HEADER TRANSCRIPTION/SIGNALING PROTEIN 12-NOV-08 2ZVO
TITLE NEMO COZI DOMAIN IN COMPLEX WITH DIUBIQUITIN IN C2 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBC PROTEIN;
COMPND 3 CHAIN: A, G;
COMPND 4 FRAGMENT: UBIQUITIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NF-KAPPA-B ESSENTIAL MODULATOR;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: CC2-LZ, COZI DOMAIN;
COMPND 10 SYNONYM: NEMO, NF-KAPPA-B ESSENTIAL MODIFIER, INHIBITOR OF NUCLEAR
COMPND 11 FACTOR KAPPA-B KINASE SUBUNIT GAMMA, IKB KINASE SUBUNIT GAMMA, I-
COMPND 12 KAPPA-B KINASE GAMMA, IKK-GAMMA, IKKG, IKB KINASE-ASSOCIATED PROTEIN
COMPND 13 1, IKKAP1, MFIP-3;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX4T1
KEYWDS NF-KB SIGNALING, UBIQUITIN BINDING, COILED COIL, CYTOPLASM, METAL-
KEYWDS 2 BINDING, NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 3 REGULATION, UBL CONJUGATION, ZINC, ZINC-FINGER, TRANSCRIPTION-
KEYWDS 4 SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RAHIGHI,F.IKEDA,M.KAWASAKI,M.AKUTSU,N.SUZUKI,R.KATO,T.KENSCHE,
AUTHOR 2 T.UEJIMA,S.BLOOR,D.KOMANDER,F.RANDOW,S.WAKATSUKI,I.DIKIC
REVDAT 4 10-NOV-21 2ZVO 1 SEQADV
REVDAT 3 11-OCT-17 2ZVO 1 REMARK
REVDAT 2 14-APR-09 2ZVO 1 JRNL
REVDAT 1 24-MAR-09 2ZVO 0
JRNL AUTH S.RAHIGHI,F.IKEDA,M.KAWASAKI,M.AKUTSU,N.SUZUKI,R.KATO,
JRNL AUTH 2 T.KENSCHE,T.UEJIMA,S.BLOOR,D.KOMANDER,F.RANDOW,S.WAKATSUKI,
JRNL AUTH 3 I.DIKIC
JRNL TITL SPECIFIC RECOGNITION OF LINEAR UBIQUITIN CHAINS BY NEMO IS
JRNL TITL 2 IMPORTANT FOR NF-KAPPAB ACTIVATION
JRNL REF CELL(CAMBRIDGE,MASS.) V. 136 1098 2009
JRNL REFN ISSN 0092-8674
JRNL PMID 19303852
JRNL DOI 10.1016/J.CELL.2009.03.007
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 11951
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 646
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 760
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 29
REMARK 3 BIN FREE R VALUE : 0.4980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3791
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.48000
REMARK 3 B22 (A**2) : 1.09000
REMARK 3 B33 (A**2) : 1.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.57000
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): 0.488
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.355
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.759
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3833 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5149 ; 1.282 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 467 ; 5.273 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;42.788 ;26.296
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 800 ;19.649 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;23.149 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 596 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2801 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1931 ; 0.245 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2610 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 170 ; 0.182 ; 0.200
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): 82 ; 0.270 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.093 ; 0.200
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): 2417 ; 0.552 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3800 ; 0.958 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1530 ; 1.120 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1349 ; 1.827 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2ZVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000028483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15653
