Header list of 2gi4.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 28-MAR-06 2GI4
TITLE SOLUTION STRUCTURE OF THE LOW MOLECULAR WEIGHT PROTEIN TYROSINE
TITLE 2 PHOSPHATASE FROM CAMPYLOBACTER JEJUNI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POSSIBLE PHOSPHOTYROSINE PROTEIN PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.3.48;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAMPYLOBACTER JEJUNI;
SOURCE 3 ORGANISM_TAXID: 197;
SOURCE 4 STRAIN: 11168;
SOURCE 5 GENE: CJ1258;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: AD202, BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI+
KEYWDS LOW MOLECULAR WEIGHT, PROTEIN TYROSINE PHOSPHATASE, BACTERIAL
KEYWDS 2 PHOSPHATASE, PROKARYOTIC PHOSPHATASE, PHOSPHATASE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.TOLKATCHEV,R.SHAYKHUTDINOV,P.XU,F.NI
REVDAT 4 09-MAR-22 2GI4 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GI4 1 VERSN
REVDAT 2 31-OCT-06 2GI4 1 JRNL
REVDAT 1 18-APR-06 2GI4 0
JRNL AUTH D.TOLKATCHEV,R.SHAYKHUTDINOV,P.XU,J.PLAMONDON,D.C.WATSON,
JRNL AUTH 2 N.M.YOUNG,F.NI
JRNL TITL THREE-DIMENSIONAL STRUCTURE AND LIGAND INTERACTIONS OF THE
JRNL TITL 2 LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE FROM
JRNL TITL 3 CAMPYLOBACTER JEJUNI.
JRNL REF PROTEIN SCI. V. 15 2381 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 17008719
JRNL DOI 10.1110/PS.062279806
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.0
REMARK 3 AUTHORS : A.T.BRUNGER, P.D.ADAMS, G.M.CLORE, W.L.DELANO,
REMARK 3 P.GROS, R.W.GROSSE-KUNSTLEVE, J.-S.JIANG,
REMARK 3 J.KUSZEWSKI, M.NILGES, N.S.PANNU, R.J.READ,
REMARK 3 L.M.RICE, T.SIMONSON, G.L.WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1464 RESTRAINTS, 1152 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 64 DIHEDRAL ANGLE RESTRAINTS, 198 CHEMICAL
REMARK 3 SHIFT-BASED DIHEDRAL ANGLE RESTRAINTS PREDICTED BY TALOS,50
REMARK 3 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 2GI4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037146.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N,13C; 20 MM PHOSPHATE
REMARK 210 BUFFER; PH 5.8; 90% H2O/10% D2O;
REMARK 210 0.2 MM EDTA, AND 0.01% NAN3; 90%
REMARK 210 H2O, 10% D2O; U-15N,13C; 20 MM
REMARK 210 PHOSPHATE BUFFER; PH 5.8; 99.96%
REMARK 210 D2O; 0.2 MM EDTA, AND 0.01% NAN3;
REMARK 210 99.96% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRVIEW 5.0.4, ARIA
REMARK 210 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING USING
REMARK 210 TORSION ANGLE AND CARTESIAN
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 11 17.41 53.96
REMARK 500 1 CYS A 13 -84.88 -151.32
REMARK 500 1 ASN A 30 -57.14 -132.45
REMARK 500 1 GLU A 34 71.19 63.75
REMARK 500 1 HIS A 46 -19.66 -145.77
REMARK 500 1 ASP A 47 102.22 -43.16
REMARK 500 1 GLU A 49 -72.45 -52.18
REMARK 500 1 LEU A 62 -42.18 -155.40
REMARK 500 1 ASN A 63 -164.43 -65.88
REMARK 500 1 HIS A 66 157.70 173.39
REMARK 500 1 LYS A 67 37.94 -169.83
REMARK 500 1 ASN A 68 35.64 -142.71
REMARK 500 1 PHE A 69 97.09 -68.07
