Header list of 2hjj.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 30-JUN-06 2HJJ TITLE SOLUTION NMR STRUCTURE OF PROTEIN YKFF FROM ESCHERICHIA COLI. TITLE 2 NORTHEAST STRUCTURAL GENOMICS TARGET ER397. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN YKFF; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 83333; SOURCE 4 STRAIN: K12; SOURCE 5 GENE: YKFF; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MGK; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: ER397-21.1 KEYWDS ER397, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), PROTEIN KEYWDS 2 STRUCTURE INITIATIVE., PSI-2, STRUCTURAL GENOMICS, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.V.T.SWAPNA,J.M.ARAMINI,L.ZHAO,K.CUNNINGHAM,H.JANJUA,L.-C.MA,R.XIAO, AUTHOR 2 M.C.BARAN,T.B.ACTON,J.LIU,B.ROST,G.T.MONTELIONE,NORTHEAST STRUCTURAL AUTHOR 3 GENOMICS CONSORTIUM (NESG) REVDAT 3 13-JUL-11 2HJJ 1 VERSN REVDAT 2 24-FEB-09 2HJJ 1 VERSN REVDAT 1 29-AUG-06 2HJJ 0 JRNL AUTH G.V.T.SWAPNA,J.M.ARAMINI,L.ZHAO,K.CUNNINGHAM,H.JANJUA, JRNL AUTH 2 L.-C.MA,R.XIAO,M.C.BARAN,T.B.ACTON,J.LIU,B.ROST, JRNL AUTH 3 G.T.MONTELIONE JRNL TITL SOLUTION NMR STRUCTURE OF PROTEIN YKFF FROM ESCHERICHIA JRNL TITL 2 COLI. NORTHEAST STRUCTURAL GENOMICS TARGET ER397. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AUTOASSIGN 2.1.1, XPLOR-NIH 2.11.2, AUTOSTRUCTURE REMARK 3 2.1.1, CNS 1.1 REMARK 3 AUTHORS : ZIMMERMAN, MOSELEY, MONTELIONE (AUTOASSIGN), CLORE REMARK 3 ET AL (XPLOR-NIH), HUANG & MONTELIONE REMARK 3 (AUTOSTRUCTURE), BRUNGER ET AL (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1044 CONFORMATIONALLY- REMARK 3 RESTRICTING NOE-DERIVED DISTANCE REMARK 3 CONSTRAINTS, 72 DIHEDRAL ANGLE CONSTRAINTS, AND 52 HYDROGEN REMARK 3 BOND CONSTRAINTS (17.7 CONSTRAINTS PER RESIDUE, 5.3 LONG RANGE REMARK 3 CONSTRAINTS PER RESIDUE, COMPUTED FOR RESIDUES 10 TO 75 BY PSVS REMARK 3 1.3). STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING REMARK 3 AUTOSTRUCTURE (XPLOR-NIH). AFTER A FINAL XPLOR CALCULATION USING REMARK 3 THE CONSTRAINTS DERIVED FROM REMARK 3 AUTOSTRUCTURE, THE 20 LOWEST ENERGY STRUCTURES OUT OF 100 WERE REMARK 3 FURTHER REFINED BY RESTRAINED MOLECULAR DYNAMICS/ENERGY REMARK 3 MINIMIZATION IN EXPLICIT WATER (CNS). THE UNSTRUCTURED N- AND C- REMARK 3 TERMINI OF THE PROTEIN WERE INCLUDED IN ALL STRUCTURE CALCULATIONS REMARK 3 BUT HAVE BEEN OMITTED FROM THIS DEPOSITION. REMARK 4 REMARK 4 2HJJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-06. REMARK 100 THE RCSB ID CODE IS RCSB038415. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 100 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.95 MM U-13C,15N-ER397, 5MM REMARK 210 CACL2, 100MM NACL, 20MM NH4OAC, REMARK 210 10MM DTT, 0.02% NAN3, PH 5.5, 5% REMARK 210 D2O / 95% H2O; 0.95 MM U-13C,15N- REMARK 210 ER397, 5MM CACL2, 100MM NACL, REMARK 210 20MM NH4OAC, 10MM DTT, 0.02% REMARK 210 NAN3, PH 5.5, 100% D2O; 0.95 MM REMARK 210 5%-13C,U-15N-ER397, 5MM CACL2, REMARK 210 100MM NACL, 20MM NH4OAC, 10MM REMARK 210 DTT, 0.02% NAN3, PH 5.5, 5% D2O / REMARK 210 95% H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HNHA; HIGH REMARK 210 RESOLUTION CH-HSQC REMARK 210 (STEREOSPECIFIC ASSIGNMENT OF REMARK 210 VAL/LEU METHYLS); 3D GFT BACKBONE REMARK 210 EXPTS; 3D HCCH-COSY AND HCCH- REMARK 210 TOCSYS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.1C, TOPSPIN 1.3, AGNUS REMARK 210 2.0, PDBSTAT 4.1, PSVS 1.3 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 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING GFT AND TRIPLE REMARK 210 RESONANCE NMR SPECTROSCOPY. AUTOMATED BACKBONE ASSIGNMENTS WERE REMARK 210 MADE FROM THE GFT DATA USING AUTOASSIGN, AND THE ASSIGNMENTS WERE REMARK 210 COMPLETED MANUALLY. AUTOMATIC NOESY ASSIGNMENTS AS WELL AS REMARK 210 DISTANCE AND HYDROGEN BOND CONSTRAINTS WERE DETERMINED USING REMARK 210 AUTOSTRUCTURE. DIHEDRAL ANGLE CONSTRAINTS WERE DETERMINED USING REMARK 210 TALOS. COMPLETENESS OF NMR ASSIGNMENTS (EXCLUDING C-TERMINAL REMARK 210 HHHHHH): BACKBONE, 95.3%, SIDE CHAIN, 93.9%, AROMATICS, 100%, REMARK 210 STEREOSPECIFIC METHYL, 90.9%. FINAL STRUCTURE QUALITY FACTORS REMARK 210 (FOR RESIDUES 10 TO 75, PSVS 1.3), WHERE ORDERED RESIDUES [S(PHI) REMARK 210 + S(PSI) > 1.8] COMPRISE 11-67,72-74: (A) RMSD (ORDERED RESIDUES) REMARK 210 : BB, 0.5, HEAVY ATOM, 1.1. (B) RAMACHANDRAN STATISTICS FOR REMARK 210 ORDERED RESIDUES: MOST FAVORED, 85.9%, ADDITIONALLY ALLOWED, REMARK 210 13.8%, GENEROUSLY ALLOWED, 0.2%, DISALLOWED, 0.1%. (C) PROCHECK REMARK 210 SCORES FOR ORDERED RESIDUES (RAW/Z-): PHI-PSI, -0.45/-1.46, ALL, REMARK 210 -0.38/-2.25. (D) MOLPROBITY CLASH SCORE (RAW/Z-): 29.98/-3.62. REMARK 210 (E) RPF SCORES FOR GOODNESS OF FIT TO NOESY DATA (ALL RESIDUES): REMARK 210 RECALL, 0.956, PRECISION, 0.934, F-MEASURE, 0.945, DP-SCORE, REMARK 210 0.848. 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 MET A 1 REMARK 465 THR A 2 REMARK 465 GLN A 3 REMARK 465 SER A 4 REMARK 465 VAL A 5 REMARK 465 LEU A 6 REMARK 465 LEU A 7 REMARK 465 PRO A 8 REMARK 465 PRO A 9 REMARK 465 THR A 76 REMARK 465 ALA A 77 REMARK 465 THR A 78 REMARK 465 ARG A 79 REMARK 465 LEU A 80 REMARK 465 GLU A 81 REMARK 465 HIS A 82 REMARK 465 HIS A 83 REMARK 465 HIS A 84 REMARK 465 HIS A 85 REMARK 465 HIS A 86 REMARK 465 HIS A 87 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 TRP A 50 125.54 -172.30 REMARK 500 1 ARG A 73 -84.35 -60.21 REMARK 500 2 ASP A 31 70.72 57.26 REMARK 500 2 ASP A 43 -166.04 -102.90 REMARK 500 2 ASP A 58 34.02 -143.01 REMARK 500 2 THR A 69 66.48 -101.73 REMARK 500 2 SER A 70 -51.70 80.37 REMARK 500 3 ASP A 43 -164.57 -104.02 REMARK 500 3 ARG A 73 -70.40 -58.60 REMARK 500 4 SER A 70 -64.73 -108.25 REMARK 500 4 ARG A 73 -74.16 -49.81 REMARK 500 5 ASP A 32 99.80 -68.03 REMARK 500 5 ASP A 43 -166.71 -100.28 REMARK 500 6 ASP A 31 -62.90 77.48 REMARK 500 6 ASP A 32 78.56 38.70 REMARK 500 6 SER A 70 -37.41 84.35 REMARK 500 7 GLN A 33 52.60 -146.57 REMARK 500 7 SER A 70 -61.83 -120.44 REMARK 500 8 PHE A 37 145.13 -176.31 REMARK 500 9 ASP A 32 95.54 -57.59 REMARK 500 9 TRP A 53 -169.13 -79.36 REMARK 500 9 SER A 70 -54.98 -134.66 REMARK 500 10 ASP A 32 99.93 -64.95 REMARK 500 10 SER A 70 -55.44 -144.91 REMARK 500 11 ARG A 73 -6.25 -48.79 REMARK 500 11 THR A 74 5.73 -68.87 REMARK 500 12 SER A 70 66.72 -159.09 REMARK 500 14 TRP A 53 -158.95 -93.90 REMARK 500 14 PHE A 55 34.73 -79.34 REMARK 500 14 SER A 70 -27.05 80.22 REMARK 500 15 ASP A 32 95.97 -64.78 REMARK 500 15 SER A 70 56.48 -147.68 REMARK 500 16 ASP A 58 59.02 -142.11 REMARK 500 16 SER A 70 -55.59 -149.59 REMARK 500 17 ASP A 31 67.66 62.59 REMARK 500 17 TRP A 53 -95.25 -80.26 REMARK 500 17 ASN A 54 -35.80 -162.10 REMARK 500 17 THR A 69 61.85 -102.89 REMARK 500 17 SER A 70 -51.63 78.18 REMARK 500 18 ASP A 32 83.51 -62.30 REMARK 500 18 GLN A 33 71.31 -119.46 REMARK 500 18 ASP A 58 25.93 -141.03 REMARK 500 18 SER A 70 -53.75 -148.77 REMARK 500 19 ASP A 43 -168.91 -104.17 REMARK 500 19 TRP A 53 -92.66 -77.39 REMARK 500 19 ASN A 54 -37.78 -175.58 REMARK 500 19 PRO A 57 5.35 -68.59 REMARK 500 19 SER A 70 -38.13 167.32 REMARK 500 20 ASP A 32 99.33 -63.18 REMARK 500 20 TRP A 53 -167.41 -75.62 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ER397 RELATED DB: TARGETDB DBREF 2HJJ A 1 79 UNP P75677 YKFF_ECOLI 1 79 SEQADV 2HJJ LEU A 80 UNP P75677 CLONING ARTIFACT SEQADV 2HJJ GLU A 81 UNP P75677 CLONING ARTIFACT SEQADV 2HJJ HIS A 82 UNP P75677 EXPRESSION TAG SEQADV 2HJJ HIS A 83 UNP P75677 EXPRESSION TAG SEQADV 2HJJ HIS A 84 UNP P75677 EXPRESSION TAG SEQADV 2HJJ HIS A 85 UNP P75677 EXPRESSION TAG SEQADV 2HJJ HIS A 86 UNP P75677 EXPRESSION TAG SEQADV 2HJJ HIS A 87 UNP P75677 EXPRESSION TAG SEQRES 1 A 87 MET THR GLN SER VAL LEU LEU PRO PRO GLY PRO PHE THR SEQRES 2 A 87 ARG ARG GLN ALA GLN ALA VAL THR THR THR TYR SER ASN SEQRES 3 A 87 ILE THR LEU GLU ASP ASP GLN GLY SER HIS PHE ARG LEU SEQRES 4 A 87 VAL VAL ARG ASP THR GLU GLY ARG MET VAL TRP ARG ALA SEQRES 5 A 87 TRP ASN PHE GLU PRO ASP ALA GLY GLU GLY LEU ASN ARG SEQRES 6 A 87 TYR ILE ARG THR SER GLY ILE ARG THR ASP THR ALA THR SEQRES 7 A 87 ARG LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 THR A 13 TYR A 24 1 12 HELIX 2 2 ASP A 58 ARG A 68 1 11 SHEET 1 A 3 ILE A 27 GLU A 30 0 SHEET 2 A 3 ARG A 38 ARG A 42 -1 O VAL A 40 N THR A 28 SHEET 3 A 3 MET A 48 TRP A 53 -1 O TRP A 50 N VAL A 41 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 25 2 Bytes