Header list of 2hh8.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-JUN-06 2HH8 TITLE SOLUTION NMR STRUCTURE OF THE YDFO PROTEIN FROM ESCHERICHIA COLI. TITLE 2 NORTHEAST STRUCTURAL GENOMICS TARGET ER251. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN YDFO; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: ESCHERICHIA COLI O6; SOURCE 5 GENE: YDFO; 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: PET21; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: ER251_21.4 KEYWDS ER251, AUTOSTRUCTURE, NESG, PSI-2, NORTHEAST STRUCTURAL GENOMICS KEYWDS 2 CONSORTIUM, PROTEIN STRUCTURE INITIATIVE, STRUCTURAL GENOMICS, KEYWDS 3 UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.ROSSI,J.R.CORT,C.K.HO,H.JANJUA,K.CUNNINGHAM,L.-C.MA,R.XIAO,J.LIU, AUTHOR 2 M.BARAN,G.V.T.SWAPNA,T.B.ACTON,B.ROST,M.A.KENNEDY,G.T.MONTELIONE, AUTHOR 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 3 09-MAR-22 2HH8 1 REMARK SEQADV REVDAT 2 24-FEB-09 2HH8 1 VERSN REVDAT 1 22-AUG-06 2HH8 0 JRNL AUTH P.ROSSI,J.R.CORT,C.K.HO,H.JANJUA,K.CUNNINGHAM,L.-C.MA, JRNL AUTH 2 R.XIAO,J.LIU,M.BARAN,G.V.T.SWAPNA,T.B.ACTON,B.ROST, JRNL AUTH 3 M.A.KENNEDY,G.T.MONTELIONE JRNL TITL SOLUTION NMR STRUCTURE OF THE YDFO PROTEIN FROM ESCHERICHIA JRNL TITL 2 COLI. NORTHEAST STRUCTURAL GENOMICS TARGET ER251. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, X-PLOR 2.11.2, PSVS 1.3, CNS 1.1, REMARK 3 PROCHECK NMR 3.51, MOLPROBITY 3.01 REMARK 3 AUTHORS : VARIAN INC. (VNMR), CLORE (X-PLOR), BHATTACHARYA, REMARK 3 MONTELIONE (PSVS), BRUNGER (CNS), LASKOWSKI, REMARK 3 MACARTHUR (PROCHECK NMR), LOVELL, RICHARDSON ET. REMARK 3 AL. (MOLPROBITY) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2HH8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-06. REMARK 100 THE DEPOSITION ID IS D_1000038345. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : 0.1 M NACL REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 0.69MM U-13C,15N ER251, 0.02% REMARK 210 NAN3, 10MM DTT, 5MM CACL2, 100MM REMARK 210 NACL, 20MM AMMONIUM ACETATE, 5% REMARK 210 D2O; 0.74MM 5%-13C,U-15N ER251 REMARK 210 0.02% NAN3, 10MM DTT, 5MM CACL2, REMARK 210 100MM NACL, 20MM AMMONIUM REMARK 210 ACETATE, 5% D2O; 0.69MM U-13C, REMARK 210 15N ER251, 0.02% NAN3, 10MM DTT, REMARK 210 5MM CACL2, 100MM NACL, 20MM REMARK 210 AMMONIUM ACETATE, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HCCH-TOCSY, REMARK 210 HCCH-COSY,CCCONH-TOCSY; 3D- REMARK 210 HNCACB, HNCOCACB, HBHACONH, HNCO; REMARK 210 C13_HSQC_NOCT STEREOSPECIFIC VL REMARK 210 ME ASSIGN.; HET-NOE, T1/T1RHO REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, DYANA 1.2, NMRPIPE REMARK 210 2005, SPARKY 3.11, AUTOASSIGN REMARK 210 2.2.1, AUTOSTRUCTURE 2.1.1, REMARK 210 HYPER 2.1, PDBSTAT 4.1 REMARK 210 METHOD USED : NOESY ASSIGNMENTS MADE WITH REMARK 210 ITERATIVE METHOD USING CS, 3J, REMARK 210 HYPER (DIHEDRAL), AND DYANA FOR REMARK 210 SIMULATED ANNEALING MD. REMARK 210 CONVERGED STRUCTURES ARE FURTHER REMARK 210 REFINED USING NIH-XPLOR FOLLOWED REMARK 210 BY CNS IN EXPLICIT WATER SHELL REMARK 210 (NIELGES) . FULL LENGHT SEQUENCE REMARK 210 WAS CARRIED THROUGH THE REMARK 210 REFINEMENT PROTOCOL, THE REMARK 210 DISORDERED REGIONS AND HEXHIS REMARK 210 TAG ARE NOT REPORTED. STRUCTURE REMARK 210 BASED ON 1885 CONSTRAINTS, 788 REMARK 210 LONG RANGE, 142 DIHEDRAL REMARK 210 CONSTRAINTS AND 114 H-BOND REMARK 210 CONSTRAINTS. 