Header list of 3gb1.pdb file
Complete list - v 27 2 Bytes
HEADER IMMUNOGLOBULIN BINDING PROTEIN 02-MAY-99 3GB1
TITLE STRUCTURES OF B1 DOMAIN OF STREPTOCOCCAL PROTEIN G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (B1 DOMAIN OF STREPTOCOCCAL PROTEIN G);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B1 DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G';
SOURCE 3 ORGANISM_TAXID: 1320;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IMMUNOGLOBULIN BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR G.M.CLORE
REVDAT 3 27-NOV-19 3GB1 1 JRNL REMARK
REVDAT 2 24-FEB-09 3GB1 1 VERSN
REVDAT 1 23-JUN-99 3GB1 0
JRNL AUTH K.JUSZEWSKI,A.M.GRONENBORN,G.M.CLORE
JRNL TITL IMPROVING THE PACKING AND ACCURACY OF NMR STRUCTURES WITH A
JRNL TITL 2 PSEUDOPOTENTIAL FOR THE RADIUS OF GYRATION
JRNL REF J.AM.CHEM.SOC. V. 121 2337 1999
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA9843730
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.M.CLORE,M.R.STARICH,A.M.GRONENBORN
REMARK 1 TITL MEASUREMENT OF RESIDUAL DIPOLAR COUPLINGS OF MACROMOLECULES
REMARK 1 TITL 2 ALIGNED IN THE NEMATIC PHASE OF A COLLOIDAL SUSPENSION OF
REMARK 1 TITL 3 ROD-SHAPED VIRUSES.
REMARK 1 REF J.AM.CHEM.SOC. V. 120 10571 1998
REMARK 1 REFN ISSN 0002-7863
REMARK 1 DOI 10.1021/JA982592F
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.M.GRONENBORN,D.R.FILPULA,N.Z.ESSIG,A.ACHARI,M.WHITLOW,
REMARK 1 AUTH 2 P.T.WINGFIELD,G.M.CLORE
REMARK 1 TITL A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING
REMARK 1 TITL 2 DOMAIN OF STREPTOCOCCAL PROTEIN G.
REMARK 1 REF SCIENCE V. 253 657 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 1871600
REMARK 1 DOI 10.1126/SCIENCE.1871600
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS/XPLOR
REMARK 3 AUTHORS : BRUNGER, A., CLORE, G.M. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 INCORPORATES RADIUS OF GYRATION RESTRAINT AND DIPOLAR COUPLINGS
REMARK 3
REMARK 3 A TOTAL OF 31 SIMULATED ANNEALING STRUCTURES WERE CALCULATED
REMARK 3
REMARK 3 THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE LISTED
REMARK 3 FIRST. THIS WAS OBTAINED BY AVERAGING THE COORDINATES OF THE
REMARK 3 INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO
REMARK 3 RESTRAINED MINIMIZATION.
REMARK 3
REMARK 3 IN THE CASE OF THE RESTRAINED MINIMIZED MEAN STRUCTURE
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. FOR THE INDIVIDUAL
REMARK 3 SIMULATED ANNEALING STRUCTURES THE NUMBERS IN THE B-FACTOR C
REMARK 3 NO MEANING
REMARK 3
REMARK 3 ALL THE INTERPROTON DISTANCE, TORSION ANGLE RESTRAINTS 3G
REMARK 3 AND DIPOLAR COUPLING RESTRAINTS
REMARK 3 ARE AVAILABLE FROM THE PROTEIN DATA BANK AS A SEPARATE
REMARK 3 ENTRY. (RMR3GB1)
REMARK 3
REMARK 3 TERMS IN TARGET FUNCTION USED FOR SIMULATED ANNEALING:
REMARK 3 NOE (SUM AVERAGING) AND TORSION ANGLE RESTRAINTS
REMARK 3 3JHNALPHA COUPLING CONSTANT RESTRAINTS (GARRETT ET AL
REMARK 3 J. MAGN. RESON. B104, 99-103 (1994).
REMARK 3 DIPOLAR COUPLING RESTRAINTS USING TWO ALIGNMENT TENSO
REMARK 3 (IN TMV AND IN BICELLES)
REMARK 3 TERM FOR THE RADIUS OF GYRATION (KUSZEWSKI J, GRONENB
REMARK 3 CLORE, GM J AM CHEM SOC 121, 2337-2338 (1999))
REMARK 3 TORSION ANGLE DATABASE POTENTIAL (KUSZEWSKI J, GRONEN
REMARK 3 CLORE GM. PROTEIN SCI 5, 1067-1080 (1996); J. MAGN
REMARK 3 125, 171-177 (1997).