REMARK 500 1 THR A 87 -63.27 -107.19
REMARK 500 1 MET A 88 -32.53 77.73
REMARK 500 1 THR A 101 -169.44 -71.83
REMARK 500 1 PHE A 113 -66.00 -90.78
REMARK 500 1 PRO A 115 -87.10 -89.59
REMARK 500 1 ASN A 118 51.53 36.12
REMARK 500 1 ASP A 120 -141.64 -92.07
REMARK 500 1 VAL A 122 136.07 70.72
REMARK 500 1 PRO A 123 -134.62 -67.18
REMARK 500 1 ASP A 124 156.04 67.47
REMARK 500 1 SER A 150 45.42 -83.62
REMARK 500 1 LYS A 151 75.89 54.22
REMARK 500 1 HIS A 153 -164.66 -125.93
REMARK 500 2 ASN A 11 49.36 -79.16
REMARK 500 2 ILE A 12 14.30 -142.09
REMARK 500 2 CYS A 13 -72.52 -151.27
REMARK 500 2 ASN A 30 -57.44 -133.40
REMARK 500 2 GLU A 34 71.30 65.39
REMARK 500 2 GLU A 49 -76.64 -62.04
REMARK 500 2 MET A 51 105.24 -167.88
REMARK 500 2 TYR A 53 176.42 -50.67
REMARK 500 2 LEU A 62 -43.29 -144.75
REMARK 500 2 ASN A 63 -162.63 -67.20
REMARK 500 2 HIS A 66 159.54 176.72
REMARK 500 2 LYS A 67 -176.45 -172.15
REMARK 500 2 THR A 101 -168.16 -67.38
REMARK 500 2 ASN A 102 8.68 -62.81
REMARK 500 2 PRO A 115 -93.83 -57.63
REMARK 500 2 LEU A 117 36.23 -93.96
REMARK 500 2 ASN A 118 92.79 -64.76
REMARK 500 2 ASP A 120 -145.86 -92.59
REMARK 500 2 VAL A 122 133.16 70.15
REMARK 500 2 PRO A 123 -131.95 -72.97
REMARK 500 2 ASP A 124 154.59 66.53
REMARK 500 2 SER A 150 71.87 -156.63
REMARK 500 2 LYS A 151 -7.51 -178.25
REMARK 500 2 HIS A 152 -60.39 -91.33
REMARK 500
REMARK 500 THIS ENTRY HAS 229 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GI4 A 1 151 GB 6968691 CAB73512 1 151
SEQADV 2GI4 HIS A 152 GB 6968691 EXPRESSION TAG
SEQADV 2GI4 HIS A 153 GB 6968691 EXPRESSION TAG
SEQADV 2GI4 HIS A 154 GB 6968691 EXPRESSION TAG
SEQADV 2GI4 HIS A 155 GB 6968691 EXPRESSION TAG
SEQADV 2GI4 HIS A 156 GB 6968691 EXPRESSION TAG
SEQRES 1 A 156 MET LYS LYS ILE LEU PHE ILE CYS LEU GLY ASN ILE CYS
SEQRES 2 A 156 ARG SER PRO MET ALA GLU PHE ILE MET LYS ASP LEU VAL
SEQRES 3 A 156 LYS LYS ALA ASN LEU GLU LYS GLU PHE PHE ILE ASN SER
SEQRES 4 A 156 ALA GLY THR SER GLY GLU HIS ASP GLY GLU GLY MET HIS
SEQRES 5 A 156 TYR GLY THR LYS ASN LYS LEU ALA GLN LEU ASN ILE GLU
SEQRES 6 A 156 HIS LYS ASN PHE THR SER LYS LYS LEU THR GLN LYS LEU
SEQRES 7 A 156 CYS ASP GLU SER ASP PHE LEU ILE THR MET ASP ASN SER
SEQRES 8 A 156 ASN PHE LYS ASN VAL LEU LYS ASN PHE THR ASN THR GLN
SEQRES 9 A 156 ASN LYS VAL LEU LYS ILE THR ASP PHE SER PRO SER LEU
SEQRES 10 A 156 ASN TYR ASP GLU VAL PRO ASP PRO TRP TYR SER GLY ASN
SEQRES 11 A 156 PHE ASP GLU THR TYR LYS ILE LEU SER LEU ALA CYS LYS
SEQRES 12 A 156 ASN LEU LEU VAL PHE LEU SER LYS HIS HIS HIS HIS HIS
HELIX 1 1 CYS A 13 ASN A 30 1 18
HELIX 2 2 HIS A 52 LEU A 62 1 11
HELIX 3 3 THR A 75 ASP A 80 1 6
HELIX 4 4 ASP A 89 PHE A 100 1 12
HELIX 5 5 THR A 101 ASN A 105 5 5
HELIX 6 6 PRO A 123 SER A 128 1 6
HELIX 7 7 PHE A 131 SER A 150 1 20
SHEET 1 A 4 PHE A 36 ALA A 40 0
SHEET 2 A 4 LYS A 3 ILE A 7 1 N PHE A 6 O ASN A 38
SHEET 3 A 4 PHE A 84 ILE A 86 1 O PHE A 84 N LEU A 5
SHEET 4 A 4 VAL A 107 LEU A 108 1 O LEU A 108 N LEU A 85
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