HEADER METAL BINDING PROTEIN 27-MAR-00 1C7W
TITLE NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-
TITLE 2 S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM VECTOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 81-161);
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 TISSUE: MUSCLE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS EF-HAND FAMILY, CALCIUM BINDING PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR I.THERET,S.BALADI,J.A.COX,H.SAKAMOTO,C.T.CRAESCU
REVDAT 5 27-DEC-23 1C7W 1 REMARK
REVDAT 4 16-FEB-22 1C7W 1 REMARK
REVDAT 3 24-FEB-09 1C7W 1 VERSN
REVDAT 2 27-SEP-00 1C7W 1 JRNL
REVDAT 1 12-APR-00 1C7W 0
JRNL AUTH I.THERET,S.BALADI,J.A.COX,H.SAKAMOTO,C.T.CRAESCU
JRNL TITL SEQUENTIAL CALCIUM BINDING TO THE REGULATORY DOMAIN OF
JRNL TITL 2 CALCIUM VECTOR PROTEIN REVEALS FUNCTIONAL ASYMMETRY AND A
JRNL TITL 3 NOVEL MODE OF STRUCTURAL REARRANGEMENT.
JRNL REF BIOCHEMISTRY V. 39 7920 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10891072
JRNL DOI 10.1021/BI000360Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, FELIX 97.0
REMARK 3 AUTHORS : MSI (SAN DIEGO) (FELIX), MSI (SAN DIEGO) (FELIX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 938 NOE
REMARK 3 RESTRAINTS, 66 HYDROGEN BOND RESTRAINTS AND 99 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1C7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000001445.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : UNLABELED; UNIFORMLY 15N LABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D (1H-15N)NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY (DGII) AND
REMARK 210 SIMULATED ANNEALING (DISCOVER)
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: THIS STRUCTURE WAS DETERMINED USING 2D, HOMONUCLEAR AND 3D
REMARK 210 HETERONUCLEAR EXPERIMENTS.
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 TRP A 81
REMARK 465 VAL A 82
REMARK 465 ARG A 83
REMARK 465 GLN A 84
REMARK 465 ASP A 85
REMARK 465 ASP A 86
REMARK 465 LYS A 155
REMARK 465 ASN A 156
REMARK 465 ALA A 157
REMARK 465 LEU A 158
REMARK 465 LYS A 159
REMARK 465 GLU A 160
REMARK 465 SER A 161
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 O GLU A 88 H GLU A 89 0.70
REMARK 500 C GLU A 88 H GLU A 89 1.19
REMARK 500 OD1 ASP A 108 HZ1 LYS A 111 1.58
REMARK 500 OE2 GLU A 87 HZ3 LYS A 95 1.59
REMARK 500 O GLU A 88 N GLU A 89 1.65
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 GLU A 88 O - C - N ANGL. DEV. = -41.8 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 MET A 114 CA - CB - CG ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLN A 115 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 LYS A 116 N - CA - CB ANGL. DEV. = -16.6 DEGREES
REMARK 500 PRO A 121 N - CA - CB ANGL. DEV. = -9.5 DEGREES
REMARK 500 PRO A 121 N - CD - CG ANGL. DEV. = -9.8 DEGREES
REMARK 500 LEU A 122 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU A 122 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 VAL A 127 CA - CB - CG1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 MET A 148 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 LEU A 150 CA - CB - CG ANGL. DEV. = 18.6 DEGREES
REMARK 500 LEU A 150 CB - CG - CD2 ANGL. DEV. = 10.7 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 ASP A 98 103.66 -52.96
REMARK 500 GLN A 115 -26.67 -151.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU A 88 -48.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C7V RELATED DB: PDB
REMARK 900 ENSEMBLE OF 20 STRUCTURES
DBREF 1C7W A 81 161 UNP P04573 CAVP_BRALA 81 161
SEQRES 1 A 81 TRP VAL ARG GLN ASP ASP GLU GLU GLU ILE LEU ARG ALA
SEQRES 2 A 81 PHE LYS VAL PHE ASP ALA ASN GLY ASP GLY VAL ILE ASP
SEQRES 3 A 81 PHE ASP GLU PHE LYS PHE ILE MET GLN LYS VAL GLY GLU
SEQRES 4 A 81 GLU PRO LEU THR ASP ALA GLU VAL GLU GLU ALA MET LYS
SEQRES 5 A 81 GLU ALA ASP GLU ASP GLY ASN GLY VAL ILE ASP ILE PRO
SEQRES 6 A 81 GLU PHE MET ASP LEU ILE LYS LYS SER LYS ASN ALA LEU
SEQRES 7 A 81 LYS GLU SER
HELIX 1 1 GLU A 87 ASP A 98 1 12
HELIX 2 2 PHE A 107 MET A 114 1 8
HELIX 3 3 THR A 123 ASP A 135 1 13
HELIX 4 4 ILE A 144 LYS A 153 1 10
SHEET 1 A 2 VAL A 104 ASP A 106 0
SHEET 2 A 2 VAL A 141 ASP A 143 -1 O ILE A 142 N ILE A 105
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
(ATOM LINES ARE NOT SHOWN.)
END
