Header list of 1xjs.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 24-SEP-04 1XJS TITLE SOLUTION STRUCTURE OF IRON-SULFUR CLUSTER ASSEMBLY PROTEIN ISCU FROM TITLE 2 BACILLUS SUBTILIS, WITH ZINC BOUND AT THE ACTIVE SITE. NORTHEAST TITLE 3 STRUCTURAL GENOMICS CONSORTIUM TARGET SR17 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NIFU-LIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IRON-SULFUR CLUSTER ASSEMBLY PROTEIN ISCU; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 GENE: NIFU; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D KEYWDS SR17, AUTOSTRUCTURE, IRON-SULFUR, ZINC, NORTHEAST STRUCTURAL GENOMICS KEYWDS 2 CONSORTIUM, NESG, NIFU-LIKE, PROTEIN STRUCTURE INITIATIVE, KEYWDS 3 STRUCTURAL GENOMICS, PSI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR G.J.KORNHABER,G.V.T.SWAPNA,T.A.RAMELOT,J.R.CORT,M.A.KENNEDY, AUTHOR 2 G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 4 02-MAR-22 1XJS 1 REMARK LINK REVDAT 3 24-FEB-09 1XJS 1 VERSN REVDAT 2 08-MAR-05 1XJS 1 AUTHOR REVDAT 1 04-JAN-05 1XJS 0 JRNL AUTH G.J.KORNHABER,G.V.T.SWAPNA,T.A.RAMELOT,J.R.CORT,M.A.KENNEDY, JRNL AUTH 2 G.T.MONTELIONE JRNL TITL SOLUTION STRUCTURE OF IRON-SULFUR CLUSTER ASSEMBLY PROTEIN JRNL TITL 2 ISCU FROM BACILLUS SUBTILIS, WITH ZINC BOUND AT THE ACTIVE JRNL TITL 3 SITE. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET SR17. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AUTOASSIGN 1.9, X-PLOR 2.0.6, CNS 1.0 REMARK 3 AUTHORS : ZIMMERMAN, MOSELEY AND MONTELIONE (AUTOASSIGN), REMARK 3 SCHWIETERS, ET AL. (X-PLOR), BRUNGER, ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XJS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000030434. 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 : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 100MM POTASSIUM PHOSPHATE, 200MM REMARK 210 GLYCEROL, 1MM DTT, 0.02% NAN3, 5% REMARK 210 D2O, 95% H2O; 20MM SODIUM REMARK 210 PHOSPHATE, 50MM SODIUM CHLORIDE, REMARK 210 10MM DTT, 0.02% NAN3, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D-TOCSYS; 13C,1H-HSQC; 15N,1H REMARK 210 -HSQC; 15N,1H-HSQC, 2D REMARK 210 HOMONUCLEAR NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; H/D EXCHANGE REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AUTOSTRUCTURE 2.0.0, TALOS 2.1, REMARK 210 HYPER & PDBSTAT 3.2 AND 3.32, REMARK 210 NMRPIPE 2.1, SPARKY 3.106 REMARK 210 METHOD USED : MINIMAL CONSTRAINT STRUCTURE REMARK 210 CONTAINED 492 CONFORMATIONALLY REMARK 210 RESTRICTING NOE-DERIVED DISTANCE REMARK 210 CONSTRAINTS, 108 HYDROGEN BOND REMARK 210 CONSTRAINTS, AND 197 DIHEDRAL REMARK 210 ANGLE CONSTRAINTS. THIS RESULTED REMARK 210 IN 5.9 CONSTRAINTS PER RESIDUE REMARK 210 AND 1.2 LONG RANGE CONSTRAINTS REMARK 210 PER RESIDUE. STRUCTURE REMARK 210 DETERMINATION WAS PERFORMED WITH REMARK 210 THE FOLLOWING STEPS: REMARK 210 AUTOSTRUCTURE-DYANA WAS USED TO REMARK 210 IDENTIFY DISTANCE CONSTRAINTS. REMARK 210 THESE DISTANCE CONSTRAINTS WERE REMARK 210 USED AS INPUT INTO A SIMULATED REMARK 210 ANNEALING WITH XPLOR-NIH. THE REMARK 210 TOP TEN STRUCTURES WERE ENERGY REMARK 210 MINIMIZED WITH WATER USING CNS. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 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: REMARK 210 THIS STRUCTURE WAS DETERMINED USING A SELECTIVE ISOTOPIC LABELING REMARK 210 STRATEGY INVOLVING THE PROTONATION OF SPECIFIC RESIDUES IN A REMARK 210 PERDEUTERATED BACKGROUND. REMARK 210 PROTONATED ATOMS INCLUDE: REMARK 210 ILE HD1, VAL HG*, LEU HD*. REMARK 210 ALL TYR AND PHE SIDE-CHAINS ARE PROTONATED. IN ADDITION TO THE REMARK 210 ATOMS MENTIONED ABOVE, EXCHANGEABLE ATOMS WERE PROTONATED. 