Header list of 2azh.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-SEP-05 2AZH
TITLE SOLUTION STRUCTURE OF IRON-SULFUR CLUSTER ASSEMBLY PROTEIN SUFU 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: SUFU;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ISCU;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YURV;
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, ISCU, SUFU, NIFU-LIKE,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.J.KORNHABER,G.V.T.SWAPNA,T.A.RAMELOT,J.R.CORT,J.M.ARAMINI,
AUTHOR 2 M.A.KENNEDY,G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 4 09-MAR-22 2AZH 1 REMARK LINK
REVDAT 3 28-APR-09 2AZH 1 REMARK
REVDAT 2 24-FEB-09 2AZH 1 VERSN
REVDAT 1 20-SEP-05 2AZH 0
JRNL AUTH G.J.KORNHABER,G.V.T.SWAPNA,T.A.RAMELOT,J.R.CORT,J.M.ARAMINI,
JRNL AUTH 2 M.A.KENNEDY,G.T.MONTELIONE
JRNL TITL SOLUTION NMR STRUCTURE OF ZN-LIGATED FE-S CLUSTER ASSEMBLY
JRNL TITL 2 SCAFFOLD PROTEIN SUFU FROM BACILLUS SUBTILIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AUTOSTRUCTURE-DYANA 1.1.2, XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : HUANG, MONTELIONE ET AL. (AUTOSTRUCTURE-DYANA),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DETERMINATION WAS PERFORMED WITH THE
REMARK 3 FOLLOWING STEPS: RESONANCE ASSIGNMENTS, TORTION ANGLE CONTRAINTS,
REMARK 3 HYDROGEN BONDED PAIRS AND NOESY CROSSPEAK DATA WAS USED AS
REMARK 3 INPUT INTO AUTOSTRUCTURE-DYANA. AUTOSTRUCTURE-DYANA IDENTIFIED
REMARK 3 DISTANCE CONSTRAINTS. THESE DISTANCE CONSTRAINTS WERE USED AS
REMARK 3 INPUT INTO AN XPLOR-NIH SIMULATED ANNEALING. USING CNS THE TOP
REMARK 3 TEN XPLOR-NIH STRUCTURES WERE ENERGY MINIMIZED IN EXPLICIT WATER
REMARK 3 WITH RDC CONSTRAINTS.
REMARK 4
REMARK 4 2AZH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034487.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 20; 20
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 100MM NACL, 50MM SODIUM
REMARK 210 PHOSPHATE; 100MM POTASSIUM
REMARK 210 PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM U-15N, U-13C,
REMARK 210 PERDEUTERATEDSUFU WITH 13C,1H-
REMARK 210 LEU, VAL AND ILE-DELTA METHYLS,
REMARK 210 IN 50MM SODIUM PHOSPHATE, 100MM
REMARK 210 NACL, 1MM DTT, 0.02% NAN3, 5%
REMARK 210 D2O, 95% H2O; 1.0 MM U-15N, U-
REMARK 210 13C, PERDEUTERATED SUFU WITH 13C,
REMARK 210 1H-LEU, VAL AND ILE-DELTA
REMARK 210 METHYLS AND 12C,15N,1H - PHE,TYR
REMARK 210 IN 100MM POTASSIUM PHOSPHATE,
REMARK 210 200MM GLYCEROL, 1MM DTT, 0.02%
REMARK 210 NAN3, 5% D2O, 95% H2O; 1.0 MM U-
REMARK 210 5%13C, U-15N SUFU IN 100MM
REMARK 210 POTASSIUM PHOSPHATE, 200MM
REMARK 210 GLYCEROL, 1MM DTT, 0.02% NAN3, 5%
REMARK 210 D2O, 95% H2O; 0.8 MM U-5%13C, U-
REMARK 210 15N SUFU IN 50MM SODIUM
REMARK 210 PHOSPHATE, 100MM NACL, 1MM DTT,
REMARK 210 0.02% NAN3, 5% HEXAETHYLENE
REMARK 210 GLYCOL MONODODECYL ETHER/N-
REMARK 210 HEXANOL, 90% H2O, 5% D2O; 0.8 MM
REMARK 210 U-5%13C, U-15N SUFU IN 50MM
REMARK 210 SODIUM PHOSPHATE, 100MM NACL,
REMARK 210 1MM DTT, 0.02% NAN3, 3.5%
REMARK 210 PENTAETHYLENE GLYCOL ETHER/N-
REMARK 210 OCTANOL, 91.5% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N-1H HSQC, 2D 13C-1H HSQC,
REMARK 210 3D HNCO, 3D HNCA, 3D HNCOCA, 3D
REMARK 210 HNCACB, 3D HNCOCACB, 3D HCCCONH-
REMARK 210 TOCSY, 3D HCCCONH-TOCSY; 2D HH
REMARK 210 NOESY, 2D 13C-1H HSQC, 2D 15N-1H
REMARK 210 HSQC, 3D 15N-NOESY, 3D 13C-NOESY,
REMARK 210 4D CC NOESY; 2D 15N-1H IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR-NIH 2.0.6, TALOS 2.1,
REMARK 210 NMRPIPE 2.1, AUTOASSIGN 1.9,
REMARK 210 SPARKY 3.2, PDBSTAT 3.2, PALES
REMARK 210 2.1
REMARK 210 METHOD USED : MINIMAL CONSTRAINT STRUCTURE,
REMARK 210 CONTAINED 512 CONFORMATIONALLY
REMARK 210 RESTRICTING NOE-DERIVED DISTANCE
REMARK 210 CONSTRAINTS, 54 HYDROGEN BONDED
REMARK 210 PAIRS, 186 RESIDUAL DIPOLAR
REMARK 210 COUPLING CONSTRAINTS, 197
REMARK 210 DIHEDRAL ANGLE CONSTRAINTS. 7.0
REMARK 210 CONSTRAINTS PER CONFORMATIONALLY
REMARK 210 CONSTRAINED RESIDUE. 1.0 LONG
REMARK 210 RANGE CONSTRAINT PER RESIDUE.
