Header list of 2igh.pdb file
Complete list - r 9 2 Bytes
HEADER IMMUNOGLOBULIN-BINDING PROTEIN 26-AUG-92 2IGH
TITLE DETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND III OF
TITLE 2 PROTEIN G FROM STREPTOCOCCUS BY 1H NMR
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. GX7805;
SOURCE 3 ORGANISM_TAXID: 1325
KEYWDS IMMUNOGLOBULIN-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR L.-Y.LIAN,J.P.DERRICK,M.J.SUTCLIFFE,J.C.YANG,G.C.K.ROBERTS
REVDAT 4 09-MAR-22 2IGH 1 REMARK
REVDAT 3 24-FEB-09 2IGH 1 VERSN
REVDAT 2 01-APR-03 2IGH 1 JRNL
REVDAT 1 31-JAN-94 2IGH 0
JRNL AUTH L.Y.LIAN,J.P.DERRICK,M.J.SUTCLIFFE,J.C.YANG,G.C.ROBERTS
JRNL TITL DETERMINATION OF THE SOLUTION STRUCTURES OF DOMAINS II AND
JRNL TITL 2 III OF PROTEIN G FROM STREPTOCOCCUS BY 1H NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE.
JRNL REF J.MOL.BIOL. V. 228 1219 1992
JRNL REFN ISSN 0022-2836
JRNL PMID 1474588
JRNL DOI 10.1016/0022-2836(92)90328-H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IGH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178251.
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 : 24
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: 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: 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 1 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 1 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 1 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 2 TYR A 38 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 2 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 2 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 2 TYR A 50 N - CA - CB ANGL. DEV. = -13.1 DEGREES
REMARK 500 2 TYR A 50 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 2 TYR A 50 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 3 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.5 DEGREES
REMARK 500 3 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 TYR A 8 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 TYR A 8 CB - CG - CD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 4 TRP A 48 CB - CG - CD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 4 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 5 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 6 TRP A 48 CB - CG - CD1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 6 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 6 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 7 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 7 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 7 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 8 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.6 DEGREES
REMARK 500 8 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 8 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 9 TRP A 48 CB - CG - CD1 ANGL. DEV. = -10.6 DEGREES
REMARK 500 9 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 10 TRP A 48 CB - CG - CD1 ANGL. DEV. = -8.7 DEGREES
REMARK 500 10 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 10 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 11 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.0 DEGREES
REMARK 500 11 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 11 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 12 TRP A 48 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 12 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 12 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 13 TRP A 48 CB - CG - CD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 13 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 13 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 14 TRP A 48 CB - CG - CD1 ANGL. DEV. = -10.1 DEGREES
REMARK 500 14 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 14 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 15 TRP A 48 CB - CG - CD1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 15 TRP A 48 CD1 - NE1 - CE2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 16 TRP A 48 CB - CG - CD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 16 TRP A 48 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 77 ANGLE DEVIATIONS.
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 PRO A 3 -71.09 -44.66
REMARK 500 1 ALA A 4 -109.26 -129.87
REMARK 500 1 ASN A 13 49.10 -104.55
REMARK 500 1 LYS A 15 -61.30 -139.43
REMARK 500 1 THR A 54 54.13 114.01
REMARK 500 1 LYS A 55 58.66 7.49
REMARK 500 2 THR A 2 76.07 6.02
REMARK 500 2 PRO A 3 34.44 -79.31
REMARK 500 2 ALA A 4 -70.80 -128.62
REMARK 500 2 LYS A 15 -59.18 -140.56
REMARK 500 2 THR A 49 -143.70 -139.55
REMARK 500 2 ALA A 53 20.60 39.36
REMARK 500 2 THR A 54 -56.57 -152.39
REMARK 500 3 PRO A 3 30.88 -80.11
REMARK 500 3 VAL A 5 82.80 -7.23
REMARK 500 3 LYS A 15 -60.55 -103.77
REMARK 500 3 THR A 16 -49.49 -130.51
REMARK 500 3 LYS A 55 58.88 105.24
REMARK 500 4 PRO A 3 49.76 -85.51
REMARK 500 4 ALA A 4 68.46 -117.98
REMARK 500 4 LYS A 15 -60.57 -144.21
REMARK 500 4 ASP A 45 60.48 -161.71
REMARK 500 4 THR A 49 -157.98 -150.89
REMARK 500 4 ALA A 53 54.43 -114.09
REMARK 500 4 THR A 54 53.81 108.77
REMARK 500 4 LYS A 55 57.73 25.52
REMARK 500 5 ALA A 4 67.46 -111.18
REMARK 500 5 VAL A 5 55.72 -100.77
REMARK 500 5 THR A 6 -159.00 -141.99
REMARK 500 5 THR A 16 -52.91 -122.23
REMARK 500 5 ASP A 45 80.45 128.23
REMARK 500 5 ASP A 52 -44.07 -132.83
REMARK 500 5 ALA A 53 -33.13 112.26
REMARK 500 5 THR A 54 -52.55 -122.63
REMARK 500 5 LYS A 55 45.22 -146.41
REMARK 500 6 THR A 2 71.17 14.38
REMARK 500 6 LYS A 15 -48.13 -175.59
REMARK 500 6 ASP A 45 163.74 145.28
REMARK 500 6 THR A 49 -147.47 -145.20
REMARK 500 6 LYS A 55 54.36 35.34
REMARK 500 7 LYS A 55 57.64 30.46
REMARK 500 8 ASP A 45 87.32 -177.90
REMARK 500 8 LYS A 55 54.29 27.92
REMARK 500 9 ALA A 4 -72.11 -6.65
REMARK 500 9 LYS A 15 -61.80 -147.32
REMARK 500 9 VAL A 26 -63.39 -106.59
REMARK 500 9 LYS A 55 53.65 135.67
REMARK 500 10 ASN A 13 57.84 -118.59
REMARK 500 10 LYS A 18 64.06 -110.22
REMARK 500 10 LYS A 55 53.10 28.08
REMARK 500
REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2IGH A 1 61 UNP P06654 SPG1_STRSG 292 352
SEQRES 1 A 61 LEU THR PRO ALA VAL THR THR TYR LYS LEU VAL ILE ASN
SEQRES 2 A 61 GLY LYS THR LEU LYS GLY GLU THR THR THR LYS ALA VAL
SEQRES 3 A 61 ASP ALA GLU THR ALA GLU LYS ALA PHE LYS GLN TYR ALA
SEQRES 4 A 61 ASN ASP ASN GLY VAL ASP GLY VAL TRP THR TYR ASP ASP
SEQRES 5 A 61 ALA THR LYS THR PHE THR VAL THR GLU
HELIX 1 1 ALA A 28 ASN A 40 1 13
SHEET 1 1 4 GLY A 19 LYS A 24 0
SHEET 2 1 4 THR A 7 ILE A 12 -1
SHEET 3 1 4 THR A 56 THR A 60 1
SHEET 4 1 4 VAL A 47 ASP A 51 -1
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 - r 9 2 Bytes