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 HA LYS A 25 HA GLU A 62 1.20 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 LYS A 25 94.33 72.64 REMARK 500 1 ASP A 30 -72.88 -152.98 REMARK 500 1 SER A 31 -71.89 -113.88 REMARK 500 1 ASP A 52 72.54 -109.72 REMARK 500 1 ASP A 54 20.48 -142.66 REMARK 500 1 ILE A 55 -162.60 -127.37 REMARK 500 1 LYS A 83 -168.60 -127.55 REMARK 500 1 ASP A 84 -165.98 -120.15 REMARK 500 1 LYS A 102 -80.95 169.94 REMARK 500 1 GLU A 103 109.50 -166.20 REMARK 500 1 TYR A 104 142.05 -173.67 REMARK 500 1 ALA A 141 -175.84 68.86 REMARK 500 1 GLU A 143 -104.89 60.15 REMARK 500 2 ASN A 6 93.82 -49.93 REMARK 500 2 LEU A 7 -15.49 76.61 REMARK 500 2 ARG A 23 25.97 -162.99 REMARK 500 2 ASN A 24 36.93 -95.83 REMARK 500 2 ASP A 30 -73.35 -141.94 REMARK 500 2 SER A 31 -85.32 -95.26 REMARK 500 2 ASP A 52 67.14 -105.93 REMARK 500 2 LYS A 83 -155.53 -134.12 REMARK 500 2 LYS A 102 -89.00 -163.26 REMARK 500 2 GLU A 103 84.18 177.71 REMARK 500 2 ASP A 106 -78.43 58.10 REMARK 500 2 ALA A 141 178.21 74.43 REMARK 500 2 GLU A 143 -67.64 65.89 REMARK 500 2 GLU A 144 -44.13 -164.56 REMARK 500 3 ASN A 6 -79.70 -148.01 REMARK 500 3 LEU A 7 -43.39 -141.43 REMARK 500 3 LEU A 28 79.22 -115.80 REMARK 500 3 SER A 31 -104.31 -144.56 REMARK 500 3 PRO A 39 -79.88 -16.81 REMARK 500 3 ASP A 43 -71.03 -20.86 REMARK 500 3 ASP A 52 66.33 -114.25 REMARK 500 3 ILE A 55 -164.00 -110.21 REMARK 500 3 GLU A 57 -71.37 -81.70 REMARK 500 3 TYR A 104 141.89 -173.43 REMARK 500 3 LEU A 131 -70.92 -52.95 REMARK 500 3 ALA A 141 155.82 68.15 REMARK 500 3 GLU A 143 117.87 66.73 REMARK 500 3 GLU A 144 -88.30 -78.07 REMARK 500 4 SER A 2 40.11 -150.25 REMARK 500 4 ASN A 6 -76.65 -59.14 REMARK 500 4 ASN A 21 71.23 -117.95 REMARK 500 4 PRO A 22 38.50 -75.85 REMARK 500 4 ASP A 30 -90.85 -141.73 REMARK 500 4 SER A 31 -65.59 -108.39 REMARK 500 4 PRO A 39 40.31 -65.58 REMARK 500 4 THR A 40 -36.69 -178.10 REMARK 500 4 ASP A 54 30.13 -143.15 REMARK 500 REMARK 500 THIS ENTRY HAS 151 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 ZN A 150 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 41 SG REMARK 620 2 ASP A 43 OD1 95.3 REMARK 620 3 ASP A 43 OD2 167.4 76.6 REMARK 620 4 CYS A 66 SG 104.3 158.9 85.3 REMARK 620 5 CYS A 128 SG 86.5 83.7 102.0 89.6 REMARK 620 N 1 2 3 4 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 150 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: SR17 RELATED DB: TARGETDB DBREF 1XJS A 1 147 UNP O32163 NIFU_BACSU 1 147 SEQRES 1 A 147 MET SER PHE ASN ALA ASN LEU ASP THR LEU TYR ARG GLN SEQRES 2 A 147 VAL ILE MET ASP HIS TYR LYS ASN PRO ARG ASN LYS GLY SEQRES 3 A 147 VAL LEU ASN ASP SER ILE VAL VAL ASP MET ASN ASN PRO SEQRES 4 A 147 THR CYS GLY ASP ARG ILE ARG LEU THR MET LYS LEU ASP SEQRES 5 A 147 GLY ASP ILE VAL GLU ASP ALA LYS PHE GLU GLY GLU GLY SEQRES 6 A 147 CYS SER ILE SER MET ALA SER ALA SER MET MET THR GLN SEQRES 7 A 147 ALA ILE LYS GLY LYS ASP ILE GLU THR ALA LEU SER MET SEQRES 8 A 147 SER LYS ILE PHE SER ASP MET MET GLN GLY LYS GLU TYR SEQRES 9 A 147 ASP ASP SER ILE ASP LEU GLY ASP ILE GLU ALA LEU GLN SEQRES 10 A 147 GLY VAL SER LYS PHE PRO ALA ARG ILE LYS CYS ALA THR SEQRES 11 A 147 LEU SER TRP LYS ALA LEU GLU LYS GLY VAL ALA LYS GLU SEQRES 12 A 147 GLU GLY GLY ASN HET ZN A 150 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 LEU A 7 ASN A 21 1 15 HELIX 2 2 CYS A 66 LYS A 81 1 16 HELIX 3 3 ASP A 84 LYS A 102 1 19 HELIX 4 4 LEU A 110 SER A 120 1 11 HELIX 5 5 ARG A 125 VAL A 140 1 16 SHEET 1 A 3 ILE A 32 ASN A 37 0 SHEET 2 A 3 ARG A 44 LYS A 50 -1 O LEU A 47 N VAL A 34 SHEET 3 A 3 ASP A 58 GLU A 64 -1 O GLU A 64 N ARG A 44 LINK SG CYS A 41 ZN ZN A 150 1555 1555 2.47 LINK OD1 ASP A 43 ZN ZN A 150 1555 1555 1.66 LINK OD2 ASP A 43 ZN ZN A 150 1555 1555 1.75 LINK SG CYS A 66 ZN ZN A 150 1555 1555 2.43 LINK SG CYS A 128 ZN ZN A 150 1555 1555 2.59 SITE 1 AC1 4 CYS A 41 ASP A 43 CYS A 66 CYS A 128 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 2 2 Bytes