Header list of 2gvs.pdb file
Complete list - r 9 2 Bytes
HEADER LIPID BINDING PROTEIN 03-MAY-06 2GVS TITLE NMR SOLUTION STRUCTURE OF CSPSG4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHEMOSENSORY PROTEIN CSP-SG4; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SCHISTOCERCA GREGARIA; SOURCE 3 ORGANISM_TAXID: 7010; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-SCHI 10 KEYWDS ALPHA-COIL, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.TOMASELLI,O.CRESCENZI,D.SANFELICE,E.AB,T.TANCREDI,D.PICONE REVDAT 3 09-MAR-22 2GVS 1 REMARK REVDAT 2 24-FEB-09 2GVS 1 VERSN REVDAT 1 12-SEP-06 2GVS 0 JRNL AUTH S.TOMASELLI,O.CRESCENZI,D.SANFELICE,E.AB,R.WECHSELBERGER, JRNL AUTH 2 S.ANGELI,A.SCALONI,R.BOELENS,T.TANCREDI,P.PELOSI,D.PICONE JRNL TITL SOLUTION STRUCTURE OF A CHEMOSENSORY PROTEIN FROM THE DESERT JRNL TITL 2 LOCUST SCHISTOCERCA GREGARIA(,). JRNL REF BIOCHEMISTRY V. 45 10606 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16939212 JRNL DOI 10.1021/BI060998W REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 99 REMARK 3 AUTHORS : REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GVS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-06. REMARK 100 THE DEPOSITION ID IS D_1000037608. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 50 MM NA PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 50MM SODIUM PHOSPHATE BUFFER, REMARK 210 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE LINUX, NMRVIEW 5.0.4, REMARK 210 CYANA 2.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: 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 4 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ASN A 55 25.61 -148.71 REMARK 500 1 ASP A 91 71.55 -152.15 REMARK 500 1 LEU A 107 88.59 -67.66 REMARK 500 2 ASN A 55 23.40 -144.72 REMARK 500 2 ASP A 91 71.05 -150.17 REMARK 500 3 ASN A 55 22.29 -144.45 REMARK 500 3 ASP A 91 72.56 -151.53 REMARK 500 3 GLU A 106 21.19 -76.23 REMARK 500 4 THR A 6 77.12 -115.99 REMARK 500 4 ASN A 55 23.12 -144.04 REMARK 500 4 GLU A 106 30.29 -92.32 REMARK 500 4 HIS A 108 53.79 -69.97 REMARK 500 5 ASN A 55 23.17 -144.98 REMARK 500 5 ASP A 91 76.54 -150.17 REMARK 500 5 LYS A 105 47.49 36.86 REMARK 500 6 ASN A 55 24.51 -145.00 REMARK 500 6 ASP A 91 74.47 -152.37 REMARK 500 6 GLU A 104 -55.27 -124.35 REMARK 500 6 HIS A 108 29.77 -141.82 REMARK 500 7 TYR A 4 55.98 -112.56 REMARK 500 7 THR A 6 28.18 -79.97 REMARK 500 7 ASN A 55 22.57 -144.23 REMARK 500 7 ASP A 91 73.23 -150.71 REMARK 500 7 LYS A 105 26.56 49.07 REMARK 500 7 GLU A 106 38.18 -75.81 REMARK 500 8 LYS A 7 107.40 -59.44 REMARK 500 8 GLU A 35 2.96 45.58 REMARK 500 8 ASN A 55 22.37 -146.75 REMARK 500 8 ASP A 91 65.33 -157.12 REMARK 500 8 LEU A 107 94.01 -62.43 REMARK 500 9 ASN A 55 22.85 -144.86 REMARK 500 9 ASP A 91 74.91 -153.88 REMARK 500 9 LYS A 105 52.15 32.64 REMARK 500 9 HIS A 108 109.44 -59.32 REMARK 500 10 ASN A 55 24.94 -142.34 REMARK 500 10 ASP A 91 69.53 -151.33 REMARK 500 10 GLU A 104 -31.28 -132.65 REMARK 500 10 LYS A 105 36.15 35.82 REMARK 500 10 LEU A 107 71.78 -67.96 REMARK 500 11 TYR A 4 41.07 -153.03 REMARK 500 11 ASN A 55 25.18 -146.62 REMARK 500 11 ASP A 91 73.17 -150.01 REMARK 500 12 GLU A 2 55.94 -150.20 REMARK 500 12 ASN A 55 22.96 -147.01 REMARK 500 12 ASP A 91 74.50 -150.57 REMARK 500 12 GLU A 104 -55.84 -127.90 REMARK 500 12 GLU A 106 47.15 -76.12 REMARK 500 13 THR A 6 78.02 -119.70 REMARK 500 13 ASN A 55 23.11 -141.11 REMARK 500 13 ASP A 91 77.95 -150.97 REMARK 500 REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2GVS A 1 109 UNP O76476 O76476_SCHGR 1 109 SEQRES 1 A 109 GLU GLU LYS TYR THR THR LYS TYR ASP ASN VAL ASN LEU SEQRES 2 A 109 ASP GLU ILE LEU ALA ASN ASP ARG LEU LEU ASN LYS TYR SEQRES 3 A 109 VAL GLN CYS LEU LEU GLU ASP ASP GLU SER ASN CYS THR SEQRES 4 A 109 ALA ASP GLY LYS GLU LEU LYS SER VAL ILE PRO ASP ALA SEQRES 5 A 109 LEU SER ASN GLU CYS ALA LYS CYS ASN GLU LYS GLN LYS SEQRES 6 A 109 GLU GLY THR LYS LYS VAL LEU LYS HIS LEU ILE ASN HIS SEQRES 7 A 109 LYS PRO ASP VAL TRP ALA GLN LEU LYS ALA LYS TYR ASP SEQRES 8 A 109 PRO ASP GLY THR TYR SER LYS LYS TYR GLU ASP ARG GLU SEQRES 9 A 109 LYS GLU LEU HIS GLN HELIX 1 1 ASN A 12 ASN A 19 1 8 HELIX 2 2 ASN A 19 GLU A 32 1 14 HELIX 3 3 ASP A 41 ILE A 49 1 9 HELIX 4 4 PRO A 50 ASN A 55 1 6 HELIX 5 5 ASN A 61 LYS A 79 1 19 HELIX 6 6 LYS A 79 ASP A 91 1 13 HELIX 7 7 SER A 97 ASP A 102 1 6 SSBOND 1 CYS A 29 CYS A 38 1555 1555 2.03 SSBOND 2 CYS A 57 CYS A 60 1555 1555 2.04 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