Header list of 2gm2.pdb file
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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 05-APR-06 2GM2 TITLE NMR STRUCTURE OF XANTHOMONAS CAMPESTRIS XCC1710: NORTHEAST STRUCTURAL TITLE 2 GENOMICS CONSORTIUM TARGET XCR35 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS STR. ATCC SOURCE 3 33913; SOURCE 4 ORGANISM_TAXID: 190485; SOURCE 5 STRAIN: PV. CAMPESTRIS STR. ATCC 33913; SOURCE 6 GENE: XCC1710; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS MTH938-LIKE FOLD, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN KEYWDS 3 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.R.CORT,R.XIAO,D.Y.WANG,L.C.MA,M.CIANO,G.T.MONTELIONE,T.A.RAMELOT, AUTHOR 2 M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 3 09-MAR-22 2GM2 1 REMARK SEQADV REVDAT 2 24-FEB-09 2GM2 1 VERSN REVDAT 1 25-APR-06 2GM2 0 JRNL AUTH J.R.CORT,T.A.RAMELOT,G.T.MONTELIONE,M.A.KENNEDY JRNL TITL NMR STRUCTURE OF XANTHOMONAS CAMPESTRIS XCC1710 PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1.C, CNS 1.1 REMARK 3 AUTHORS : VARIAN (VNMR), A. BRUNGER ET AL (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 935 RESTRAINTS. REMARK 3 SUMMARY OF EXPERIMENTAL CONSTRAINTS REMARK 3 RESTRAINING DISTANCE RESTRAINTS: TOTAL = 758; REMARK 3 INTRA-RESIDUE [I=J] = 174; REMARK 3 SEQUENTIAL [(I-J)=1] = 174; REMARK 3 MEDIUM RANGE [1<(I-J)<5] = 109; REMARK 3 LONG RANGE [(I-J)>=5] = 301; REMARK 3 HYDROGEN BOND RESTRAINTS = 56 (2 PER H-BOND); REMARK 3 NUMBER OF RESTRAINING DISTANCE RESTRAINTS PER RESTRAINED RESIDUE = REMARK 3 7.3; REMARK 3 DIHEDRAL-ANGLE RESTRAINTS = 121 (60 PHI, 59 PSI, 2 CHI-1); REMARK 3 TOTAL NUMBER OF RESTRAINTS PER RESTRAINED RESIDUE = 8.3; REMARK 3 NUMBER OF LONG RANGE NOE DISTANCE RESTRAINTS PER RESTRAINED REMARK 3 RESIDUE = 2.7; REMARK 3 NUMBER OF STRUCTURES COMPUTED = 40; REMARK 3 NUMBER OF STRUCTURES USED = 20; REMARK 3 AVERAGE DISTANCE VIOLATIONS >0.0001 ANG = 19.8 +/- 3.5; REMARK 3 AVERAGE R.M.S. DISTANCE VIOLATION = 0.0009 +/- 0.0003 ANG; REMARK 3 MAXIMUM NUMBER OF DISTANCE VIOLATIONS 25; REMARK 3 MAXIMUM DISTANCE VIOLATION = 0.03 ANG; REMARK 3 AVERAGE DIHEDRAL ANGLE VIOLATIONS: >0.0001 DEG = 2.5+/-1.3; REMARK 3 MAX NUMBER OF DIHEDRAL ANGLE VIOLATIONS = 4; REMARK 3 AVERAGE R.M.S. DIHEDRAL ANGLE VIOLATION = 0.02 +/- .01 DEG.; REMARK 3 RMSD VALUES TO AVERAGE STRUCTURE: REMARK 3 BACKBONE ATOMS (N,C,C' RESIDUES 12-125) = 0.88 ANG, REMARK 3 ALL HEAVY ATOMS = 1.38 ANG; REMARK 3 BACKBONE ATOMS (N,C,C' RESIDUES 32-122) = 0.71 ANG, REMARK 3 ALL HEAVY ATOMS = 1.21 ANG; REMARK 3 BACKBONE ATOMS (N,C,C' RESIDUES 