Header list of 1jcu.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS 11-JUN-01 1JCU TITLE SOLUTION STRUCTURE OF MTH1692 PROTEIN FROM METHANOBACTERIUM TITLE 2 THERMOAUTOTROPHICUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONSERVED PROTEIN MTH1692; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS; SOURCE 3 ORGANISM_TAXID: 145262; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD MAGIC; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS MIXED ALPHA-BETA STRUCTURE, STRUCTURAL GENOMICS EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.KOZLOV,I.EKIEL,K.GEHRING REVDAT 4 23-FEB-22 1JCU 1 REMARK REVDAT 3 24-FEB-09 1JCU 1 VERSN REVDAT 2 01-APR-03 1JCU 1 JRNL REVDAT 1 24-JUL-02 1JCU 0 JRNL AUTH A.YEE,X.CHANG,A.PINEDA-LUCENA,B.WU,A.SEMESI,B.LE,T.RAMELOT, JRNL AUTH 2 G.M.LEE,S.BHATTACHARYYA,P.GUTIERREZ,A.DENISOV,C.H.LEE, JRNL AUTH 3 J.R.CORT,G.KOZLOV,J.LIAO,G.FINAK,L.CHEN,D.WISHART,W.LEE, JRNL AUTH 4 L.P.MCINTOSH,K.GEHRING,M.A.KENNEDY,A.M.EDWARDS, JRNL AUTH 5 C.H.ARROWSMITH JRNL TITL AN NMR APPROACH TO STRUCTURAL PROTEOMICS. JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 1825 2002 JRNL REFN ISSN 0027-8424 JRNL PMID 11854485 JRNL DOI 10.1073/PNAS.042684599 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.1, CNS 0.9 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON 1467 NON-REDUNDANT NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, REMARK 3 197 DIHEDRAL ANGLE RESTRAINTS, AND 86 HYDROGEN BONDS. REMARK 4 REMARK 4 1JCU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-01. REMARK 100 THE DEPOSITION ID IS D_1000013634. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 320 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 0.3M REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 3MM MTH1692 U-15N; 50MM REMARK 210 PHOSPHATE BUFFER; 0.15 M NACL; REMARK 210 1MM DTT; 1MM NAN3; 3MM MTH1692 U- REMARK 210 15N,13C; 50MM PHOSPHATE BUFFER; REMARK 210 0.15 M NACL; 1MM DTT; 1MM NAN3; REMARK 210 3MM MTH1692 UNLABELED; 50MM REMARK 210 PHOSPHATE BUFFER; 0.15 M NACL; REMARK 210 1MM DTT; 1MM NAN3; 3MM MTH1692 REMARK 210 UNLABELED; 50MM PHOSPHATE BUFFER; REMARK 210 0.15 M NACL; 1MM DTT; 1MM NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS; DRX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : GIFA 4.31, XEASY 1.3.13, ARIA REMARK 210 0.9 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: THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE REMARK 210 -RESONANCE NMR TECHNIQUES. 