HEADER CELL ADHESION 14-APR-09 3H2V
TITLE HUMAN RAVER1 RRM1 DOMAIN IN COMPLEX WITH HUMAN VINCULIN TAIL DOMAIN VT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VINCULIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RAVER-1;
COMPND 8 CHAIN: E, F, G, H;
COMPND 9 FRAGMENT: RRM 1 DOMAIN;
COMPND 10 SYNONYM: RIBONUCLEOPROTEIN PTB-BINDING 1;
COMPND 11 ENGINEERED: 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 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: RAVER1, KIAA1978;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOCAL ADHESION, ACTIN CYTOSKELETON, RNP MOTIF, RNA BINDING,
KEYWDS 2 ALTERNATIVE SPLICING, CYTOPLASM, NUCLEUS, PHOSPHOPROTEIN, RNA-
KEYWDS 3 BINDING, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.LEE,E.S.RANGARAJAN,S.D.YOGESHA,T.IZARD
REVDAT 2 06-SEP-23 3H2V 1 SEQADV
REVDAT 1 28-JUL-09 3H2V 0
JRNL AUTH J.H.LEE,E.S.RANGARAJAN,S.D.YOGESHA,T.IZARD
JRNL TITL RAVER1 INTERACTIONS WITH VINCULIN AND RNA SUGGEST A
JRNL TITL 2 FEED-FORWARD PATHWAY IN DIRECTING MRNA TO FOCAL ADHESIONS
JRNL REF STRUCTURE V. 17 833 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19523901
JRNL DOI 10.1016/J.STR.2009.04.010
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.3.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 23051
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.96
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3308
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2639
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3141
REMARK 3 BIN R VALUE (WORKING SET) : 0.2595
REMARK 3 BIN FREE R VALUE : 0.3483
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.05
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 167
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.33061
REMARK 3 B22 (A**2) : 6.17486
REMARK 3 B33 (A**2) : -11.50547
REMARK 3 B12 (A**2) : -1.62686
REMARK 3 B13 (A**2) : 2.47506
REMARK 3 B23 (A**2) : -2.35676
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.403
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 7762 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 10395 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 1738 ; 0.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 219 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 1097 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 7762 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : 222 ; 5.000 ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23190
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1RKE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS (PH 7.5), 200 MM SODIUM
REMARK 280 NITRATE, AND 16% PEG-3,350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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
