5 D 5 GLN B 271 PHE B 273 -1 O ALA B 272 N PHE B 262
SHEET 1 E 3 ILE C 283 ILE C 286 0
SHEET 2 E 3 GLU C 298 CYS C 303 -1 O LEU C 302 N CYS C 284
SHEET 3 E 3 ALA C 336 LYS C 340 -1 O PHE C 339 N LEU C 299
SHEET 1 F 5 SER C 290 PRO C 292 0
SHEET 2 F 5 LEU C 371 LEU C 376 1 O LEU C 376 N GLY C 291
SHEET 3 F 5 VAL C 353 GLN C 360 -1 N VAL C 355 O PHE C 373
SHEET 4 F 5 SER C 312 SER C 316 -1 N SER C 316 O ASN C 356
SHEET 5 F 5 GLU C 321 ARG C 323 -1 O GLY C 322 N PHE C 315
SHEET 1 G 4 ILE D 230 MET D 233 0
SHEET 2 G 4 GLU D 245 CYS D 250 -1 O LEU D 249 N ARG D 232
SHEET 3 G 4 ALA D 286 ARG D 290 -1 O ILE D 287 N LEU D 248
SHEET 4 G 4 VAL D 281 HIS D 282 -1 N HIS D 282 O ALA D 286
SHEET 1 H 5 ALA D 237 SER D 239 0
SHEET 2 H 5 LYS D 321 TYR D 326 1 O THR D 324 N GLY D 238
SHEET 3 H 5 VAL D 303 ARG D 311 -1 N VAL D 305 O PHE D 323
SHEET 4 H 5 ILE D 258 TYR D 263 -1 N ARG D 261 O GLN D 308
SHEET 5 H 5 GLN D 271 PHE D 273 -1 O ALA D 272 N PHE D 262
SHEET 1 I 3 ILE E 283 ILE E 286 0
SHEET 2 I 3 GLU E 298 CYS E 303 -1 O LEU E 302 N CYS E 284
SHEET 3 I 3 ALA E 336 LYS E 340 -1 O PHE E 339 N LEU E 299
SHEET 1 J 5 SER E 290 PRO E 292 0
SHEET 2 J 5 LEU E 371 LEU E 376 1 O LEU E 376 N GLY E 291
SHEET 3 J 5 VAL E 353 GLN E 360 -1 N VAL E 353 O TYR E 375
SHEET 4 J 5 SER E 312 SER E 316 -1 N SER E 316 O ASN E 356
SHEET 5 J 5 GLU E 321 ARG E 323 -1 O GLY E 322 N PHE E 315
SHEET 1 K 4 ILE F 230 MET F 233 0
SHEET 2 K 4 GLU F 245 CYS F 250 -1 O LEU F 249 N ARG F 232
SHEET 3 K 4 ALA F 286 ARG F 290 -1 O ILE F 287 N LEU F 248
SHEET 4 K 4 VAL F 281 HIS F 282 -1 N HIS F 282 O ALA F 286
SHEET 1 L 5 ALA F 237 SER F 239 0
SHEET 2 L 5 LYS F 321 TYR F 326 1 O TYR F 326 N GLY F 238
SHEET 3 L 5 VAL F 303 ARG F 311 -1 N VAL F 303 O TYR F 325
SHEET 4 L 5 ILE F 258 TYR F 263 -1 N ARG F 261 O GLN F 308
SHEET 5 L 5 GLN F 271 PHE F 273 -1 O ALA F 272 N PHE F 262
SITE 1 AC1 3 LYS A 308 VAL A 331 ARG A 333
SITE 1 AC2 5 LYS B 235 ASP B 244 GLU B 245 ARG B 290
SITE 2 AC2 5 GLN D 271
SITE 1 AC3 4 LYS B 255 LYS B 283 GLN B 284 HOH B 476
SITE 1 AC4 4 LYS C 308 VAL C 331 ARG C 333 HOH C 505
SITE 1 AC5 5 LYS D 235 GLU D 245 ARG D 290 HOH D 473
SITE 2 AC5 5 GLN F 271
SITE 1 AC6 2 LYS D 283 GLN D 284
SITE 1 AC7 3 LYS E 308 ARG E 333 HOH E 509
SITE 1 AC8 3 GLN B 271 GLU F 245 ARG F 290
SITE 1 AC9 2 LYS F 255 LYS F 283
CRYST1 126.335 141.144 168.986 90.00 90.00 90.00 I 2 2 2 24
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 0.007915 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007085 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005918 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
