Header list of 1xgb.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 18-JAN-98 1XGB
TITLE ALPHA CONOTOXIN GI: 2-13;3-7 DISULFIDE BOND ISOMER NMR, 24 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-CONOTOXIN GI;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GI(2-13,3-7);
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: AMIDATED C-TERMINUS
SOURCE MOL_ID: 1
KEYWDS ALPHA-CONOTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR, DISULFIDE BOND
KEYWDS 2 ISOMERS, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR J.GEHRMANN,P.F.ALEWOOD,D.J.CRAIK
REVDAT 3 02-MAR-22 1XGB 1 REMARK LINK
REVDAT 2 24-FEB-09 1XGB 1 VERSN
REVDAT 1 16-FEB-99 1XGB 0
JRNL AUTH J.GEHRMANN,P.F.ALEWOOD,D.J.CRAIK
JRNL TITL STRUCTURE DETERMINATION OF THE THREE DISULFIDE BOND ISOMERS
JRNL TITL 2 OF ALPHA-CONOTOXIN GI: A MODEL FOR THE ROLE OF DISULFIDE
JRNL TITL 3 BONDS IN STRUCTURAL STABILITY.
JRNL REF J.MOL.BIOL. V. 278 401 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9571060
JRNL DOI 10.1006/JMBI.1998.1701
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XGB 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_1000177257.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; NOESY; DQF-COSY; HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : ARX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : 24 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 300MS NOESY EXPERIMENTS
REMARK 210 ON A 5MM SAMPLE OF GI(2-13;3-7).
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 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 7 CYS A 13 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 8 CYS A 13 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 9 CYS A 13 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 11 CYS A 13 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 15 CYS A 13 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 16 CYS A 13 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 21 CYS A 13 CA - CB - SG ANGL. DEV. = 9.6 DEGREES
REMARK 500 24 CYS A 13 CA - CB - SG ANGL. DEV. = 8.1 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 1 CYS A 2 101.85 -49.65
REMARK 500 1 CYS A 3 55.86 36.87
REMARK 500 1 ALA A 6 69.47 -160.60
REMARK 500 1 HIS A 10 71.40 54.14
REMARK 500 2 CYS A 2 85.25 59.90
REMARK 500 2 CYS A 3 71.10 37.38
REMARK 500 2 ALA A 6 78.68 -164.80
REMARK 500 3 ALA A 6 57.31 -159.93
REMARK 500 4 CYS A 2 100.75 61.49
REMARK 500 4 CYS A 3 60.89 26.68
REMARK 500 4 ALA A 6 58.09 -162.69
REMARK 500 5 CYS A 3 59.80 -142.08
REMARK 500 5 ALA A 6 57.88 -160.69
REMARK 500 5 CYS A 7 29.09 49.90
REMARK 500 6 CYS A 3 56.05 -141.65
REMARK 500 6 ALA A 6 59.42 -161.00
REMARK 500 7 CYS A 2 109.19 -165.37
REMARK 500 7 ALA A 6 57.99 -160.95
REMARK 500 8 CYS A 2 109.19 -165.37
REMARK 500 8 ALA A 6 57.99 -160.95
REMARK 500 9 CYS A 2 102.23 -166.31
REMARK 500 9 ALA A 6 59.65 -163.79
REMARK 500 9 CYS A 7 46.27 39.49
REMARK 500 10 CYS A 3 67.64 8.81
REMARK 500 10 ALA A 6 60.11 -162.47
REMARK 500 10 HIS A 10 82.92 59.07
REMARK 500 11 ALA A 6 66.07 -156.82
REMARK 500 11 CYS A 7 29.54 48.34
REMARK 500 11 HIS A 10 85.67 58.68
REMARK 500 12 CYS A 2 85.83 58.48
REMARK 500 12 CYS A 3 59.15 21.87
REMARK 500 12 ALA A 6 57.32 -163.98
REMARK 500 13 CYS A 2 96.25 65.64
REMARK 500 13 CYS A 3 52.15 29.24
REMARK 500 13 ALA A 6 109.08 -169.08
REMARK 500 13 CYS A 7 -60.56 -0.01
REMARK 500 13 HIS A 10 77.49 58.00
REMARK 500 14 CYS A 3 54.24 34.75
REMARK 500 14 ALA A 6 54.84 -164.02
REMARK 500 15 CYS A 2 94.87 57.11
REMARK 500 15 CYS A 3 60.52 36.48
REMARK 500 15 ALA A 6 53.88 -162.92
REMARK 500 15 HIS A 10 77.09 58.64
REMARK 500 16 CYS A 3 72.56 43.17
REMARK 500 16 ALA A 6 72.52 -163.07
REMARK 500 16 HIS A 10 52.86 146.46
REMARK 500 17 CYS A 3 58.74 -141.74
REMARK 500 17 ALA A 6 62.53 -158.50
REMARK 500 17 CYS A 7 26.66 49.29
REMARK 500 17 HIS A 10 73.77 58.47
REMARK 500
REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 14
DBREF 1XGB A 1 13 UNP P01519 CXAA_CONGE 1 13
SEQRES 1 A 14 GLU CYS CYS ASN PRO ALA CYS GLY ARG HIS TYR SER CYS
SEQRES 2 A 14 NH2
HET NH2 A 14 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 2 CYS A 13 1555 1555 2.02
SSBOND 2 CYS A 3 CYS A 7 1555 1555 2.02
LINK C CYS A 13 N NH2 A 14 1555 1555 1.31
CISPEP 1 ASN A 4 PRO A 5 1 2.65
CISPEP 2 ASN A 4 PRO A 5 2 0.16
CISPEP 3 ASN A 4 PRO A 5 3 10.45
CISPEP 4 ASN A 4 PRO A 5 4 6.14
CISPEP 5 ASN A 4 PRO A 5 5 9.73
CISPEP 6 ASN A 4 PRO A 5 6 10.47
CISPEP 7 ASN A 4 PRO A 5 7 7.07
CISPEP 8 ASN A 4 PRO A 5 8 7.07
CISPEP 9 ASN A 4 PRO A 5 9 3.64
CISPEP 10 ASN A 4 PRO A 5 10 8.60
CISPEP 11 ASN A 4 PRO A 5 11 8.57
CISPEP 12 ASN A 4 PRO A 5 12 4.90
CISPEP 13 ASN A 4 PRO A 5 13 -8.33
CISPEP 14 ASN A 4 PRO A 5 14 2.88
CISPEP 15 ASN A 4 PRO A 5 15 3.32
CISPEP 16 ASN A 4 PRO A 5 16 -10.68
CISPEP 17 ASN A 4 PRO A 5 17 11.92
CISPEP 18 ASN A 4 PRO A 5 18 5.31
CISPEP 19 ASN A 4 PRO A 5 19 9.43
CISPEP 20 ASN A 4 PRO A 5 20 -2.16
CISPEP 21 ASN A 4 PRO A 5 21 7.64
CISPEP 22 ASN A 4 PRO A 5 22 5.77
CISPEP 23 ASN A 4 PRO A 5 23 10.07
CISPEP 24 ASN A 4 PRO A 5 24 5.04
SITE 1 AC1 1 CYS A 13
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 - 2 20 Bytes