Header list of 2gzo.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 11-MAY-06 2GZO TITLE NMR STRUCTURE OF UPF0301 PROTEIN SO3346 FROM SHEWANELLA ONEIDENSIS: TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET SOR39 COMPND MOL_ID: 1; COMPND 2 MOLECULE: UPF0301 PROTEIN SO3346; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA ONEIDENSIS; SOURCE 3 ORGANISM_TAXID: 70863; SOURCE 4 STRAIN: XL-10; SOURCE 5 GENE: SO3346; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+ MAGIC; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS GFT-NMR, PROTEIN STRUCTURE, NESGC, ALPHA-BETA, STRUCTURAL GENOMICS, KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.K.SINGARAPU,G.LIU,A.ELETSKY,D.XU,D.K.SUKUMARAN,J.MEI,R.XIAO, AUTHOR 2 K.CUNNINGHAM,L.C.MA,S.RITU,T.B.ACTON,B.ROST,G.T.MONTELIONE, AUTHOR 3 T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 3 09-MAR-22 2GZO 1 REMARK SEQADV REVDAT 2 24-FEB-09 2GZO 1 VERSN REVDAT 1 20-JUN-06 2GZO 0 JRNL AUTH K.K.SINGARAPU,G.LIU,A.ELETSKY,D.XU,D.K.SUKUMARAN,J.MEI, JRNL AUTH 2 R.XIAO,K.CUNNINGHAM,L.C.MA,S.RITU,T.B.ACTON,B.ROST, JRNL AUTH 3 G.T.MONTELIONE,T.SZYPERSKI JRNL TITL NMR STRUCTURE OF UPF0301 PROTEIN SO3346 FROM SHEWANELLA JRNL TITL 2 ONEIDENSIS: NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET JRNL TITL 3 SOR39 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.5, CYANA 2.1, CNS 1.1 REMARK 3 AUTHORS : FRANK DELAGLIO, ET AL (NMRPIPE), PETER GUNTERT., REMARK 3 ET AL (CYANA), A.T.BRUNGER., ET AL (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 RESTRAINTS, 1828 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 126 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 35 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS. REMARK 4 REMARK 4 2GZO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-06. REMARK 100 THE DEPOSITION ID IS D_1000037746. 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 : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : MC2023, 50MM ARGININE, 10MM DTT, REMARK 210 50MM BIS TRIS PH 6.5, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : [4,3]D GFT, HNNCABCA; [4,3]D REMARK 210 GFT, CABCA(CO)NHN; [4,3]D GFT REMARK 210 ALI-HCCH; [4,3]D GFT ARO-HCCH; REMARK 210 [4,3]D GFT, HABCAB(CO)NHN; REMARK 210 SIMULTANIOUS HETERONUCLEAR REMARK 210 RESOLVED [1H, 1H]-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, AUTOSTRUCTURE 2.0.0, REMARK 210 XEASY 1.3.11 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS, REMARK 210 TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 LEU A 188 REMARK 465 GLU A 189 REMARK 465 HIS A 190 REMARK 465 HIS A 191 REMARK 465 HIS A 192 REMARK 465 HIS A 193 REMARK 465 HIS A 194 REMARK 465 HIS A 195 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 HG LEU A 103 HD2 HIS A 154 1.21 REMARK 500 HA LEU A 4 HE1 HIS A 7 1.28 REMARK 500 HG1 THR A 88 OD1 ASP A 122 1.60 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 GLN A 5 142.63 84.90 REMARK 500 1 PRO A 13 44.66 -71.12 REMARK 500 1 PHE A 20 -34.52 -175.30 REMARK 500 1 ARG A 22 -159.47 52.29 REMARK 500 1 THR A 23 -174.87 63.78 REMARK 500 1 GLU A 32 -86.44 64.03 REMARK 500 1 ILE A 40 48.87 -107.85 REMARK 500 1 GLN A 61 -83.50 -173.97 REMARK 500 1 VAL A 62 160.00 68.61 REMARK 500 1 SER A 63 84.67 76.93 REMARK 500 1 ALA A 64 44.06 -101.55 REMARK 500 1 SER A 70 -61.63 66.43 REMARK 500 1 ARG A 82 -95.46 -134.28 REMARK 500 1 TYR A 92 -169.35 -112.81 REMARK 500 1 TRP A 93 143.76 74.98 REMARK 500 1 ARG A 109 -63.33 -163.55 REMARK 500 1 ASP A 122 -57.95 -157.13 REMARK 500 1 ASN A 136 -78.76 -83.41 REMARK 500 