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 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 GLU A 879
REMARK 465 GLU A 880
REMARK 465 LYS A 881
REMARK 465 ASP A 882
REMARK 465 GLU A 883
REMARK 465 LYS A 889
REMARK 465 ALA A 890
REMARK 465 GLY A 891
REMARK 465 GLU A 892
REMARK 465 THR A 1062
REMARK 465 PRO A 1063
REMARK 465 TRP A 1064
REMARK 465 TYR A 1065
REMARK 465 GLN A 1066
REMARK 465 GLU B 879
REMARK 465 GLU B 880
REMARK 465 LYS B 881
REMARK 465 ASP B 882
REMARK 465 GLU B 883
REMARK 465 GLN B 888
REMARK 465 LYS B 889
REMARK 465 ALA B 890
REMARK 465 GLY B 891
REMARK 465 ILE B 1046
REMARK 465 LYS B 1047
REMARK 465 ILE B 1048
REMARK 465 ARG B 1049
REMARK 465 THR B 1050
REMARK 465 ASP B 1051
REMARK 465 ALA B 1052
REMARK 465 GLY B 1053
REMARK 465 PHE B 1054
REMARK 465 TRP B 1064
REMARK 465 TYR B 1065
REMARK 465 GLN B 1066
REMARK 465 GLU C 879
REMARK 465 GLU C 880
REMARK 465 LYS C 881
REMARK 465 ASP C 882
REMARK 465 GLU C 883
REMARK 465 GLN C 888
REMARK 465 LYS C 889
REMARK 465 ALA C 890
REMARK 465 GLY C 891
REMARK 465 GLU C 892
REMARK 465 LYS C 1047
REMARK 465 ILE C 1048
REMARK 465 ARG C 1049
REMARK 465 THR C 1050
REMARK 465 ASP C 1051
REMARK 465 ALA C 1052
REMARK 465 GLY C 1053
REMARK 465 PHE C 1054
REMARK 465 TRP C 1064
REMARK 465 TYR C 1065
REMARK 465 GLN C 1066
REMARK 465 GLU D 879
REMARK 465 GLU D 880
REMARK 465 LYS D 881
REMARK 465 ASP D 882
REMARK 465 GLU D 883
REMARK 465 GLN D 888
REMARK 465 LYS D 889
REMARK 465 ALA D 890
REMARK 465 GLY D 891
REMARK 465 GLU D 892
REMARK 465 TRP D 1064
REMARK 465 TYR D 1065
REMARK 465 GLN D 1066
REMARK 465 HIS F 57
REMARK 465 HIS H 57
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 GLU A 887 CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 885 CG PHE A 885 CD1 -0.129
REMARK 500 PHE A 885 CZ PHE A 885 CE2 -0.190
REMARK 500 PHE A 885 CE2 PHE A 885 CD2 -0.157
REMARK 500 PHE A 885 C PHE A 885 O -0.117
REMARK 500 PRO A 886 CG PRO A 886 CD -0.241
REMARK 500 VAL A1038 N VAL A1038 CA -0.122
REMARK 500 VAL A1038 CA VAL A1038 CB -0.266
REMARK 500 VAL A1038 CB VAL A1038 CG1 -0.346
REMARK 500 VAL A1038 CB VAL A1038 CG2 -0.177
REMARK 500 VAL A1038 CA VAL A1038 C -0.174
REMARK 500 VAL A1038 C VAL A1038 O -0.194
REMARK 500 ARG A1039 CB ARG A1039 CG -0.194
REMARK 500 ARG A1039 CZ ARG A1039 NH2 -0.084
REMARK 500 ARG A1039 CA ARG A1039 C -0.172
REMARK 500 ARG A1039 C ARG A1039 O -0.179
REMARK 500 GLU A1040 N GLU A1040 CA -0.126
REMARK 500 GLU A1040 CD GLU A1040 OE2 -0.088
REMARK 500 GLU A1040 C GLU A1040 O -0.190
REMARK 500 ARG E 119 CZ ARG E 119 NH1 -0.104
REMARK 500 ARG E 119 CZ ARG E 119 NH2 -0.092
REMARK 500 ARG E 119 C ARG E 119 O -0.156