REMARK 3 COVALENT GEOMETRY RESTRAINTS (BONDS, ANGLES, IMPROPER
REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM (NILGES. M,
REMARK 3 GRONENBORN, A.M., BRUNGER, A.T., CLORE, G.M. (1988)
REMARK 3 PROTEIN ENG. 2, 27-38).
REMARK 3
REMARK 3 RESTRAINTS:
REMARK 3 NOES: 138 SEQUENTIAL, 133 MEDIUM, 279 LONG RANGE IN
REMARK 3 185 INTRARESIDUE
REMARK 3 TORSION ANGLES: 145
REMARK 3 3JHNALPHA COUPLINGS: 53
REMARK 3 DIPOLAR COUPLINGS: 152 IN TMV AND 148 IN BICELLES
REMARK 3 (NH, N-C AND HN-C)
REMARK 3 THE B-FACTOR COLUMN GIVES THE AVERAGE RMS OF THE 31
REMARK 3 SIMULATED AN
REMARK 3 STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS
REMARK 3 FILENAME=G_TMV_BICE_RGYR_AVE.MIN
REMARK 3 ============================================================
REMARK 3
REMARK 3 BONDS,ANGLES,IMPROPERS,CDIH,NOE,COUP
REMARK 3
REMARK 3 162664E-03,0.47617,0.436105,0,1.84255E-02,0.534352
REMARK 3 ============================================================
REMARK 4
REMARK 4 3GB1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000000953.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D HOMO AND HETERONUCLEAR; 3D
REMARK 210 QUNATITATIVE J CORRELATION
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS/XPLOR MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 32
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINED MINIMIZATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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
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 1 ASN A 8 59.78 -111.59
REMARK 500 2 ASN A 8 68.59 -114.66
REMARK 500 3 ASN A 8 68.73 -116.34
REMARK 500 4 ASN A 8 69.00 -112.10
REMARK 500 4 ASP A 40 -98.62 -112.30
REMARK 500 5 ASN A 8 68.52 -118.75
REMARK 500 5 ASP A 40 -97.15 -111.68
REMARK 500 7 ASN A 8 69.05 -114.54
REMARK 500 8 ASN A 8 70.63 -113.37
REMARK 500 9 ASN A 8 67.04 -115.27
REMARK 500 9 ASP A 40 -98.63 -110.86
REMARK 500 10 ASN A 8 67.76 -116.49
REMARK 500 10 ASP A 40 -99.74 -110.02
REMARK 500 11 ASN A 8 70.83 -116.95
REMARK 500 12 ASN A 8 71.39 -113.60
REMARK 500 13 ASN A 8 68.74 -111.97
REMARK 500 15 ASN A 8 71.99 -114.88
REMARK 500 15 ASP A 40 -99.88 -110.19
REMARK 500 16 ASN A 8 67.63 -117.13
REMARK 500 17 ASN A 8 72.80 -116.59
REMARK 500 17 ASP A 40 -98.49 -110.52
REMARK 500 18 ASN A 8 72.32 -114.33
REMARK 500 18 ASP A 40 -96.59 -111.68
REMARK 500 19 ASN A 8 71.22 -117.01
REMARK 500 20 ASN A 8 71.35 -114.88
REMARK 500 21 ASN A 8 71.15 -113.71
REMARK 500 21 ASP A 40 -96.20 -111.65
REMARK 500 23 ASN A 8 72.37 -118.75
REMARK 500 23 ASP A 40 -98.74 -110.62
REMARK 500 24 ASN A 8 70.15 -117.57
REMARK 500 25 ASN A 8 72.46 -113.50
REMARK 500 25 ASP A 40 -99.82 -109.99
REMARK 500 26 ASN A 8 71.42 -114.87
REMARK 500 28 ASN A 8 69.38 -116.96
REMARK 500 29 ASN A 8 71.12 -113.67
REMARK 500 29 ASP A 40 -95.03 -111.61
REMARK 500 30 ASN A 8 68.33 -114.07
REMARK 500 31 ASN A 8 71.55 -112.50
REMARK 500 32 ASN A 8 68.52 -114.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3GB1 A 1 56 PDB 3GB1 3GB1 1 56
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 ASN A 37 1 16
SHEET 1 A 4 LYS A 13 GLU A 19 0
SHEET 2 A 4 THR A 2 ASN A 8 -1 N TYR A 3 O THR A 18
SHEET 3 A 4 THR A 51 THR A 55 1 N PHE A 52 O LYS A 4
SHEET 4 A 4 GLU A 42 ASP A 46 -1 N GLU A 42 O THR A 55
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
MODEL 1
Complete list - v 27 2 Bytes