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 HB3 LEU A 172 H ASP A 173 1.34 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 LEU A 2 -66.01 -105.35 REMARK 500 1 THR A 7 -178.04 -69.75 REMARK 500 1 ARG A 8 -65.22 -99.06 REMARK 500 1 PRO A 13 179.82 -59.65 REMARK 500 1 TYR A 31 104.41 -167.96 REMARK 500 1 THR A 33 -150.68 -123.05 REMARK 500 1 THR A 35 -112.79 -99.74 REMARK 500 1 ILE A 36 -161.75 -112.58 REMARK 500 1 ASN A 42 100.60 -55.52 REMARK 500 1 LYS A 56 -74.07 -79.78 REMARK 500 1 ARG A 58 -80.66 -112.37 REMARK 500 1 ILE A 74 54.81 -113.54 REMARK 500 1 PRO A 75 -83.14 -61.74 REMARK 500 1 ILE A 91 57.52 -115.53 REMARK 500 1 PRO A 93 -153.24 -78.92 REMARK 500 1 PRO A 95 32.57 -79.58 REMARK 500 1 ASN A 103 -165.56 -74.97 REMARK 500 1 GLU A 104 43.58 -76.65 REMARK 500 1 PRO A 107 103.87 -49.27 REMARK 500 1 SER A 115 51.10 -105.75 REMARK 500 1 ARG A 133 -87.59 -75.94 REMARK 500 1 ASN A 142 32.57 -158.13 REMARK 500 1 ILE A 143 -155.78 -75.50 REMARK 500 1 ALA A 161 14.64 -153.95 REMARK 500 1 VAL A 162 -78.93 -80.67 REMARK 500 1 VAL A 165 -169.88 -69.36 REMARK 500 1 ASP A 170 -161.49 -70.90 REMARK 500 1 CYS A 171 -53.25 -146.20 REMARK 500 1 LEU A 172 -128.63 -130.92 REMARK 500 1 PRO A 176 -139.73 -91.93 REMARK 500 1 ASP A 181 65.63 -108.25 REMARK 500 1 LEU A 182 89.38 -69.90 REMARK 500 1 THR A 183 -80.08 -81.19 REMARK 500 1 VAL A 184 -127.21 -120.45 REMARK 500 1 ARG A 188 41.63 -101.08 REMARK 500 1 VAL A 189 105.24 -56.95 REMARK 500 1 LEU A 197 40.44 -157.09 REMARK 500 2 ILE A 6 -141.11 -75.07 REMARK 500 2 TYR A 31 103.76 -165.29 REMARK 500 2 THR A 33 -152.15 -116.93 REMARK 500 2 THR A 35 -116.14 -100.04 REMARK 500 2 ASN A 42 109.73 -56.58 REMARK 500 2 ARG A 58 77.37 -117.36 REMARK 500 2 SER A 59 71.51 -154.89 REMARK 500 2 ILE A 74 61.23 -113.31 REMARK 500 2 PRO A 75 -72.06 -65.04 REMARK 500 2 ILE A 91 65.78 -113.80 REMARK 500 2 PRO A 93 -154.55 -79.03 REMARK 500 2 PRO A 95 42.37 -78.67 REMARK 500 2 ASN A 103 -157.21 -74.52 REMARK 500 REMARK 500 THIS ENTRY HAS 664 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1JCU A 1 208 UNP O27727 O27727_METTH 1 208 SEQRES 1 A 208 MET LEU ILE ARG LYS ILE THR ARG LYS ASN PRO SER PRO SEQRES 2 A 208 ASP VAL LEU GLU GLU ALA ILE SER VAL MET GLU GLY GLY SEQRES 3 A 208 GLY ILE VAL ILE TYR PRO THR ASP THR ILE TYR GLY LEU SEQRES 4 A 208 GLY VAL ASN ALA LEU ASP GLU ASP ALA VAL ARG ARG LEU SEQRES 5 A 208 PHE ARG VAL LYS GLY ARG SER PRO HIS LYS PRO VAL SER SEQRES 6 A 208 ILE CYS VAL SER CYS VAL ASP GLU ILE PRO ARG PHE SER SEQRES 7 A 208 ARG PRO SER GLY ASP ALA MET GLU LEU MET GLU ARG ILE SEQRES 8 A 208 LEU PRO GLY PRO TYR THR VAL VAL LEU GLU ARG ASN GLU SEQRES 9 A 208 LEU ILE PRO ASP VAL ILE THR GLY GLY SER SER ARG VAL SEQRES 10 A 208 GLY ILE ARG VAL PRO ASP ASP GLU ILE CYS ARG ARG ILE SEQRES 11 A 208 ALA ALA ARG PHE PRO VAL THR ALA THR SER ALA ASN ILE SEQRES 12 A 208 SER GLY LYS PRO PRO SER PRO ARG LEU GLU GLU ILE VAL SEQRES 13 A 208 ARG ASP LEU ASP ALA VAL ASP LEU VAL LEU ASP ALA GLY SEQRES 14 A 208 ASP CYS LEU ASP MET GLU PRO SER THR VAL ILE ASP LEU SEQRES 15 A 208 THR VAL ASN