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 88.9
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.16200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4620
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.23600
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: NULL
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 (%): 56.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP
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 65.43050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.18600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.43050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.18600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 LEU A 149
REMARK 465 ARG A 150
REMARK 465 GLY A 151
REMARK 465 GLY A 152
REMARK 465 GLY G -1
REMARK 465 SER G 0
REMARK 465 LEU G 147
REMARK 465 ARG G 148
REMARK 465 LEU G 149
REMARK 465 ARG G 150
REMARK 465 GLY G 151
REMARK 465 GLY G 152
REMARK 465 GLY B 248
REMARK 465 SER B 249
REMARK 465 VAL B 338
REMARK 465 GLY B 339
REMARK 465 GLY D 248
REMARK 465 SER D 249
REMARK 465 VAL D 338
REMARK 465 GLY D 339
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 NH2 ARG B 309 OE2 GLU D 308 2.15
REMARK 500 O GLY A 75 O HOH A 153 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 PRO G 38 C - N - CA ANGL. DEV. = 9.4 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 MET A 1 -174.63 -58.09
REMARK 500 LYS A 11 98.70 84.82
REMARK 500 LEU A 84 28.21 -69.87
REMARK 500 ALA A 122 74.48 43.20
REMARK 500 ASN A 136 63.09 21.03
REMARK 500 LYS G 11 83.37 60.63
REMARK 500 GLU G 64 6.13 55.51
REMARK 500 PRO G 95 49.91 -68.23
REMARK 500 SER G 96 -24.35 -152.62
REMARK 500 ALA G 122 73.60 45.99
REMARK 500 LYS G 124 100.37 76.74
REMARK 500 MET B 251 -18.97 60.17
REMARK 500 MET D 251 -9.39 -56.92
REMARK 500 LEU D 253 33.30 -81.75
REMARK 500 ALA D 285 -39.38 -39.01
REMARK 500 GLN D 328 5.33 -58.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZVN RELATED DB: PDB
REMARK 900 RELATED ID: 3F89 RELATED DB: PDB
DBREF 2ZVO A 1 152 UNP Q96C32 Q96C32_HUMAN 1 152
DBREF 2ZVO G 1 152 UNP Q96C32 Q96C32_HUMAN 1 152
DBREF 2ZVO B 250 339 UNP O88522 NEMO_MOUSE 250 339
DBREF 2ZVO D 250 339 UNP O88522 NEMO_MOUSE 250 339
SEQADV 2ZVO GLY A -1 UNP Q96C32 EXPRESSION TAG
SEQADV 2ZVO SER A 0 UNP Q96C32 EXPRESSION TAG
SEQADV 2ZVO GLY G -1 UNP Q96C32 EXPRESSION TAG
SEQADV 2ZVO SER G 0 UNP Q96C32 EXPRESSION TAG
SEQADV 2ZVO GLY B 248 UNP O88522 EXPRESSION TAG
SEQADV 2ZVO SER B 249 UNP O88522 EXPRESSION TAG
SEQADV 2ZVO ALA B 282 UNP O88522 GLU 282 ENGINEERED MUTATION
SEQADV 2ZVO ALA B 285 UNP O88522 LYS 285 ENGINEERED MUTATION
SEQADV 2ZVO GLY D 248 UNP O88522 EXPRESSION TAG
SEQADV 2ZVO SER D 249 UNP O88522 EXPRESSION TAG
SEQADV 2ZVO ALA D 282 UNP O88522 GLU 282 ENGINEERED MUTATION
SEQADV 2ZVO ALA D 285 UNP O88522 LYS 285 ENGINEERED MUTATION
SEQRES 1 A 154 GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS
SEQRES 2 A 154 THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU
SEQRES 3 A 154 ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO
SEQRES 4 A 154 PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU
SEQRES 5 A 154 GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS
SEQRES 6 A 154 GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 7 A 154 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 8 A 154 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 9 A 154 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 10 A 154 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 11 A 154 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 12 A 154 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 G 154 GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS
