Header list of 1gjs.pdb file
Complete list - r 8 2 Bytes
HEADER IMMUNOGLOBULIN-BINDING PROTEIN 02-AUG-01 1GJS
TITLE SOLUTION STRUCTURE OF THE ALBUMIN BINDING DOMAIN OF
TITLE 2 STREPTOCOCCAL PROTEIN G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN G;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALBUMIN-BINDING DOMAIN RESIDUES 254-299;
COMPND 5 SYNONYM: ABD, ALBUMIN-BINDING DOMAIN OF PROTEIN G, IGG
COMPND 6 BINDING PROTEIN G;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP.;
SOURCE 3 ORGANISM_COMMON: GROUP G STREPTOCOCCI;
SOURCE 4 ORGANISM_TAXID: 1306;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IMMUNOGLOBULIN-BINDING PROTEIN, BACTERIAL SURFACE PROTEIN,
KEYWDS 2 ALBUMIN BINDING, PROTEIN G
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.U.JOHANSSON,I.M.FRICK,H.NILSSON,P.J.KRAULIS,S.HOBER,
AUTHOR 2 P.JONASSON,P.A.NYGREN,M.UHLEN,L.BJORCK,T.DRAKENBERG,S.FORSEN,
AUTHOR 3 M.WIKSTROM
REVDAT 6 08-APR-15 1GJS 1 AUTHOR REMARK VERSN
REVDAT 5 24-FEB-09 1GJS 1 VERSN
REVDAT 4 05-APR-05 1GJS 1 REMARK
REVDAT 3 21-MAR-02 1GJS 1 SOURCE
REVDAT 2 15-MAR-02 1GJS 1 JRNL
REVDAT 1 09-AUG-01 1GJS 0
JRNL AUTH M.JOHANSSON,I.FRICK,H.NILSSON,P.KRAULIS,S.HOBER,
JRNL AUTH 2 P.JONASSON,M.LINHULT,P.NYGREN,M.UHLEN,L.BJORCK,
JRNL AUTH 3 T.DRAKENBERG,S.FORSEN,M.WIKSTROM
JRNL TITL STRUCTURE, SPECIFICITY, AND MODE OF INTERACTION
JRNL TITL 2 FOR BACTERIAL ALBUMIN-BINDING MODULES
JRNL REF J.BIOL.CHEM. V. 277 8114 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11751858
JRNL DOI 10.1074/JBC.M109943200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT CAN BE FOUND IN THE JRNL
REMARK 3 CITATION ABOVE.
REMARK 4
REMARK 4 1GJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-AUG-01.
REMARK 100 THE PDBE ID CODE IS EBI-8403.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB, CBCA(CO)NH,
REMARK 210 3D HCC(CO)NH-TOCSY,
REMARK 210 3D CC(CO)NH-TOCSY,
REMARK 210 15N-; 13C EDITED 3D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : UNITY 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND
REMARK 210 RESTRAINED SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED ABD.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 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 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 ALA A 3 -37.85 -160.86
REMARK 500 1 SER A 19 -49.26 -157.86
REMARK 500 1 ALA A 63 12.33 -69.24
REMARK 500 2 VAL A 6 -13.72 -148.47
REMARK 500 2 HIS A 11 97.22 -62.92
REMARK 500 2 ASN A 18 -52.77 -163.70
REMARK 500 2 VAL A 36 30.72 -88.80
REMARK 500 2 ASP A 38 -98.44 -0.61
REMARK 500 3 ILE A 4 -97.59 -110.01
REMARK 500 3 LEU A 7 -41.41 -159.98
REMARK 500 3 ALA A 14 -152.18 -69.20
REMARK 500 4 HIS A 11 10.32 -140.04
