Header list of 1gpx.pdb file
Complete list - r 14 2 Bytes
HEADER ELECTRON TRANSPORT 10-JUN-98 1GPX TITLE C85S GAPDX, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PUTIDAREDOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: C85S GAPDX; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: COORDINATION OF GA+3 BY SG OF CYS 39, CYS 45, CYS 48 COMPND 8 AND CYS 86 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA; SOURCE 3 ORGANISM_TAXID: 303; SOURCE 4 GENE: CAMB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKM536; SOURCE 8 OTHER_DETAILS: FROM P. PUTIDA CAMPHOR HYDROXYLASE SYSTEM KEYWDS ELECTRON TRANSPORT, GAPDX C85S, 20 STRUCTURES ALIGNED AND SA EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.C.POCHAPSKY,M.KUTI,S.KAZANIS REVDAT 5 14-MAR-18 1GPX 1 SEQADV REVDAT 4 29-NOV-17 1GPX 1 REMARK HELIX REVDAT 3 24-FEB-09 1GPX 1 VERSN REVDAT 2 16-FEB-99 1GPX 1 SOURCE COMPND REMARK TITLE REVDAT 2 2 1 FORMUL JRNL KEYWDS HEADER REVDAT 1 27-JAN-99 1GPX 0 JRNL AUTH T.C.POCHAPSKY,M.KUTI,S.KAZANIS JRNL TITL THE SOLUTION STRUCTURE OF A GALLIUM-SUBSTITUTED JRNL TITL 2 PUTIDAREDOXIN MUTANT: GAPDX C85S. JRNL REF J.BIOMOL.NMR V. 12 407 1998 JRNL REFN ISSN 0925-2738 JRNL PMID 9835048 JRNL DOI 10.1023/A:1008354113765 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.KAZANIS,T.C.POCHAPSKY REMARK 1 TITL STRUCTURAL FEATURES OF THE METAL BINDING SITE AND DYNAMICS REMARK 1 TITL 2 OF GALLIUM PUTIDAREDOXIN, A DIAMAGNETIC DERIVATIVE OF A REMARK 1 TITL 3 CYS4FE2S2 FERREDOXIN REMARK 1 REF J.BIOMOL.NMR V. 9 337 1997 REMARK 1 REFN ISSN 0925-2738 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.KAZANIS,T.C.POCHAPSKY,T.M.BARNHART,J.E.PENNER-HAHN, REMARK 1 AUTH 2 U.A.MIRZA,B.T.CHAIT REMARK 1 TITL CONVERSION OF A FE2S2 FERREDOXIN INTO A GA+3 RUBREDOXIN REMARK 1 REF J.AM.CHEM.SOC. V. 117 6625 1995 REMARK 1 REFN ISSN 0002-7863 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.85 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS IN PRIMARY REFERENCE REMARK 4 REMARK 4 1GPX 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_1000173666. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 0.01M REMARK 210 PRESSURE : 1 ATMOSPHERE REMARK 210 SAMPLE CONTENTS : 90/10 H2O/D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HOMO; HETERONUCLEAR NMR 2D; 3D REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX500; DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.85 REMARK 210 METHOD USED : DG, SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: TRIPLE-RESONANCE 13C,15N NMR SPECTROSCOPY 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 O LEU A 84 HE21 GLN A 87 1.23 REMARK 500 O MET A 24 H VAL A 28 1.32 REMARK 500 H TYR A 51 O ASP A 100 1.43 REMARK 500 SD MET A 24 SG CYS A 86 1.47 REMARK 500 O VAL A 4 H VAL A 99 1.48 REMARK 500 H TYR A 5 O ARG A 13 1.50 REMARK 500 H2 SER A 1 O VAL A 17 1.52 REMARK 500 O VAL A 28 H GLY A 31 1.52 REMARK 500 O ASN A 64 H GLU A 67 1.54 REMARK 500 H LYS A 79 OG SER A 82 1.57 