PRO PRO ARG VAL LEU ARG ARG GLY LYS GLY SEQRES 16 A 208 PRO LEU ASP PRO VAL LEU LEU ARG GLY ALA GLY ASP VAL HELIX 1 1 PRO A 13 GLY A 25 1 13 HELIX 2 2 ASP A 45 LYS A 56 1 12 HELIX 3 3 SER A 81 ILE A 91 1 11 HELIX 4 4 PRO A 107 GLY A 112 1 6 HELIX 5 5 ASP A 124 PHE A 134 1 11 HELIX 6 6 ARG A 151 LEU A 159 1 9 SHEET 1 A 8 ASP A 163 LEU A 164 0 SHEET 2 A 8 ILE A 28 ILE A 30 1 O ILE A 28 N LEU A 164 SHEET 3 A 8 GLY A 38 ASN A 42 -1 N GLY A 40 O VAL A 29 SHEET 4 A 8 VAL A 136 SER A 140 -1 N THR A 137 O VAL A 41 SHEET 5 A 8 SER A 65 CYS A 67 -1 O SER A 65 N ALA A 138 SHEET 6 A 8 ARG A 116 ARG A 120 1 O GLY A 118 N ILE A 66 SHEET 7 A 8 TYR A 96 ARG A 102 -1 N VAL A 98 O ILE A 119 SHEET 8 A 8 SER A 78 ARG A 79 -1 O ARG A 79 N GLU A 101 SHEET 1 B 9 ASP A 163 LEU A 164 0 SHEET 2 B 9 ILE A 28 ILE A 30 1 O ILE A 28 N LEU A 164 SHEET 3 B 9 GLY A 38 ASN A 42 -1 N GLY A 40 O VAL A 29 SHEET 4 B 9 VAL A 136 SER A 140 -1 N THR A 137 O VAL A 41 SHEET 5 B 9 SER A 65 CYS A 67 -1 O SER A 65 N ALA A 138 SHEET 6 B 9 ARG A 116 ARG A 120 1 O GLY A 118 N ILE A 66 SHEET 7 B 9 TYR A 96 ARG A 102 -1 N VAL A 98 O ILE A 119 SHEET 8 B 9 THR A 178 ILE A 180 1 O THR A 178 N THR A 97 SHEET 9 B 9 VAL A 189 ARG A 191 -1 N LEU A 190 O VAL A 179 CISPEP 1 LEU A 92 PRO A 93 1 -2.21 CISPEP 2 GLU A 175 PRO A 176 1 0.45 CISPEP 3 LEU A 92 PRO A 93 2 -1.70 CISPEP 4 GLU A 175 PRO A 176 2 1.16 CISPEP 5 LEU A 92 PRO A 93 3 -1.30 CISPEP 6 GLU A 175 PRO A 176 3 1.28 CISPEP 7 LEU A 92 PRO A 93 4 -0.30 CISPEP 8 GLU A 175 PRO A 176 4 1.44 CISPEP 9 LEU A 92 PRO A 93 5 -1.03 CISPEP 10 GLU A 175 PRO A 176 5 0.79 CISPEP 11 LEU A 92 PRO A 93 6 -0.10 CISPEP 12 GLU A 175 PRO A 176 6 0.99 CISPEP 13 LEU A 92 PRO A 93 7 -0.99 CISPEP 14 GLU A 175 PRO A 176 7 1.16 CISPEP 15 LEU A 92 PRO A 93 8 0.38 CISPEP 16 GLU A 175 PRO A 176 8 1.46 CISPEP 17 LEU A 92 PRO A 93 9 -0.51 CISPEP 18 GLU A 175 PRO A 176 9 3.34 CISPEP 19 LEU A 92 PRO A 93 10 -0.82 CISPEP 20 GLU A 175 PRO A 176 10 0.89 CISPEP 21 LEU A 92 PRO A 93 11 -0.16 CISPEP 22 GLU A 175 PRO A 176 11 0.96 CISPEP 23 LEU A 92 PRO A 93 12 -1.22 CISPEP 24 GLU A 175 PRO A 176 12 0.98 CISPEP 25 LEU A 92 PRO A 93 13 -0.09 CISPEP 26 GLU A 175 PRO A 176 13 0.82 CISPEP 27 LEU A 92 PRO A 93 14 -1.40 CISPEP 28 GLU A 175 PRO A 176 14 0.80 CISPEP 29 LEU A 92 PRO A 93 15 0.05 CISPEP 30 GLU A 175 PRO A 176 15 1.15 CISPEP 31 LEU A 92 PRO A 93 16 0.02 CISPEP 32 GLU A 175 PRO A 176 16 1.09 CISPEP 33 LEU A 92 PRO A 93 17 -0.34 CISPEP 34 GLU A 175 PRO A 176 17 0.26 CISPEP 35 LEU A 92 PRO A 93 18 -1.79 CISPEP 36 GLU A 175 PRO A 176 18 0.58 CISPEP 37 LEU A 92 PRO A 93 19 -1.13 CISPEP 38 GLU A 175 PRO A 176 19 0.75 CISPEP 39 LEU A 92 PRO A 93 20 0.53 CISPEP 40 GLU A 175 PRO A 176 20 1.44 CRYST1 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 - b 23 2 Bytes