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: 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 HA GLU A 137 HB2 ALA A 141 1.34
REMARK 500 HZ1 LYS A 25 OE2 GLU A 62 1.59
REMARK 500 H ASN A 38 O ASP A 43 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 ALA A 5 -22.88 69.86
REMARK 500 1 ASN A 6 82.28 -60.26
REMARK 500 1 LEU A 7 -39.09 177.32
REMARK 500 1 ARG A 23 -140.18 -85.83
REMARK 500 1 ASN A 24 52.46 -116.91
REMARK 500 1 SER A 31 -85.45 -153.39
REMARK 500 1 ASP A 52 57.19 -91.75
REMARK 500 1 LYS A 81 -18.31 -49.88
REMARK 500 1 LYS A 102 -21.87 85.71
REMARK 500 1 TYR A 104 -110.75 -137.27
REMARK 500 1 ASP A 106 -11.08 -46.72
REMARK 500 1 SER A 120 -14.69 -41.22
REMARK 500 1 VAL A 140 41.93 -172.67
REMARK 500 1 LYS A 142 -10.46 -171.02
REMARK 500 1 GLU A 143 -67.29 71.19
REMARK 500 2 SER A 2 -76.61 66.97
REMARK 500 2 ASN A 4 18.78 -179.15
REMARK 500 2 ALA A 5 -176.20 82.93
REMARK 500 2 ASN A 6 -88.50 -174.13
REMARK 500 2 LEU A 7 -25.76 -143.99
REMARK 500 2 PRO A 22 39.21 -73.93
REMARK 500 2 ASN A 29 79.64 -102.20
REMARK 500 2 ASP A 30 -130.61 -115.80
REMARK 500 2 SER A 31 -71.71 -52.08
REMARK 500 2 THR A 40 23.76 -74.91
REMARK 500 2 CYS A 41 -52.73 -136.22
REMARK 500 2 ASP A 43 -88.45 -157.28
REMARK 500 2 ARG A 44 -179.35 179.63
REMARK 500 2 LYS A 50 95.82 -160.79
REMARK 500 2 ASP A 52 59.35 -90.89
REMARK 500 2 ALA A 59 101.74 -167.74
REMARK 500 2 LYS A 102 -18.54 81.48
REMARK 500 2 TYR A 104 -134.03 -137.03
REMARK 500 2 ASP A 106 -2.86 -58.50
REMARK 500 2 ALA A 141 152.39 91.78
REMARK 500 2 GLU A 143 -88.66 65.81
REMARK 500 3 PHE A 3 -57.93 -137.39
REMARK 500 3 ASN A 4 152.71 64.93
REMARK 500 3 ASN A 6 -82.14 -103.33
REMARK 500 3 PRO A 22 45.97 -78.57
REMARK 500 3 ASN A 24 25.93 -142.24
REMARK 500 3 VAL A 27 93.77 -165.39
REMARK 500 3 ASP A 30 -125.86 -101.48
REMARK 500 3 ASP A 52 59.92 -99.17
REMARK 500 3 ALA A 59 118.04 -160.36
REMARK 500 3 GLU A 64 106.63 -163.15
REMARK 500 3 LYS A 83 -153.04 -134.53
REMARK 500 3 TYR A 104 -101.20 -124.64
REMARK 500 3 SER A 120 -13.23 -42.98
REMARK 500 3 LYS A 121 -0.37 -142.93
REMARK 500
REMARK 500 THIS ENTRY HAS 176 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 OD2 90.6
REMARK 620 3 CYS A 66 SG 113.3 93.5
REMARK 620 4 CYS A 128 SG 112.5 98.9 132.3
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 150
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XJS RELATED DB: PDB
REMARK 900 PREVIOUS REFINEMENT OF NESG TARGET SR17 WITHOUT RESIDUAL DIPOLAR
REMARK 900 COUPLING DATA
REMARK 900 RELATED ID: 6362 RELATED DB: BMRB
REMARK 900 PREVIOUS BMRB DEPOSITION OF SR17 WITHOUT RESIDUAL DIPOLAR COUPLING
REMARK 900 DATA
REMARK 900 RELATED ID: SR17 RELATED DB: TARGETDB
DBREF 2AZH 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 HIS A 18 1 12
HELIX 2 2 ILE A 68 LYS A 81 1 14
HELIX 3 3 ASP A 84 LYS A 102 1 19
HELIX 4 4 LEU A 110 GLN A 117 1 8
HELIX 5 5 ARG A 125 ALA A 141 1 17
SHEET 1 A 3 ILE A 32 ASN A 37 0
SHEET 2 A 3 ARG A 44 LYS A 50 -1 O ILE A 45 N MET A 36
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 2.53
LINK OD2 ASP A 43 ZN ZN A 150 1555 1555 1.62
LINK SG CYS A 66 ZN ZN A 150 1555 1555 2.29
LINK SG CYS A 128 ZN ZN A 150 1555 1555 2.11
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 9 2 Bytes