16-17,21-36,39-41,44-46,53-73,76- REMARK 3 122) = 0.70 ANG, REMARK 3 ALL HEAVY ATOMS = 1.14 ANG; REMARK 3 PROCHECK (RESIDUES 16-17,21-36,39-41,44-46,53-73,76-122): REMARK 3 MOST FAVORED REGIONS = 84.6%; REMARK 3 ADDITIONAL ALLOWED REGIONS = 14.0%; REMARK 3 GENEROUSLY ALLOWED REGIONS = 0.2%; REMARK 3 DISALLOWED REGIONS = 1.2%; REMARK 3 PROCHECK (RESIDUES 12-125): REMARK 3 MOST FAVORED REGIONS = 77.8%; REMARK 3 ADDITIONAL ALLOWED REGIONS = 19.2%; REMARK 3 GENEROUSLY ALLOWED REGIONS = 2.0%; REMARK 3 DISALLOWED REGIONS = 1.0%. REMARK 4 REMARK 4 2GM2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-06. REMARK 100 THE DEPOSITION ID IS D_1000037282. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100 MM NACL, 20 MM CACL2 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM XCC1710; 0.5 MM XCC1710 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98, SPARKY 3.106, REMARK 210 AUTOSTRUCTURE 2.1.1, X-PLOR NIH, REMARK 210 CNS 1.1 REMARK 210 METHOD USED : THE INITIAL STRUCTURE WAS REMARK 210 DETERMINED USING AUTOMATED REMARK 210 STRUCTURE DETERMINATION REMARK 210 (AUTOSTRUCTURE) AND REFINED REMARK 210 MANUALLY. A FINAL REFINEMENT REMARK 210 USED SIMULTATED ANNEALING IN REMARK 210 EXPLICIT SOLVENT. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FEWEST RESTRAINT REMARK 210 VIOLATIONS, LOW RESTRAINT REMARK 210 VIOLATION ENERGIES, AND REMARK 210 ACCEPTABLE GEOMETRY 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 4 76.75 -105.95 REMARK 500 1 GLN A 5 -155.55 -137.78 REMARK 500 1 GLU A 6 93.45 65.95 REMARK 500 1 ASP A 9 -150.56 59.26 REMARK 500 1 ASN A 25 -86.42 64.57 REMARK 500 1 GLN A 31 -157.13 -141.37 REMARK 500 1 PRO A 37 39.16 -70.56 REMARK 500 1 ASP A 38 -45.28 -139.12 REMARK 500 1 PRO A 45 34.21 -79.10 REMARK 500 1 ASN A 64 81.05 59.41 REMARK 500 1 THR A 72 35.97 -98.49 REMARK 500 1 ARG A 75 77.76 -113.19 REMARK 500 1 HIS A 127 -150.38 -133.15 REMARK 500 1 HIS A 130 -33.58 -144.64 REMARK 500 2 LEU A 3 45.53 -80.87 REMARK 500 2 ASN A 4 -58.05 177.30 REMARK 500 2 HIS A 7 123.59 -173.37 REMARK 500 2 ASN A 25 -83.89 60.53 REMARK 500 2 GLN A 31 -154.66 -125.20 REMARK 500 2 HIS A 43 43.92 -86.72 REMARK 500 2 SER A 48 161.87 67.65 REMARK 500 2 ASN A 64 80.20 62.60 REMARK 500 2 ARG A 75 170.44 65.02 REMARK 500 2 HIS A 128 -85.96 69.64 REMARK 500 2 HIS A 129 -77.72 63.59 REMARK 500 2 HIS A 130 107.75 173.77 REMARK 500 3 GLN A 5 -158.03 57.61 REMARK 500 3 GLU A 6 168.48 70.87 REMARK 500 3 ALA A 13 -96.20 -71.31 REMARK 500 3 ASN A 25 -82.68 66.23 REMARK 500 3 GLN A 31 -86.87 -120.87 REMARK 500 3 PRO A 37 29.16 -71.18 REMARK 500 3 ASP A 38 -56.51 -151.41 REMARK 500 3 HIS