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 A 886 C - N - CD ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG A1039 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 GLU A1040 OE1 - CD - OE2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 PRO B 989 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO B1063 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO B1063 C - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO C 989 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO C1063 C - N - CD ANGL. DEV. = -20.8 DEGREES
REMARK 500 PRO D 886 C - N - CD ANGL. DEV. = -32.8 DEGREES
REMARK 500 ARG E 119 NE - CZ - NH1 ANGL. DEV. = 3.9 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 GLU A 887 -149.62 -48.15
REMARK 500 ILE A 894 -140.71 -127.43
REMARK 500 PRO B 886 -167.86 -77.26
REMARK 500 VAL B 893 53.38 -104.69
REMARK 500 ILE B 894 -145.07 -122.62
REMARK 500 GLN B 896 -56.53 -25.84
REMARK 500 LYS B 915 100.48 -51.60
REMARK 500 VAL B 937 -8.55 -55.59
REMARK 500 PRO C 886 -174.63 -61.49
REMARK 500 ILE C 894 -144.67 -124.64
REMARK 500 LYS C 915 108.65 -57.81
REMARK 500 VAL C 937 -5.01 -57.30
REMARK 500 GLN C 983 -71.55 -51.21
REMARK 500 PHE D 885 150.34 157.76
REMARK 500 PRO D 886 -159.92 -103.62
REMARK 500 ASN D 895 100.58 -42.39
REMARK 500 ALA D1052 83.82 -170.61
REMARK 500 TRP D1058 78.19 -115.47
REMARK 500 ASP E 69 32.06 -99.70
REMARK 500 LEU E 79 42.47 -93.86
REMARK 500 GLN E 115 8.49 81.41
REMARK 500 GLU E 120 9.15 80.46
REMARK 500 ASP F 69 30.78 -97.73
REMARK 500 LEU F 79 47.53 -96.93
REMARK 500 GLN F 115 8.10 88.78
REMARK 500 GLU F 120 8.37 83.74
REMARK 500 LEU G 79 48.23 -95.06
REMARK 500 GLN G 115 8.87 89.17
REMARK 500 GLU G 120 7.78 83.73
REMARK 500 LEU H 79 52.07 -98.76
REMARK 500 ASN H 102 -166.82 -160.44
REMARK 500 GLU H 120 8.31 84.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RKE RELATED DB: PDB
REMARK 900 RELATED ID: 1TR2 RELATED DB: PDB
REMARK 900 RELATED ID: 3H2U RELATED DB: PDB
DBREF 3H2V A 879 1066 UNP B4DTM7 B4DTM7_HUMAN 140 327
DBREF 3H2V B 879 1066 UNP B4DTM7 B4DTM7_HUMAN 140 327
DBREF 3H2V C 879 1066 UNP B4DTM7 B4DTM7_HUMAN 140 327
DBREF 3H2V D 879 1066 UNP B4DTM7 B4DTM7_HUMAN 140 327
DBREF 3H2V E 59 130 UNP Q8IY67 RAVR1_HUMAN 59 130
DBREF 3H2V F 59 130 UNP Q8IY67 RAVR1_HUMAN 59 130
DBREF 3H2V G 59 130 UNP Q8IY67 RAVR1_HUMAN 59 130
DBREF 3H2V H 59 130 UNP Q8IY67 RAVR1_HUMAN 59 130
SEQADV 3H2V HIS E 57 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V MET E 58 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V HIS F 57 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V MET F 58 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V HIS G 57 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V MET G 58 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V HIS H 57 UNP Q8IY67 CLONING ARTIFACT