1 SER A 146 -38.71 -157.01 REMARK 500 1 PHE A 158 -67.82 -91.88 REMARK 500 1 ASN A 161 -106.63 35.74 REMARK 500 1 HIS A 162 -61.40 -145.05 REMARK 500 1 SER A 172 -165.18 54.92 REMARK 500 1 LEU A 173 -74.44 -157.31 REMARK 500 1 PHE A 175 133.55 -172.01 REMARK 500 1 GLN A 179 68.96 -105.15 REMARK 500 1 LEU A 180 118.05 -168.00 REMARK 500 1 SER A 181 81.79 -162.42 REMARK 500 2 GLU A 2 -60.37 68.88 REMARK 500 2 ASN A 6 89.41 -163.79 REMARK 500 2 HIS A 7 -169.57 -163.79 REMARK 500 2 LEU A 15 -74.24 -55.96 REMARK 500 2 ASP A 16 -80.42 -155.28 REMARK 500 2 THR A 18 -84.02 -67.37 REMARK 500 2 PHE A 19 -17.43 65.83 REMARK 500 2 PHE A 20 -69.98 -105.28 REMARK 500 2 THR A 23 -87.84 70.72 REMARK 500 2 GLU A 60 -82.81 -170.12 REMARK 500 2 GLN A 61 -59.97 -158.74 REMARK 500 2 SER A 63 9.63 59.58 REMARK 500 2 ALA A 64 -68.35 -104.07 REMARK 500 2 PRO A 91 74.68 -67.54 REMARK 500 2 TYR A 92 153.64 67.39 REMARK 500 2 LEU A 99 -59.17 74.79 REMARK 500 2 ARG A 109 -69.77 -158.48 REMARK 500 2 SER A 117 -71.68 -141.67 REMARK 500 2 ARG A 119 -176.16 67.70 REMARK 500 2 SER A 120 -55.32 -153.95 REMARK 500 2 TYR A 130 -167.03 -161.01 REMARK 500 2 LEU A 138 36.46 -150.97 REMARK 500 REMARK 500 THIS ENTRY HAS 602 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: SOR39 RELATED DB: TARGETDB DBREF 2GZO A 1 187 UNP Q8EBZ9 Y3346_SHEON 1 187 SEQADV 2GZO LEU A 188 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO GLU A 189 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO HIS A 190 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO HIS A 191 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO HIS A 192 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO HIS A 193 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO HIS A 194 UNP Q8EBZ9 EXPRESSION TAG SEQADV 2GZO HIS A 195 UNP Q8EBZ9 EXPRESSION TAG SEQRES 1 A 195 MET GLU SER LEU GLN ASN HIS PHE LEU ILE ALA MET PRO SEQRES 2 A 195 SER LEU ASP ASP THR PHE PHE GLU ARG THR VAL ILE TYR SEQRES 3 A 195 LEU CYS GLU HIS ASP GLU LYS GLY ALA MET GLY LEU VAL SEQRES 4 A 195 ILE ASN LYS PRO LEU GLY ILE GLU VAL ASN SER LEU LEU SEQRES 5 A 195 GLU GLN MET ASP LEU PRO THR GLU GLN VAL SER ALA ASP SEQRES 6 A 195 LEU ALA MET GLY SER GLN VAL LEU MET GLY GLY PRO VAL SEQRES 7 A 195 SER GLN ASP ARG GLY PHE VAL LEU HIS THR SER GLN PRO SEQRES 8 A 195 TYR TRP ALA ASN SER THR GLU LEU GLY SER GLY LEU MET SEQRES 9 A 195 LEU THR THR SER ARG ASP VAL LEU THR ALA ILE GLY SER SEQRES 10 A 195 LYS ARG SER PRO ASP LYS PHE LEU VAL ALA LEU GLY TYR SEQRES 11 A 195 ALA GLY TRP SER LYS ASN GLN LEU GLU GLN GLU LEU ALA SEQRES 12 A 195 ASP ASN SER TRP LEU THR ILE PRO ALA ASP HIS ALA LEU SEQRES 13 A 195 LEU PHE ASP ILE ASN HIS GLU ASP ARG TRP GLN GLN ALA SEQRES 14 A 195 SER ARG SER LEU GLY PHE GLU ALA TRP GLN LEU SER THR SEQRES 15 A 195 GLN ALA GLY HIS ALA LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 GLU A 47 ASP A 56 1 10 HELIX 2 2 ARG A 109 GLY A 116 1 8 HELIX 3 3 GLY A 132 GLN A 137 1 6 HELIX 4 4 LEU A 138 SER A 146 1 9 HELIX 5 5 ASP A 153 PHE A 158 1 6 HELIX 6 6 GLU A 163 SER A 172 1 10 SHEET 1 A 4 GLY A 37 VAL A 39 0 SHEET 2 A 4 THR A 23 LEU A 27 -1 N TYR A 26 O LEU A 38 SHEET 3 A 4 HIS A 7 ALA A 11 -1 N LEU A 9 O ILE A 25 SHEET 4 A 4 LEU A 148 PRO A 151 -1 O LEU A 148 N ILE A 10 SHEET 1 B 2 LEU A 73 MET A 74 0 SHEET 2 B 2 ALA A 127 LEU A 128 1 O LEU A 128 N LEU A 73 SHEET 1 C 3 LEU A 103 THR A 106 0 SHEET 2 C 3 VAL A 85 THR A 88 -1 N VAL A 85 O THR A 106 SHEET 3 C 3 PHE A 124 LEU A 125 -1 O LEU A 125 N LEU 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 9 2 Bytes