REMARK 500 H SER A 7 O THR A 11 1.57 REMARK 500 O LEU A 84 NE2 GLN A 87 2.04 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 TYR A 33 61.21 -111.21 REMARK 500 1 ASP A 34 48.85 -78.53 REMARK 500 1 ILE A 35 -141.33 -83.43 REMARK 500 1 VAL A 36 -158.07 -93.18 REMARK 500 1 ASP A 38 -69.18 -120.16 REMARK 500 1 GLU A 54 -24.47 -36.69 REMARK 500 1 VAL A 60 162.92 -39.73 REMARK 500 1 ILE A 68 -61.76 -91.78 REMARK 500 1 THR A 75 85.25 -48.76 REMARK 500 1 GLU A 77 52.55 39.23 REMARK 500 1 LEU A 78 119.79 -19.79 REMARK 500 1 SER A 82 153.35 -48.97 REMARK 500 1 SER A 85 -22.11 -39.58 REMARK 500 1 ARG A 104 -18.64 -49.47 REMARK 500 2 ALA A 18 -133.73 -116.01 REMARK 500 2 VAL A 28 -60.03 -29.97 REMARK 500 2 TYR A 33 60.58 -109.14 REMARK 500 2 SER A 42 -0.80 -140.12 REMARK 500 2 ALA A 43 57.22 77.57 REMARK 500 2 CYS A 48 32.42 -84.24 REMARK 500 2 ASN A 53 -157.52 -59.23 REMARK 500 2 ASN A 64 -156.41 -100.33 REMARK 500 2 CYS A 73 -81.18 -48.79 REMARK 500 2 THR A 75 85.18 -49.11 REMARK 500 2 ALA A 76 48.41 -104.54 REMARK 500 2 GLU A 77 60.73 39.30 REMARK 500 2 LEU A 78 147.38 -30.28 REMARK 500 2 CYS A 86 40.31 -102.38 REMARK 500 2 LEU A 94 54.91 -97.00 REMARK 500 2 ASP A 103 77.07 -110.58 REMARK 500 2 ARG A 104 -77.41 -70.38 REMARK 500 3 SER A 7 -152.56 -79.56 REMARK 500 3 ALA A 18 -159.07 -123.43 REMARK 500 3 SER A 22 -169.72 -118.47 REMARK 500 3 MET A 24 -65.86 -90.90 REMARK 500 3 GLN A 25 -26.42 -39.32 REMARK 500 3 TYR A 33 101.35 -161.72 REMARK 500 3 ALA A 43 55.43 75.51 REMARK 500 3 GLU A 54 -27.89 -36.79 REMARK 500 3 GLU A 67 10.71 -65.55 REMARK 500 3 THR A 75 97.06 -48.53 REMARK 500 3 GLU A 77 60.45 39.67 REMARK 500 3 LEU A 78 144.22 -29.87 REMARK 500 3 SER A 82 165.64 -49.12 REMARK 500 3 CYS A 86 43.78 -108.32 REMARK 500 3 LEU A 94 52.94 -94.14 REMARK 500 3 PRO A 102 80.99 -69.62 REMARK 500 3 ARG A 104 -172.63 -56.41 REMARK 500 4 ALA A 18 -149.95 -126.09 REMARK 500 4 MET A 24 -72.20 -84.22 REMARK 500 REMARK 500 THIS ENTRY HAS 313 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 12 0.21 SIDE CHAIN REMARK 500 1 ARG A 13 0.24 SIDE CHAIN REMARK 500 1 ARG A 66 0.22 SIDE CHAIN REMARK 500 1 ARG A 83 0.29 SIDE CHAIN REMARK 500 1 ARG A 104 0.29 SIDE CHAIN REMARK 500 2 ARG A 12 0.21 SIDE CHAIN REMARK 500 2 ARG A 13 0.17 SIDE CHAIN REMARK 500 2 ARG A 66 0.14 SIDE CHAIN REMARK 500 2 ARG A 83 0.31 SIDE CHAIN REMARK 500 2 ARG A 104 0.18 SIDE CHAIN REMARK 500 3 ARG A 12 0.20 SIDE CHAIN REMARK 500 3 ARG A 13 0.19 SIDE CHAIN REMARK 500 3 ARG A 66 0.10 SIDE CHAIN REMARK 500 3 ARG A 83 0.28 SIDE CHAIN REMARK 500 3 ARG A 104 0.30 SIDE CHAIN REMARK 500 4 ARG A 12 0.28 SIDE CHAIN REMARK 500 4 ARG A 13 0.18 SIDE CHAIN REMARK 500 4 ARG A 66 0.26 SIDE CHAIN REMARK 500 4 ARG A 83 0.10 SIDE CHAIN REMARK 500 4 ARG A 104 0.18 SIDE CHAIN REMARK 500 5 ARG A 12 0.31 SIDE CHAIN REMARK 500 5 ARG A 13 0.31 SIDE CHAIN REMARK 500 5 ARG A 66 0.22 SIDE CHAIN REMARK 500 5 ARG A 83 0.27 SIDE CHAIN REMARK 500 5 ARG A 104 0.31 SIDE CHAIN REMARK 500 6 ARG