SEQADV 3H2V MET H 58 UNP Q8IY67 CLONING ARTIFACT
SEQRES 1 A 188 GLU GLU LYS ASP GLU GLU PHE PRO GLU GLN LYS ALA GLY
SEQRES 2 A 188 GLU VAL ILE ASN GLN PRO MET MET MET ALA ALA ARG GLN
SEQRES 3 A 188 LEU HIS ASP GLU ALA ARG LYS TRP SER SER LYS GLY ASN
SEQRES 4 A 188 ASP ILE ILE ALA ALA ALA LYS ARG MET ALA LEU LEU MET
SEQRES 5 A 188 ALA GLU MET SER ARG LEU VAL ARG GLY GLY SER GLY THR
SEQRES 6 A 188 LYS ARG ALA LEU ILE GLN CYS ALA LYS ASP ILE ALA LYS
SEQRES 7 A 188 ALA SER ASP GLU VAL THR ARG LEU ALA LYS GLU VAL ALA
SEQRES 8 A 188 LYS GLN CYS THR ASP LYS ARG ILE ARG THR ASN LEU LEU
SEQRES 9 A 188 GLN VAL CYS GLU ARG ILE PRO THR ILE SER THR GLN LEU
SEQRES 10 A 188 LYS ILE LEU SER THR VAL LYS ALA THR MET LEU GLY ARG
SEQRES 11 A 188 THR ASN ILE SER ASP GLU GLU SER GLU GLN ALA THR GLU
SEQRES 12 A 188 MET LEU VAL HIS ASN ALA GLN ASN LEU MET GLN SER VAL
SEQRES 13 A 188 LYS GLU THR VAL ARG GLU ALA GLU ALA ALA SER ILE LYS
SEQRES 14 A 188 ILE ARG THR ASP ALA GLY PHE THR LEU ARG TRP VAL ARG
SEQRES 15 A 188 LYS THR PRO TRP TYR GLN
SEQRES 1 B 188 GLU GLU LYS ASP GLU GLU PHE PRO GLU GLN LYS ALA GLY
SEQRES 2 B 188 GLU VAL ILE ASN GLN PRO MET MET MET ALA ALA ARG GLN
SEQRES 3 B 188 LEU HIS ASP GLU ALA ARG LYS TRP SER SER LYS GLY ASN
SEQRES 4 B 188 ASP ILE ILE ALA ALA ALA LYS ARG MET ALA LEU LEU MET
SEQRES 5 B 188 ALA GLU MET SER ARG LEU VAL ARG GLY GLY SER GLY THR
SEQRES 6 B 188 LYS ARG ALA LEU ILE GLN CYS ALA LYS ASP ILE ALA LYS
SEQRES 7 B 188 ALA SER ASP GLU VAL THR ARG LEU ALA LYS GLU VAL ALA
SEQRES 8 B 188 LYS GLN CYS THR ASP LYS ARG ILE ARG THR ASN LEU LEU
SEQRES 9 B 188 GLN VAL CYS GLU ARG ILE PRO THR ILE SER THR GLN LEU
SEQRES 10 B 188 LYS ILE LEU SER THR VAL LYS ALA THR MET LEU GLY ARG
SEQRES 11 B 188 THR ASN ILE SER ASP GLU GLU SER GLU GLN ALA THR GLU
SEQRES 12 B 188 MET LEU VAL HIS ASN ALA GLN ASN LEU MET GLN SER VAL
SEQRES 13 B 188 LYS GLU THR VAL ARG GLU ALA GLU ALA ALA SER ILE LYS
SEQRES 14 B 188 ILE ARG THR ASP ALA GLY PHE THR LEU ARG TRP VAL ARG
SEQRES 15 B 188 LYS THR PRO TRP TYR GLN
SEQRES 1 C 188 GLU GLU LYS ASP GLU GLU PHE PRO GLU GLN LYS ALA GLY
SEQRES 2 C 188 GLU VAL ILE ASN GLN PRO MET MET MET ALA ALA ARG GLN
SEQRES 3 C 188 LEU HIS ASP GLU ALA ARG LYS TRP SER SER LYS GLY ASN
SEQRES 4 C 188 ASP ILE ILE ALA ALA ALA LYS ARG MET ALA LEU LEU MET
SEQRES 5 C 188 ALA GLU MET SER ARG LEU VAL ARG GLY GLY SER GLY THR
SEQRES 6 C 188 LYS ARG ALA LEU ILE GLN CYS ALA LYS ASP ILE ALA LYS
SEQRES 7 C 188 ALA SER ASP GLU VAL THR ARG LEU ALA LYS GLU VAL ALA
SEQRES 8 C 188 LYS GLN CYS THR ASP LYS ARG ILE ARG THR ASN LEU LEU
SEQRES 9 C 188 GLN VAL CYS GLU ARG ILE PRO THR ILE SER THR GLN LEU
SEQRES 10 C 188 LYS ILE LEU SER THR VAL LYS ALA THR MET LEU GLY ARG