REMARK 500 4 GLU A 13 -50.08 -168.51
REMARK 500 5 LEU A 7 -12.20 -168.45
REMARK 500 5 HIS A 11 91.45 -41.89
REMARK 500 5 ASP A 16 -166.45 -174.85
REMARK 500 5 ALA A 17 -108.56 -158.36
REMARK 500 6 ALA A 3 15.56 -168.46
REMARK 500 6 LEU A 7 -47.91 -154.52
REMARK 500 6 ASN A 46 49.14 -97.46
REMARK 500 7 VAL A 6 -9.85 -50.25
REMARK 500 7 ALA A 17 -14.18 -171.88
REMARK 500 9 ALA A 3 -6.36 -164.78
REMARK 500 9 PHE A 5 -119.80 -60.00
REMARK 500 9 LEU A 7 -44.26 -169.37
REMARK 500 9 ALA A 14 -11.57 -161.40
REMARK 500 9 ALA A 17 -35.73 -175.45
REMARK 500 9 ALA A 47 92.49 -47.93
REMARK 500 10 VAL A 6 36.42 -166.48
REMARK 500 10 ASN A 8 64.50 -69.65
REMARK 500 10 ALA A 17 -80.88 -159.96
REMARK 500 10 VAL A 36 -177.97 -69.43
REMARK 500 11 ALA A 3 -35.83 -164.04
REMARK 500 11 ASP A 12 -121.22 -153.39
REMARK 500 11 ASP A 16 84.54 -154.35
REMARK 500 12 PHE A 5 72.15 -64.51
REMARK 500 12 ALA A 9 42.57 -172.48
REMARK 500 12 ASP A 12 19.15 -173.58
REMARK 500 12 ALA A 14 -142.17 -166.38
REMARK 500 12 VAL A 36 -167.33 -57.07
REMARK 500 13 PHE A 5 -38.47 -151.87
REMARK 500 13 VAL A 6 86.18 -162.13
REMARK 500 13 ASN A 8 -26.58 -160.80
REMARK 500 13 ASP A 12 42.94 -69.67
REMARK 500 13 ASP A 38 -107.77 -167.78
REMARK 500 14 ALA A 3 -70.50 -45.21
REMARK 500 14 ALA A 9 -130.33 -161.61
REMARK 500 14 ALA A 14 -5.56 -168.53
REMARK 500 14 ASP A 38 -100.12 -165.33
REMARK 500 15 ALA A 3 159.97 -39.89
REMARK 500 15 VAL A 6 -147.49 -67.17
REMARK 500 16 LEU A 7 72.33 -67.12
REMARK 500 16 ALA A 17 -5.85 -55.38
REMARK 500 17 ALA A 3 112.85 -170.13
REMARK 500 17 ILE A 4 -32.39 -168.12
REMARK 500 17 ASP A 12 -117.76 -170.14
REMARK 500 17 ASP A 16 -118.53 -56.92
REMARK 500 17 ALA A 17 -101.49 -173.59
REMARK 500 17 VAL A 36 -173.50 -66.13
REMARK 500 18 ASP A 12 118.20 -171.05
REMARK 500 18 GLU A 13 -80.03 -140.64
REMARK 500 19 ALA A 3 16.10 -150.69
REMARK 500 19 PHE A 5 155.06 -47.28
REMARK 500 19 HIS A 11 -101.69 -144.04
REMARK 500 19 ALA A 17 -34.12 -149.73
REMARK 500 20 ASN A 8 -121.13 -96.72
REMARK 500 20 ALA A 14 21.74 -153.06
REMARK 500 20 ASN A 18 -79.88 -89.93
REMARK 500 21 ALA A 14 -129.59 -157.11
REMARK 500 22 ASN A 8 2.06 -153.92
REMARK 500 22 ALA A 9 -80.02 -90.67
REMARK 500 22 ALA A 14 -58.72 -140.69
REMARK 500 22 ASN A 18 -79.95 -90.01
REMARK 500 23 ALA A 3 -52.83 -156.48
REMARK 500 23 ALA A 9 -104.24 -90.90
REMARK 500 23 ASP A 16 -138.03 -137.15
REMARK 500 23 ALA A 17 -29.93 -38.40
REMARK 500 24 ASN A 18 -43.74 -134.54
REMARK 500 24 ALA A 63 -25.89 -147.58
REMARK 500 25 VAL A 6 -154.13 -95.96
REMARK 500 25 ASN A 8 20.78 -69.94
REMARK 500 25 ALA A 14 -160.02 -78.60
REMARK 500 26 ILE A 4 -24.82 -170.00
REMARK 500 26 ALA A 9 98.75 -61.01
