Header list of 1r9p.pdb file
Complete list - p 24 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 30-OCT-03 1R9P TITLE SOLUTION NMR STRUCTURE OF THE HAEMOPHILUS INFLUENZAE IRON-SULFUR TITLE 2 CLUSTER ASSEMBLY PROTEIN U (ISCU) WITH ZINC BOUND AT THE ACTIVE SITE. TITLE 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET IR24. COMPND MOL_ID: 1; COMPND 2 MOLECULE: NIFU-LIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ISCU; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE; SOURCE 3 ORGANISM_TAXID: 727; SOURCE 4 GENE: HI0377; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (LAMDA DE3) PMGK; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D KEYWDS IRON-SULFUR CLUSTER BINDING, ZINC BINDING, THREE CONSERVED CYS, 3BETA KEYWDS 2 STRANDS, 4 ALPHA HELIXES, NESG, STRUCTURAL GENOMICS, PSI-2, PROTEIN KEYWDS 3 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, KEYWDS 4 UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.A.RAMELOT,J.R.CORT,R.XIAO,R.SHASTRY,T.B.ACTON,G.T.MONTELIONE, AUTHOR 2 M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 7 24-SEP-14 1R9P 1 JRNL VERSN REVDAT 6 24-FEB-09 1R9P 1 VERSN REVDAT 5 14-NOV-06 1R9P 1 HEADER REVDAT 4 12-JUL-05 1R9P 1 TITLE JRNL REMARK MASTER REVDAT 3 07-DEC-04 1R9P 1 AUTHOR REVDAT 2 23-NOV-04 1R9P 1 SOURCE DBREF SEQADV REVDAT 1 09-NOV-04 1R9P 0 JRNL AUTH T.A.RAMELOT,J.R.CORT,S.GOLDSMITH-FISCHMAN,G.J.KORNHABER, JRNL AUTH 2 R.XIAO,R.SHASTRY,T.B.ACTON,B.HONIG,G.T.MONTELIONE, JRNL AUTH 3 M.A.KENNEDY JRNL TITL SOLUTION NMR STRUCTURE OF THE IRON-SULFUR CLUSTER ASSEMBLY JRNL TITL 2 PROTEIN U (ISCU) WITH ZINC BOUND AT THE ACTIVE SITE. JRNL REF J.MOL.BIOL. V. 344 567 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 15522305 JRNL DOI 10.1016/J.JMB.2004.08.038 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR XPLOR-NIH-2.0.6, AUTOSTRUCTURE 1.1.2 REMARK 3 AUTHORS : SCHWIETERS, C.D., KUSZEWSKI, J.J. TJANDRA, N., REMARK 3 CLORE, G.M. (XPLOR), HUANG, Y.J., MONTELIONE, G.T. REMARK 3 (AUTOSTRUCTURE) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 933 RESTRAINTS. SUMMARY OF EXPERIMENTAL CONSTRAINTS: DISTANCE REMARK 3 RESTRAINTS: TOTAL = 800; INTRA-RESIDUE [I=J] = 12; SEQUENTIAL [(I REMARK 3 -J)=1] = 260; MEDIUM RANGE [1<(I-J)<5] = 185; LONG RANGE [(I-J)>= REMARK 3 5] = 255; HYDROGEN BOND RESTRAINTS = 78 (2 PER H-BOND); ZN REMARK 3 RESTRAINTS 10; NUMBER OF DISTANCE RESTRAINTS PER RESIDUE = 8.2; REMARK 3 DIHEDRAL-ANGLE RESTRAINTS = 133 (66 PHI, 67 PSI); TOTAL NUMBER OF REMARK 3 RESTRAINTS PER RESIDUE = 9.5 (RESIDES 26-123); NUMBER OF LONG REMARK 3 RANGE RESTRAINTS PER RESIDUE = 2.6; NUMBER OF STRUCTURES COMPUTED REMARK 3 = 25; NUMBER OF STRUCTURES USED = 20. AVERAGE DISTANCE VIOLATIONS REMARK 3 >0.0001 ANG = 27.4; AVERAGE R.M.S. DISTANCE VIOLATION = 0.003 REMARK 3 ANG; MAXIMUM NUMBER OF DISTANCE VIOLATIONS 33. AVERAGE DIHEDRAL REMARK 3 ANGLE VIOLATIONS: >0.0001 DEG = 1.0; MAX NUMBER OF DIHEDRAL ANGLE REMARK 3 VIOLATIONS = 3; AVERAGE R.M.S. ANGLE VIOLATION = 0.01 DEG. RMSD REMARK 3 VALUES: BACKBONE ATOMS (N,C,C',O, RESIDUES 26-123) = 0.76 ANG; REMARK 3 ALL HEAVY ATOMS = 1.19 ANG; PROCHECK (RESDIUES 26-123): MOST REMARK 3 FAVORED REGIONS = 78%; ADDITIONAL ALLOWED REGIONS = 18%; REMARK 3 GENEROUSLY ALLOWED REGIONS = 3%; DISALLOWED REGIONS = 0%. REMARK 4 REMARK 4 1R9P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-03. REMARK 100 THE RCSB ID CODE IS RCSB020611. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 20 MM MES, 100 MM NACL, 5 MM REMARK 210 CACL2 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM U-15N, U-13C ISCU IN 20 MM REMARK 210 MES, 100MM NACL, 5 MM CACL2, 10 REMARK 210 MM DTT, 0.02% NAN3; 1 MM U-15N, U REMARK 210 -13C ISCU IN 20 MM MES, 100MM REMARK 210 NACL, 5 MM CACL2, 10 MM DTT, REMARK 210 0.02% NAN3; 1 MM U-15N, U-5%-13C REMARK 210 ISCU IN 20 MM MES, 100MM NACL, 5 REMARK 210 MM CACL2, 10 MM DTT, 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNHA; 4D_13C- REMARK 210 SEPARATED_NOESY; 13C_HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98, X-PLOR XPLOR-NIH- REMARK 210 2.0.6, SPARKY 3.98, TALOS REMARK 210 1999.019.15.47 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS, AUTOMATED REMARK 210 ANALYSIS OF NOESY DATA AND 3D REMARK 210 STRUCTURES REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 25 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY 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, AUTOMATED ANALYSIS OF 3D STRUCTURE. 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 400 REMARK 400 COMPOUND REMARK 400 THIS PROTEIN HAS STOICHIOMETRIC ZINC BOUND. THIS PDB ENTRY REMARK 400 IS A MODEL CALCULATED WITH THE ZINC-BINDING CONSTRAINTS REMARK 400 OBTAINED BY INDIRECT METHODS. PDB ENTRY 1Q48 IS THE SAME REMARK 400 PROTEIN MODELED WITHOUT ZINC-BINDING CONSTRAINTS. 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 SER A 81 H GLU A 83 1.29 REMARK 500 O ASP A 48 H ASN A 50 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 ALA A 2 155.23 56.15 REMARK 500 1 SER A 4 120.40 -37.30 REMARK 500 1 VAL A 7 -152.47 -93.30 REMARK 500 1 ILE A 8 99.95 44.50 REMARK 500 1 HIS A 10 5.52 -150.40 REMARK 500 1 TYR A 11 129.11 59.71 REMARK 500 1 GLU A 12 95.54 -53.17 REMARK 500 1 VAL A 17 -119.55 -114.42 REMARK 500 1 ASP A 21 20.67 -141.21 REMARK 500 1 LYS A 22 10.34 50.64 REMARK 500 1 ASP A 24 -146.61 58.37 REMARK 500 1 SER A 25 -7.79 71.48 REMARK 500 1 ASN A 26 30.12 178.29 REMARK 500 1 PRO A 35 -16.06 -48.85 REMARK 500 1 ASP A 48 -37.32 -172.47 REMARK 500 1 ASP A 49 45.72 -62.73 REMARK 500 1 ASN A 50 51.22 78.50 REMARK 500 1 LYS A 59 101.40 -171.88 REMARK 500 1 SER A 65 -47.02 -166.29 REMARK 500 1 ILE A 67 -19.69 -47.52 REMARK 500 1 LEU A 72 -73.55 -66.65 REMARK 500 1 VAL A 77 50.21 -109.25 REMARK 500 1 ALA A 87 -34.62 -163.27 REMARK 500 1 ILE A 88 -14.08 -45.15 REMARK 500 1 LYS A 89 -173.96 46.68 REMARK 500 1 GLU A 98 62.41 69.72 REMARK 500 1 PRO A 100 158.50 -39.96 REMARK 500 1 VAL A 102 -2.87 -58.04 REMARK 500 1 HIS A 130 96.34 42.65 REMARK 500 1 HIS A 132 173.39 -50.01 REMARK 500 2 SER A 4 -174.45 -53.50 REMARK 500 2 LYS A 6 -89.80 -170.07 REMARK 500 2 VAL A 7 -47.84 -138.43 REMARK 500 2 HIS A 10 111.65 57.69 REMARK 500 2 ASN A 13 60.74 -155.73 REMARK 500 2 ASN A 16 161.34 53.29 REMARK 500 2 VAL A 17 -92.74 -102.96 REMARK 500 2 LEU A 20 -132.06 -117.11 REMARK 500 2 LYS A 22 -38.44 62.48 REMARK 500 2 LYS A 23 45.40 -73.80 REMARK 500 2 ASP A 48 -32.72 178.19 REMARK 500 2 ASP A 49 45.25 -62.45 REMARK 500 2 ASN A 50 45.92 81.09 REMARK 500 2 ILE A 53 94.38 -56.48 REMARK 500 2 LYS A 59 116.64 -160.94 REMARK 500 2 ALA A 66 4.37 -58.51 REMARK 500 2 ALA A 87 -34.03 -147.27 REMARK 500 2 ILE A 88 -28.11 -33.42 REMARK 500 2 LYS A 89 153.10 63.11 REMARK 500 2 GLU A 98 73.04 70.21 REMARK 500 REMARK 500 THIS ENTRY HAS 517 RAMACHANDRAN OUTLIERS. 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 1 ZN A 135 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 37 SG REMARK 620 2 HIS A 105 NE2 114.6 REMARK 620 3 CYS A 63 SG 104.3 117.2 REMARK 620 4 CYS A 106 SG 105.5 115.7 97.5 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 135 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Q48 RELATED DB: PDB REMARK 900 STRUCTURE CALCULATED WITHOUT ZINC BINDING RESTRAINTS. REMARK 900 RELATED ID: 5842 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFTS FOR H. INFLUENZAE ISCU. DBREF 1R9P A 1 126 UNP Q57074 NIFU_HAEIN 1 126 SEQADV 1R9P LEU A 127 UNP Q57074 CLONING ARTIFACT SEQADV 1R9P GLU A 128 UNP Q57074 CLONING ARTIFACT SEQADV 1R9P HIS A 129 UNP Q57074 EXPRESSION TAG SEQADV 1R9P HIS A 130 UNP Q57074 EXPRESSION TAG SEQADV 1R9P HIS A 131 UNP Q57074 EXPRESSION TAG SEQADV 1R9P HIS A 132 UNP Q57074 EXPRESSION TAG SEQADV 1R9P HIS A 133 UNP Q57074 EXPRESSION TAG SEQADV 1R9P HIS A 134 UNP Q57074 EXPRESSION TAG SEQRES 1 A 134 MET ALA TYR SER GLU LYS VAL ILE ASP HIS TYR GLU ASN SEQRES 2 A 134 PRO ARG ASN VAL GLY SER LEU ASP LYS LYS ASP SER ASN SEQRES 3 A 134 VAL GLY THR GLY MET VAL GLY ALA PRO ALA CYS GLY ASP SEQRES 4 A 134 VAL MET GLN LEU GLN ILE LYS VAL ASP ASP ASN GLY ILE SEQRES 5 A 134 ILE GLU ASP ALA LYS PHE LYS THR TYR GLY CYS GLY SER SEQRES 6 A 134 ALA ILE ALA SER SER SER LEU ILE THR GLU TRP VAL LYS SEQRES 7 A 134 GLY LYS SER LEU GLU GLU ALA GLY ALA ILE LYS ASN SER SEQRES 8 A 134 GLN ILE ALA GLU GLU LEU GLU LEU PRO PRO VAL LYS VAL SEQRES 9 A 134 HIS CYS SER ILE LEU ALA GLU ASP ALA ILE LYS ALA ALA SEQRES 10 A 134 ILE ALA ASP TYR LYS ALA LYS GLN GLY LEU GLU HIS HIS SEQRES 11 A 134 HIS HIS HIS HIS HET ZN A 135 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 SER A 65 VAL A 77 1 13 HELIX 2 2 SER A 81 GLY A 86 1 6 HELIX 3 3 ILE A 88 GLU A 98 1 11 HELIX 4 4 LYS A 103 LYS A 124 1 22 SHEET 1 A 3 VAL A 27 ALA A 34 0 SHEET 2 A 3 ASP A 39 VAL A 47 -1 O LEU A 43 N GLY A 30 SHEET 3 A 3 ILE A 53 TYR A 61 -1 O LYS A 57 N GLN A 44 LINK ZN ZN A 135 SG CYS A 37 1555 1555 2.40 LINK ZN ZN A 135 NE2 HIS A 105 1555 1555 2.03 LINK ZN ZN A 135 SG CYS A 63 1555 1555 2.38 LINK ZN ZN A 135 SG CYS A 106 1555 1555 2.41 SITE 1 AC1 4 CYS A 37 CYS A 63 HIS A 105 CYS A 106 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 - p 24 2 Bytes