SEQRES 2 G 154 THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU
SEQRES 3 G 154 ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO
SEQRES 4 G 154 PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU
SEQRES 5 G 154 GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS
SEQRES 6 G 154 GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 7 G 154 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 8 G 154 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 9 G 154 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 10 G 154 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 11 G 154 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 12 G 154 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 B 92 GLY SER GLY MET GLN LEU GLU ASP LEU ARG GLN GLN LEU
SEQRES 2 B 92 GLN GLN ALA GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU
SEQRES 3 B 92 ILE ASP LYS LEU LYS GLU GLU ALA ALA GLN HIS ALA ILE
SEQRES 4 B 92 VAL MET GLU THR VAL PRO VAL LEU LYS ALA GLN ALA ASP
SEQRES 5 B 92 ILE TYR LYS ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG
SEQRES 6 B 92 GLU LYS LEU VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN
SEQRES 7 B 92 LEU GLU GLN LEU GLN ARG GLU PHE ASN LYS LEU LYS VAL
SEQRES 8 B 92 GLY
SEQRES 1 D 92 GLY SER GLY MET GLN LEU GLU ASP LEU ARG GLN GLN LEU
SEQRES 2 D 92 GLN GLN ALA GLU GLU ALA LEU VAL ALA LYS GLN GLU LEU
SEQRES 3 D 92 ILE ASP LYS LEU LYS GLU GLU ALA ALA GLN HIS ALA ILE
SEQRES 4 D 92 VAL MET GLU THR VAL PRO VAL LEU LYS ALA GLN ALA ASP
SEQRES 5 D 92 ILE TYR LYS ALA ASP PHE GLN ALA GLU ARG HIS ALA ARG
SEQRES 6 D 92 GLU LYS LEU VAL GLU LYS LYS GLU TYR LEU GLN GLU GLN
SEQRES 7 D 92 LEU GLU GLN LEU GLN ARG GLU PHE ASN LYS LEU LYS VAL
SEQRES 8 D 92 GLY
FORMUL 5 HOH *174(H2 O)
HELIX 1 1 THR A 22 GLY A 35 1 14
HELIX 2 2 PRO A 37 ASP A 39 5 3
HELIX 3 3 LEU A 56 ASN A 60 5 5
HELIX 4 4 ILE A 99 GLY A 111 1 13
HELIX 5 5 PRO A 113 ASP A 115 5 3
HELIX 6 6 LEU A 132 ASN A 136 5 5
HELIX 7 7 THR G 22 GLY G 35 1 14
HELIX 8 8 PRO G 37 ASP G 39 5 3
HELIX 9 9 THR G 98 GLY G 111 1 14
HELIX 10 10 PRO G 113 GLN G 117 5 5
HELIX 11 11 LEU B 253 GLU B 289 1 37
HELIX 12 12 THR B 290 LYS B 337 1 48
HELIX 13 13 MET D 251 GLU D 289 1 39
HELIX 14 14 GLU D 289 GLN D 325 1 37
HELIX 15 15 LEU D 326 LEU D 336 1 11
SHEET 1 A 5 THR A 12 GLU A 16 0
SHEET 2 A 5 GLN A 2 LYS A 6 -1 N VAL A 5 O ILE A 13
SHEET 3 A 5 THR A 66 LEU A 71 1 O LEU A 67 N PHE A 4
SHEET 4 A 5 GLN A 41 PHE A 45 -1 N ARG A 42 O VAL A 70
SHEET 5 A 5 LYS A 48 GLN A 49 -1 O LYS A 48 N PHE A 45
SHEET 1 B 5 THR A 88 VAL A 93 0
SHEET 2 B 5 MET A 77 THR A 83 -1 N VAL A 81 O ILE A 89
SHEET 3 B 5 THR A 142 LEU A 147 1 O LEU A 143 N LYS A 82
SHEET 4 B 5 GLN A 117 PHE A 121 -1 N ARG A 118 O VAL A 146
SHEET 5 B 5 LYS A 124 GLN A 125 -1 O LYS A 124 N PHE A 121
SHEET 1 C 5 THR G 12 GLU G 16 0
SHEET 2 C 5 GLN G 2 THR G 7 -1 N VAL G 5 O ILE G 13
SHEET 3 C 5 THR G 66 LEU G 71 1 O LEU G 67 N PHE G 4
SHEET 4 C 5 GLN G 41 PHE G 45 -1 N ILE G 44 O HIS G 68
SHEET 5 C 5 LYS G 48 GLN G 49 -1 O LYS G 48 N PHE G 45
SHEET 1 D 4 THR G 88 VAL G 93 0
SHEET 2 D 4 MET G 77 LYS G 82 -1 N ILE G 79 O LEU G 91
SHEET 3 D 4 THR G 142 VAL G 146 1 O LEU G 143 N PHE G 80
SHEET 4 D 4 ARG G 118 ILE G 120 -1 N ARG G 118 O VAL G 146
CRYST1 130.861 98.372 50.616 90.00 101.96 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 0.007642 0.000000 0.001619 0.00000
SCALE2 0.000000 0.010165 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020195 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