SEQRES 11 C 188 THR ASN ILE SER ASP GLU GLU SER GLU GLN ALA THR GLU
SEQRES 12 C 188 MET LEU VAL HIS ASN ALA GLN ASN LEU MET GLN SER VAL
SEQRES 13 C 188 LYS GLU THR VAL ARG GLU ALA GLU ALA ALA SER ILE LYS
SEQRES 14 C 188 ILE ARG THR ASP ALA GLY PHE THR LEU ARG TRP VAL ARG
SEQRES 15 C 188 LYS THR PRO TRP TYR GLN
SEQRES 1 D 188 GLU GLU LYS ASP GLU GLU PHE PRO GLU GLN LYS ALA GLY
SEQRES 2 D 188 GLU VAL ILE ASN GLN PRO MET MET MET ALA ALA ARG GLN
SEQRES 3 D 188 LEU HIS ASP GLU ALA ARG LYS TRP SER SER LYS GLY ASN
SEQRES 4 D 188 ASP ILE ILE ALA ALA ALA LYS ARG MET ALA LEU LEU MET
SEQRES 5 D 188 ALA GLU MET SER ARG LEU VAL ARG GLY GLY SER GLY THR
SEQRES 6 D 188 LYS ARG ALA LEU ILE GLN CYS ALA LYS ASP ILE ALA LYS
SEQRES 7 D 188 ALA SER ASP GLU VAL THR ARG LEU ALA LYS GLU VAL ALA
SEQRES 8 D 188 LYS GLN CYS THR ASP LYS ARG ILE ARG THR ASN LEU LEU
SEQRES 9 D 188 GLN VAL CYS GLU ARG ILE PRO THR ILE SER THR GLN LEU
SEQRES 10 D 188 LYS ILE LEU SER THR VAL LYS ALA THR MET LEU GLY ARG
SEQRES 11 D 188 THR ASN ILE SER ASP GLU GLU SER GLU GLN ALA THR GLU
SEQRES 12 D 188 MET LEU VAL HIS ASN ALA GLN ASN LEU MET GLN SER VAL
SEQRES 13 D 188 LYS GLU THR VAL ARG GLU ALA GLU ALA ALA SER ILE LYS
SEQRES 14 D 188 ILE ARG THR ASP ALA GLY PHE THR LEU ARG TRP VAL ARG
SEQRES 15 D 188 LYS THR PRO TRP TYR GLN
SEQRES 1 E 74 HIS MET ARG LYS ILE LEU ILE ARG GLY LEU PRO GLY ASP
SEQRES 2 E 74 VAL THR ASN GLN GLU VAL HIS ASP LEU LEU SER ASP TYR
SEQRES 3 E 74 GLU LEU LYS TYR CYS PHE VAL ASP LYS TYR LYS GLY THR
SEQRES 4 E 74 ALA PHE VAL THR LEU LEU ASN GLY GLU GLN ALA GLU ALA
SEQRES 5 E 74 ALA ILE ASN ALA PHE HIS GLN SER ARG LEU ARG GLU ARG
SEQRES 6 E 74 GLU LEU SER VAL GLN LEU GLN PRO THR
SEQRES 1 F 74 HIS MET ARG LYS ILE LEU ILE ARG GLY LEU PRO GLY ASP
SEQRES 2 F 74 VAL THR ASN GLN GLU VAL HIS ASP LEU LEU SER ASP TYR
SEQRES 3 F 74 GLU LEU LYS TYR CYS PHE VAL ASP LYS TYR LYS GLY THR
SEQRES 4 F 74 ALA PHE VAL THR LEU LEU ASN GLY GLU GLN ALA GLU ALA
SEQRES 5 F 74 ALA ILE ASN ALA PHE HIS GLN SER ARG LEU ARG GLU ARG
SEQRES 6 F 74 GLU LEU SER VAL GLN LEU GLN PRO THR
SEQRES 1 G 74 HIS MET ARG LYS ILE LEU ILE ARG GLY LEU PRO GLY ASP
SEQRES 2 G 74 VAL THR ASN GLN GLU VAL HIS ASP LEU LEU SER ASP TYR
SEQRES 3 G 74 GLU LEU LYS TYR CYS PHE VAL ASP LYS TYR LYS GLY THR
SEQRES 4 G 74 ALA PHE VAL THR LEU LEU ASN GLY GLU GLN ALA GLU ALA
SEQRES 5 G 74 ALA ILE ASN ALA PHE HIS GLN SER ARG LEU ARG GLU ARG
SEQRES 6 G 74 GLU LEU SER VAL GLN LEU GLN PRO THR
SEQRES 1 H 74 HIS MET ARG LYS ILE LEU ILE ARG GLY LEU PRO GLY ASP
SEQRES 2 H 74 VAL THR ASN GLN GLU VAL HIS ASP LEU LEU SER ASP TYR
SEQRES 3 H 74 GLU LEU LYS TYR CYS PHE VAL ASP LYS TYR LYS GLY THR
SEQRES 4 H 74 ALA PHE VAL THR LEU LEU ASN GLY GLU GLN ALA GLU ALA
