Header list of 1j7r.pdb file
Complete list - 23 20 Bytes
HEADER METAL BINDING PROTEIN 18-MAY-01 1J7R
TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE DEFUNCT EF-HAND DOMAIN
TITLE 2 OF CALCIUM VECTOR PROTEIN
CAVEAT 1J7R CHIRALITY ERROR AT CB CENTER OF THR 76.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM VECTOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-86);
COMPND 5 SYNONYM: CAVP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRANCHIOSTOMA LANCEOLATUM;
SOURCE 3 ORGANISM_COMMON: AMPHIOXUS;
SOURCE 4 ORGANISM_TAXID: 7740;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS EF-HAND, CALCIUM BINDING PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR I.THERET,S.BALADI,J.A.COX,J.GALLAY,H.SAKAMOTO,C.T.CRAESCU
REVDAT 4 23-FEB-22 1J7R 1 REMARK
REVDAT 3 24-FEB-09 1J7R 1 VERSN
REVDAT 2 28-DEC-01 1J7R 1 JRNL
REVDAT 1 06-JUN-01 1J7R 0
JRNL AUTH I.THERET,S.BALADI,J.A.COX,J.GALLAY,H.SAKAMOTO,C.T.CRAESCU
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE DEFUNCT
JRNL TITL 2 DOMAIN OF CALCIUM VECTOR PROTEIN.
JRNL REF BIOCHEMISTRY V. 40 13888 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11705378
JRNL DOI 10.1021/BI011444Q
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, DISCOVER
REMARK 3 AUTHORS : MSI (FELIX), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J7R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013465.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM N-CAVP UNLABELED, 20 MM
REMARK 210 DEUTERATED TRIS BUFFER, 100 MM
REMARK 210 KCL; 1.5 MM N-CAVP UNIFORMLY 15N
REMARK 210 LABELED, 20 MM DEUTERATED TRIS
REMARK 210 BUFFER, 100 MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97.0, DGII 97.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: RESIDUES LISTED IN REMARK 465 ARE MISSING DUE TO LACK OF
REMARK 210 NMR CONTSRAINTS.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 ALA A 2
REMARK 465 PRO A 3
REMARK 465 LYS A 4
REMARK 465 ALA A 5
REMARK 465 ARG A 6
REMARK 465 ALA A 7
REMARK 465 ASP A 85
REMARK 465 ASP A 86
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 OE2 GLU A 12 HH TYR A 47 1.56
REMARK 500 O MET A 39 H LEU A 43 1.59
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 TRP A 74 CB - CG - CD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 TRP A 74 CB - CG - CD1 ANGL. DEV. = -9.5 DEGREES
REMARK 500 TRP A 74 NE1 - CE2 - CZ2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 TRP A 74 CG - CD2 - CE3 ANGL. DEV. = -12.9 DEGREES
REMARK 500 TRP A 81 NE1 - CE2 - CZ2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 TRP A 81 CG - CD2 - CE3 ANGL. DEV. = -11.7 DEGREES
REMARK 500 GLN A 84 N - CA - C ANGL. DEV. = -57.5 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 25 -57.80 87.69
REMARK 500 ASN A 26 -51.72 167.70
REMARK 500 ALA A 27 79.81 -153.03
REMARK 500 GLU A 28 -44.44 -133.72
REMARK 500 MET A 39 -74.08 -66.99
REMARK 500 LEU A 40 0.06 -68.84
REMARK 500 GLN A 45 -57.46 -178.03
REMARK 500 TYR A 47 -103.30 -111.40
REMARK 500 THR A 48 -96.27 -83.31
REMARK 500 LYS A 49 -68.04 -165.05
REMARK 500 ARG A 60 -87.29 -50.11
REMARK 500 LYS A 66 55.54 -144.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 20 0.26 SIDE CHAIN
REMARK 500 ARG A 25 0.20 SIDE CHAIN
REMARK 500 TYR A 47 0.10 SIDE CHAIN
REMARK 500 ARG A 50 0.12 SIDE CHAIN
REMARK 500 ARG A 60 0.21 SIDE CHAIN
REMARK 500 ARG A 83 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1J7R A 1 86 UNP P04573 CAVP_BRALA 1 86
SEQRES 1 A 86 ALA ALA PRO LYS ALA ARG ALA LEU GLY PRO GLU GLU LYS
SEQRES 2 A 86 ASP GLU CYS MET LYS ILE PHE ASP ILE PHE ASP ARG ASN
SEQRES 3 A 86 ALA GLU ASN ILE ALA PRO VAL SER ASP THR MET ASP MET
SEQRES 4 A 86 LEU THR LYS LEU GLY GLN THR TYR THR LYS ARG GLU THR
SEQRES 5 A 86 GLU ALA ILE MET LYS GLU ALA ARG GLY PRO LYS GLY ASP
SEQRES 6 A 86 LYS LYS ASN ILE GLY PRO GLU GLU TRP LEU THR LEU CYS
SEQRES 7 A 86 SER LYS TRP VAL ARG GLN ASP ASP
HELIX 1 1 LEU A 8 PRO A 10 5 3
HELIX 2 2 GLU A 11 PHE A 23 1 13
HELIX 3 3 PRO A 32 LEU A 43 1 12
HELIX 4 4 ARG A 50 ALA A 59 1 10
HELIX 5 5 GLU A 72 ARG A 83 1 12
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 23 20 Bytes