Header list of 2gb1.pdb file
Complete list - 9 202 Bytes
HEADER IMMUNOGLOBULIN BINDING PROTEIN 15-MAY-91 2GB1
TITLE A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF
TITLE 2 STREPTOCOCCAL PROTEIN G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN G;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G';
SOURCE 3 ORGANISM_TAXID: 1320
KEYWDS IMMUNOGLOBULIN BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.M.GRONENBORN,G.M.CLORE
REVDAT 3 09-MAR-22 2GB1 1 REMARK
REVDAT 2 24-FEB-09 2GB1 1 VERSN
REVDAT 1 15-APR-93 2GB1 0
JRNL AUTH A.M.GRONENBORN,D.R.FILPULA,N.Z.ESSIG,A.ACHARI,M.WHITLOW,
JRNL AUTH 2 P.T.WINGFIELD,G.M.CLORE
JRNL TITL A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING
JRNL TITL 2 DOMAIN OF STREPTOCOCCAL PROTEIN G.
JRNL REF SCIENCE V. 253 657 1991
JRNL REFN ISSN 0036-8075
JRNL PMID 1871600
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN THE PAPER CITED ON THE JRNL RECORDS
REMARK 3 ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS,
REMARK 3 DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES
REMARK 3 AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES
REMARK 3 BETWEEN THE CALCULATED STRUCTURES). THE STRUCTURES ARE
REMARK 3 BASED ON 854 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM
REMARK 3 NOE MEASUREMENTS; 60 HYDROGEN-BONDING DISTANCE RESTRAINTS
REMARK 3 FOR 30 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE
REMARK 3 AND AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL
REMARK 3 STRUCTURE CALCULATIONS; AND 54 PHI AND 51 PSI BACKBONE
REMARK 3 TORSION ANGLE RESTRAINTS AND 39 CHI1 SIDE CHAIN TORSION
REMARK 3 ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE
REMARK 3 DATA. THE LATTER ARE OBTAINED USING THE CONFORMATIONAL
REMARK 3 GRID SEARCH PROGRAM STEREOSEARCH [NILGES, M., CLORE, G.M.
REMARK 3 & GRONENBORN, A.M. (1990) BIOPOLYMERS 29, 813-822.
REMARK 3 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID
REMARK 3 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED
REMARK 3 ANNEALING METHOD [NILGES, M., CLORE, G.M. & GRONENBORN,
REMARK 3 A.M. FEBS LETT. 229, 317-324 (1988)].
REMARK 3
REMARK 3 A TOTAL OF 60 STRUCTURES WERE CALCULATED. THE COORDINATES
REMARK 3 OF THE RESTRAINED MINIMIZED STRUCTURE ARE PRESENTED IN
REMARK 3 PROTEIN DATA BANK ENTRY 2GB1. THIS WAS OBTAINED BY
REMARK 3 AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND
REMARK 3 SUBJECTING THE RESULTING COORDINATES TO RESTRAINED
REMARK 3 MINIMIZATION. THE 60 STRUCTURES ARE PRESENTED IN PROTEIN
REMARK 3 DATA BANK ENTRY 1GB1.
REMARK 3
REMARK 3 THE QUANTITY PRESENTED IN THE B VALUE FIELD (COLUMNS 61 -
REMARK 3 66 OF THE ATOM AND HETATM RECORDS BELOW) REPRESENTS THE
REMARK 3 ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE
REMARK 3 MEAN COORDINATE POSITIONS.
REMARK 4
REMARK 4 2GB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178123.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
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: NULL
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 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 TRP A 43 CG TRP A 43 CD2 -0.102
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 LYS A 10 CD - CE - NZ ANGL. DEV. = 19.6 DEGREES
REMARK 500 LYS A 13 CD - CE - NZ ANGL. DEV. = 19.5 DEGREES
REMARK 500 TRP A 43 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 43 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 43 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TRP A 43 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 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 GLU A 15 130.90 -175.48
REMARK 500 ASP A 36 4.51 -66.75
REMARK 500 ASP A 46 77.49 -108.06
REMARK 500 ASP A 47 1.17 -66.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GB1 RELATED DB: PDB
DBREF 2GB1 A 2 56 UNP P06654 SPG1_STRSG 228 282
SEQRES 1 A 56 MET THR TYR LYS LEU ILE LEU ASN GLY LYS THR LEU LYS
SEQRES 2 A 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR ALA
SEQRES 3 A 56 GLU LYS VAL PHE LYS GLN TYR ALA ASN ASP ASN GLY VAL
SEQRES 4 A 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR PHE
SEQRES 5 A 56 THR VAL THR GLU
HELIX 1 1 ASP A 22 ASP A 36 1 15
SHEET 1 A 2 THR A 2 LEU A 7 0
SHEET 2 A 2 GLY A 14 GLU A 19 -1 O GLY A 14 N LEU A 7
SHEET 1 B 2 GLU A 42 ASP A 46 0
SHEET 2 B 2 THR A 51 THR A 55 -1 N THR A 51 O ASP A 46
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 - 9 202 Bytes