REMARK 500 26 ASP A 12 -120.05 -115.80
REMARK 500 26 VAL A 36 170.10 -54.73
REMARK 500 27 LEU A 7 -33.11 -151.02
REMARK 500 27 GLU A 13 10.31 -146.50
REMARK 500 27 VAL A 36 -169.21 -68.41
REMARK 500 27 LEU A 56 -70.52 -84.50
REMARK 500 28 ALA A 3 101.78 -175.35
REMARK 500 28 PHE A 5 -11.60 -172.41
REMARK 500 28 ALA A 17 -75.51 -173.20
REMARK 500 28 VAL A 36 -171.70 -63.33
REMARK 500 29 ILE A 4 -141.23 -137.07
REMARK 500 29 ALA A 9 14.11 -164.25
REMARK 500 29 ASN A 18 -51.66 -159.90
REMARK 500 29 SER A 37 -97.92 -45.02
REMARK 500 29 ASP A 38 -47.02 -171.49
REMARK 500 30 ALA A 3 60.80 -67.83
REMARK 500 30 LEU A 7 -108.04 -72.68
REMARK 500 30 ASN A 8 59.90 -101.07
REMARK 500 30 GLN A 10 41.83 -85.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FCC RELATED DB: PDB
REMARK 900
REMARK 900 RELATED ID: 1FCL RELATED DB: PDB
REMARK 900 DELTA1.5: A COMPUTATIONALLY DESIGNED CORE
REMARK 900 VARIANT OF THE B1DOMAIN OF STREPTOCOCCAL
REMARK 900 PROTEIN G
REMARK 900 RELATED ID: 1FD6 RELATED DB: PDB
REMARK 900 DELTA0: A COMPUTATIONALLY DESIGNED CORE
REMARK 900 VARIANT OF THE B1DOMAIN OF STREPTOCOCCAL
REMARK 900 PROTEIN G
REMARK 900 RELATED ID: 1GB4 RELATED DB: PDB
REMARK 900 HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN
REMARK 900 FROMSTREPTOCOCCAL PROTEIN G, NMR, 47
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1GJT RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ALBUMIN BINDING
REMARK 900 DOMAIN OF STREPTOCOCCAL PROTEIN G
REMARK 900 RELATED ID: 1IBX RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF DFF40 AND DFF45 N-
REMARK 900 TERMINAL DOMAIN COMPLEX
REMARK 900 RELATED ID: 1P7E RELATED DB: PDB
REMARK 900 GB3 SOLUTION STRUCTURE OBTAINED BY REFINEMENT
REMARK 900 OF X-RAYSTRUCTURE WITH DIPOLAR COUPLINGS
REMARK 900 RELATED ID: 1P7F RELATED DB: PDB
REMARK 900 GB3 SOLUTION STRUCTURE OBTAINED BY REFINEMENT
REMARK 900 OF X-RAYSTRUCTURE WITH DIPOLAR COUPLINGS
REMARK 900 RELATED ID: 2IGG RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1 TO 19 ARE DERIVED FROM THE CLONING
REMARK 999 CONSTRUCT (KRAULIS ET AL., FEBS LETTERS (1996) 378, 190-194
DBREF 1GJS A 1 19 PDB 1GJS 1GJS 1 19
DBREF 1GJS A 20 65 UNP P19909 SPG2_STRSP 254 299
SEQRES 1 A 65 MET LYS ALA ILE PHE VAL LEU ASN ALA GLN HIS ASP GLU
SEQRES 2 A 65 ALA VAL ASP ALA ASN SER LEU ALA GLU ALA LYS VAL LEU
SEQRES 3 A 65 ALA ASN ARG GLU LEU ASP LYS TYR GLY VAL SER ASP TYR
SEQRES 4 A 65 TYR LYS ASN LEU ILE ASN ASN ALA LYS THR VAL GLU GLY
SEQRES 5 A 65 VAL LYS ALA LEU ILE ASP GLU ILE LEU ALA ALA LEU PRO
HELIX 1 1 SER A 19 TYR A 34 1 16
HELIX 2 2 ASP A 38 ASN A 45 1 8
HELIX 3 3 VAL A 50 ALA A 63 1 14
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 8 2 Bytes