SEQRES 5 H 74 ALA ILE ASN ALA PHE HIS GLN SER ARG LEU ARG GLU ARG
SEQRES 6 H 74 GLU LEU SER VAL GLN LEU GLN PRO THR
FORMUL 9 HOH *4(H2 O)
HELIX 1 1 ASN A 895 ARG A 910 1 16
HELIX 2 2 ASN A 917 VAL A 937 1 21
HELIX 3 3 GLY A 942 CYS A 972 1 31
HELIX 4 4 ASP A 974 LEU A 1006 1 33
HELIX 5 5 SER A 1012 ALA A 1044 1 33
HELIX 6 6 ASN B 895 ARG B 910 1 16
HELIX 7 7 ASN B 917 VAL B 937 1 21
HELIX 8 8 GLY B 942 CYS B 972 1 31
HELIX 9 9 ASP B 974 LEU B 1006 1 33
HELIX 10 10 SER B 1012 ALA B 1044 1 33
HELIX 11 11 ASN C 895 LYS C 911 1 17
HELIX 12 12 ASN C 917 VAL C 937 1 21
HELIX 13 13 GLY C 942 CYS C 972 1 31
HELIX 14 14 ASP C 974 CYS C 985 1 12
HELIX 15 15 GLU C 986 LEU C 1006 1 21
HELIX 16 16 SER C 1012 ALA C 1044 1 33
HELIX 17 17 ASN D 895 ARG D 910 1 16
HELIX 18 18 ASN D 917 VAL D 937 1 21
HELIX 19 19 GLY D 942 CYS D 972 1 31
HELIX 20 20 ASP D 974 LEU D 1006 1 33
HELIX 21 21 SER D 1012 ALA D 1044 1 33
HELIX 22 22 THR E 71 LEU E 79 1 9
HELIX 23 23 ASN E 102 HIS E 114 1 13
HELIX 24 24 THR F 71 LEU F 79 1 9
HELIX 25 25 ASN F 102 HIS F 114 1 13
HELIX 26 26 THR G 71 LEU G 79 1 9
HELIX 27 27 ASN G 102 HIS G 114 1 13
HELIX 28 28 THR H 71 LEU H 79 1 9
HELIX 29 29 ASN H 102 HIS H 114 1 13
SHEET 1 A 4 TYR E 86 ASP E 90 0
SHEET 2 A 4 THR E 95 THR E 99 -1 O THR E 95 N ASP E 90
SHEET 3 A 4 LYS E 60 ARG E 64 -1 N ILE E 63 O ALA E 96
SHEET 4 A 4 SER E 124 LEU E 127 -1 O GLN E 126 N LEU E 62
SHEET 1 B 2 ARG E 117 LEU E 118 0
SHEET 2 B 2 ARG E 121 GLU E 122 -1 O ARG E 121 N LEU E 118
SHEET 1 C 4 LEU F 84 ASP F 90 0
SHEET 2 C 4 THR F 95 LEU F 100 -1 O THR F 95 N ASP F 90
SHEET 3 C 4 LYS F 60 ARG F 64 -1 N ILE F 63 O ALA F 96
SHEET 4 C 4 SER F 124 LEU F 127 -1 O GLN F 126 N LEU F 62
SHEET 1 D 2 ARG F 117 LEU F 118 0
SHEET 2 D 2 ARG F 121 GLU F 122 -1 O ARG F 121 N LEU F 118
SHEET 1 E 4 LEU G 84 ASP G 90 0
SHEET 2 E 4 THR G 95 LEU G 100 -1 O THR G 99 N LYS G 85
SHEET 3 E 4 LYS G 60 ARG G 64 -1 N ILE G 63 O ALA G 96
SHEET 4 E 4 SER G 124 LEU G 127 -1 O GLN G 126 N LEU G 62
SHEET 1 F 2 ARG G 117 LEU G 118 0
SHEET 2 F 2 ARG G 121 GLU G 122 -1 O ARG G 121 N LEU G 118
SHEET 1 G 4 LEU H 84 ASP H 90 0
SHEET 2 G 4 THR H 95 LEU H 100 -1 O THR H 95 N ASP H 90
SHEET 3 G 4 LYS H 60 ARG H 64 -1 N ILE H 63 O ALA H 96
SHEET 4 G 4 SER H 124 LEU H 127 -1 O GLN H 126 N LEU H 62
SHEET 1 H 2 ARG H 117 LEU H 118 0
SHEET 2 H 2 ARG H 121 GLU H 122 -1 O ARG H 121 N LEU H 118
CISPEP 1 SER D 941 GLY D 942 0 -7.77
CISPEP 2 ALA D 1052 GLY D 1053 0 2.25
CRYST1 41.818 70.921 99.342 89.77 90.04 104.04 P 1 4
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 0.023913 0.005980 -0.000007 0.00000
SCALE2 0.000000 0.014534 -0.000058 0.00000
SCALE3 0.000000 0.000000 0.010066 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