A 12 0.22 SIDE CHAIN REMARK 500 6 ARG A 13 0.21 SIDE CHAIN REMARK 500 6 ARG A 66 0.29 SIDE CHAIN REMARK 500 6 ARG A 83 0.20 SIDE CHAIN REMARK 500 6 ARG A 104 0.27 SIDE CHAIN REMARK 500 7 ARG A 12 0.27 SIDE CHAIN REMARK 500 7 ARG A 13 0.30 SIDE CHAIN REMARK 500 7 ARG A 66 0.28 SIDE CHAIN REMARK 500 7 ARG A 83 0.15 SIDE CHAIN REMARK 500 8 ARG A 12 0.17 SIDE CHAIN REMARK 500 8 ARG A 13 0.31 SIDE CHAIN REMARK 500 8 ARG A 66 0.26 SIDE CHAIN REMARK 500 8 ARG A 83 0.12 SIDE CHAIN REMARK 500 8 ARG A 104 0.20 SIDE CHAIN REMARK 500 9 ARG A 12 0.18 SIDE CHAIN REMARK 500 9 ARG A 13 0.10 SIDE CHAIN REMARK 500 9 ARG A 66 0.31 SIDE CHAIN REMARK 500 9 ARG A 83 0.14 SIDE CHAIN REMARK 500 9 ARG A 104 0.31 SIDE CHAIN REMARK 500 10 ARG A 12 0.30 SIDE CHAIN REMARK 500 10 ARG A 13 0.23 SIDE CHAIN REMARK 500 10 ARG A 66 0.14 SIDE CHAIN REMARK 500 10 ARG A 83 0.29 SIDE CHAIN REMARK 500 10 ARG A 104 0.32 SIDE CHAIN REMARK 500 11 ARG A 12 0.31 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 95 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 GA A 107 GA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 39 SG REMARK 620 2 CYS A 45 SG 101.5 REMARK 620 3 CYS A 48 SG 117.4 100.3 REMARK 620 4 CYS A 86 SG 96.3 119.5 121.2 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: GAL REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: GALLIUM METAL ION BINDING LIGANDS. REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA A 107 DBREF 1GPX A 1 106 UNP P00259 PUTX_PSEPU 1 106 SEQADV 1GPX SER A 85 UNP P00259 CYS 85 ENGINEERED MUTATION SEQRES 1 A 106 SER LYS VAL VAL TYR VAL SER HIS ASP GLY THR ARG ARG SEQRES 2 A 106 GLU LEU ASP VAL ALA ASP GLY VAL SER LEU MET GLN ALA SEQRES 3 A 106 ALA VAL SER ASN GLY ILE TYR ASP ILE VAL GLY ASP CYS SEQRES 4 A 106 GLY GLY SER ALA SER CYS ALA THR CYS HIS VAL TYR VAL SEQRES 5 A 106 ASN GLU ALA PHE THR ASP LYS VAL PRO ALA ALA ASN GLU SEQRES 6 A 106 ARG GLU ILE GLY MET LEU GLU CYS VAL THR ALA GLU LEU SEQRES 7 A 106 LYS PRO ASN SER ARG LEU SER CYS GLN ILE ILE MET THR SEQRES 8 A 106 PRO GLU LEU ASP GLY ILE VAL VAL ASP VAL PRO ASP ARG SEQRES 9 A 106 GLN TRP HET GA A 107 1 HETNAM GA GALLIUM (III) ION FORMUL 2 GA GA 3+ HELIX 1 D LEU A 23 GLY A 31 1 9 HELIX 2 F THR A 57 PRO A 61 1 5 HELIX 3 G GLU A 65 CYS A 73 1 9 SHEET 1 A 5 ARG A 12 VAL A 17 0 SHEET 2 A 5 SER A 1 VAL A 6 -1 N TYR A 5 O ARG A 13 SHEET 3 A 5 VAL A 98 VAL A 101 1 N VAL A 99 O VAL A 4 SHEET 4 A 5 VAL A 50 ASN A 53 -1 O TYR A 51 N ASP A 100 SHEET 5 A 5 SER A 82 LEU A 84 -1 N ARG A 83 O VAL A 50 SHEET 1 B 2 ILE A 89 MET A 90 0 SHEET 2 B 2 VAL A 21 SER A 22 -1 O VAL A 21 N MET A 90 LINK GA GA A 107 SG CYS A 39 1555 1555 2.24 LINK GA GA A 107 SG CYS A 45 1555 1555 2.27 LINK GA GA A 107 SG CYS A 48 1555 1555 2.27 LINK GA GA A 107 SG CYS A 86 1555 1555 2.27 SITE 1 GAL 4 CYS A 39 CYS A 45 CYS A 48 CYS A 86 SITE 1 AC1 6 MET A 24 CYS A 39 CYS A 45 CYS A 48 SITE 2 AC1 6 SER A 85 CYS A 86 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 14 2 Bytes