A 43 47.51 -87.31 REMARK 500 3 SER A 48 -164.13 61.30 REMARK 500 3 LEU A 49 30.32 -88.78 REMARK 500 3 ASN A 64 83.16 30.70 REMARK 500 4 ASN A 4 32.81 -99.49 REMARK 500 4 GLN A 5 87.05 69.04 REMARK 500 4 THR A 11 -49.51 -131.49 REMARK 500 4 ASN A 25 -78.53 67.78 REMARK 500 4 ASP A 38 -49.33 -159.99 REMARK 500 4 GLU A 42 -160.43 -100.35 REMARK 500 4 SER A 48 103.27 -54.03 REMARK 500 4 LEU A 49 19.82 58.43 REMARK 500 4 ASN A 64 81.17 62.89 REMARK 500 4 HIS A 130 98.21 63.10 REMARK 500 5 LEU A 3 -75.74 -96.94 REMARK 500 5 ASN A 4 -61.70 70.62 REMARK 500 5 GLN A 5 41.82 -83.71 REMARK 500 REMARK 500 THIS ENTRY HAS 226 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2FVT RELATED DB: PDB REMARK 900 RHODOPSEUDOMONAS PALUSTRIS RPA2829, DISTANT SEQUENCE HOMOLOG (22% REMARK 900 IDENTITY), NMR STRUCTURE SOLVED IN SAME LABORATORY. REMARK 900 RELATED ID: XCR35 RELATED DB: TARGETDB DBREF 2GM2 A 1 124 GB 21112802 AAM41004 1 124 SEQADV 2GM2 LEU A 125 GB 21112802 CLONING ARTIFACT SEQADV 2GM2 GLU A 126 GB 21112802 CLONING ARTIFACT SEQADV 2GM2 HIS A 127 GB 21112802 EXPRESSION TAG SEQADV 2GM2 HIS A 128 GB 21112802 EXPRESSION TAG SEQADV 2GM2 HIS A 129 GB 21112802 EXPRESSION TAG SEQADV 2GM2 HIS A 130 GB 21112802 EXPRESSION TAG SEQADV 2GM2 HIS A 131 GB 21112802 EXPRESSION TAG SEQADV 2GM2 HIS A 132 GB 21112802 EXPRESSION TAG SEQRES 1 A 132 MET PRO LEU ASN GLN GLU HIS PRO ASP TYR THR TYR ALA SEQRES 2 A 132 LEU ARG ALA ALA ASP GLY ARG HIS ALA LYS VAL ASN GLU SEQRES 3 A 132 GLN ILE LEU GLN GLN SER PHE ILE LEU MET PRO ASP GLU SEQRES 4 A 132 LEU VAL GLU HIS TRP PRO VAL PRO SER LEU GLY GLN LEU SEQRES 5 A 132 GLN PRO ALA HIS MET ASP ALA VAL LEU ALA LEU ASN PRO SEQRES 6 A 132 ALA VAL ILE LEU LEU GLY THR GLY GLU ARG GLN GLN PHE SEQRES 7 A 132 PRO SER THR ASP VAL LEU ALA ALA CYS LEU THR ARG GLY SEQRES 8 A 132 ILE GLY LEU GLU ALA MET THR ASN ALA ALA ALA ALA ARG SEQRES 9 A 132 THR TYR ASN VAL LEU ALA SER GLU GLY ARG ARG VAL ALA SEQRES 10 A 132 LEU ALA MET ILE VAL GLY GLY LEU GLU HIS HIS HIS HIS SEQRES 11 A 132 HIS HIS HELIX 1 1 SER A 48 LEU A 52 5 5 HELIX 2 2 MET A 57 ASN A 64 1 8 HELIX 3 3 SER A 80 GLY A 91 1 12 HELIX 4 4 THR A 98 GLY A 113 1 16 SHEET 1 A 3 LEU A 14 ALA A 17 0 SHEET 2 A 3 ALA A 22 VAL A 24 -1 O LYS A 23 N ALA A 16 SHEET 3 A 3 GLN A 27 LEU A 29 -1 O GLN A 27 N VAL A 24 SHEET 1 B 5 LEU A 40 VAL A 41 0 SHEET 2 B 5 SER A 32 LEU A 35 -1 N ILE A 34 O VAL A 41 SHEET 3 B 5 VAL A 116 ILE A 121 -1 O LEU A 118 N LEU A 35 SHEET 4 B 5 VAL A 67 GLY A 71 1 N GLY A 71 O ALA A 119 SHEET 5 B 5 GLY A 93 MET A 97 1 O GLU A 95 N LEU A 70 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