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: STRUCTURE DETERMINED BY TRIPLE RESONANCE NMR SPECTROSCOPY. REMARK 210 MONOMER UNDER NMR CONDITIONS. TC = 9.1 +/-0.5 NS (1D T1/T1RHO +/- REMARK 210 FIT STD). COORDINATES REPORTED FROM RESIDUE 7 TO 133 BASED ON REMARK 210 ORDER PARAMETER. AUTOASSIGN USED FOR BACKBONE ASSIGNMENT, REMARK 210 MANUALLY COMPLETED SIDECHAIN. 13C AND 15N NOESY WERE ASSIGNED REMARK 210 WITH AUTOSTRUCTURE. DIHEDRAL ANGLE RESTRAINTS DETERMINED BY REMARK 210 HYPER . ASSIGNMENT STATS (EXCLUDING C-TERM TAG): BACKBONE 96.7%, REMARK 210 SIDECHAIN 83.7%, AROMATIC (SC) 79.8%, VL METHYL STEREOSPECIFIC REMARK 210 100%, UNAMBIGUOS SIDECHAIN NH2 88.9%. STRUCTURE QUALITY FACTOR REMARK 210 PSVS 1.3: ORDERED RESIDUES RANGES ALPHA HELIX (8-22, 26-35, 76- REMARK 210 88, 93-102), B-STRAND (39-43, 48-52, 58-62, 107-111, 116-120, REMARK 210 126-131) [S(PHI)+S(PSI)]>1.8. RMSD 0.5 BB, 1.1 ALL HEAVY ATOMS. REMARK 210 RAMA: 87.4% MOST FAV, 12.5% ADDTL. ALL., 0.0 GEN. ALL.,0.0% REMARK 210 DISALL. PROCHECK (PSI-PHI): -0.17/-0.35 (RAW/Z), PROCHECK (ALL): REMARK 210 -0.15/-0.89 (RAW/Z), MOLPROBITY CLASH: 24.43/-2.67 (RAW/Z) . RPF REMARK 210 SCORES ALL ASSIGNED RESIDUES (FIT OF NOESY PEAKLISTS TO REMARK 210 STRUCTURE): RECALL: 0.965, PRECISION: 0.919, F-MEASURE: 0.942, REMARK 210 DP-SCORE: 0.817. L139F CLONING MUTATION OF E. COLI YDFO GENE REMARK 210 PRESENT. 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 GLU A 2 REMARK 465 GLY A 3 REMARK 465 LEU A 4 REMARK 465 SER A 5 REMARK 465 MET A 6 REMARK 465 LYS A 134 REMARK 465 THR A 135 REMARK 465 THR A 136 REMARK 465 GLN A 137 REMARK 465 ILE A 138 REMARK 465 PHE A 139 REMARK 465 PRO A 140 REMARK 465 ARG A 141 REMARK 465 LEU A 142 REMARK 465 GLU A 143 REMARK 465 HIS A 144 REMARK 465 HIS A 145 REMARK 465 HIS A 146 REMARK 465 HIS A 147 REMARK 465 HIS A 148 REMARK 465 HIS A 149 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 OE1 GLU A 47 HH12 ARG A 97 1.54 REMARK 500 HH21 ARG A 117 OE1 GLU A 130 1.56 REMARK 500 HZ3 LYS A 13 OD2 ASP A 17 1.59 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 HIS A 35 -58.32 -130.63 REMARK 500 1 SER A 38 -91.74 -117.01 REMARK 500 1 ASN A 55 21.46 -160.15 REMARK 500 1 ASP A 56 -73.91 -86.20 REMARK 500 1 LEU A 64 61.35 37.21 REMARK 500 1 LYS A 65 92.31 -68.80 REMARK 500 1 ASN A 66 -44.94 -146.15 REMARK 500 1 ILE A 67 147.17 71.86 REMARK 500 1 VAL A 68 69.98 66.71 REMARK 500 1 SER A 88 -70.26 -78.25 REMARK 500 1 GLU A 90 -12.52 70.26 REMARK 500 1 ILE A 91 -103.21 35.35 REMARK 500 1 ASN A 124 16.58 53.67 REMARK 500 2 HIS A 35 -58.55 -130.85 REMARK 500 2 SER A 38 -94.84 -95.10 REMARK 500 2 ALA A 45 -53.45 72.26 REMARK 500 2 LYS A 54 -64.21 -148.94 REMARK 500 2 ASN A 55 19.21 -167.59 REMARK 500 2 ASP A 56 -73.35 -98.05 REMARK 500 2 LEU A 64 -76.96 -136.80 REMARK 500 2 LYS A 65 -62.07 -161.88 REMARK 500 2 ASN A 66 133.45 -171.29 REMARK 500 2 VAL A 68 154.24 73.01 REMARK 500 2 VAL A 70 134.16 69.88 REMARK 500 2 PHE A 72 32.35 -82.63 REMARK 500 2 GLU A 90 74.57 54.97 REMARK 500 2 ILE A 91 -113.09 -79.13 REMARK 500 3 HIS A 35 -57.29 -130.51 REMARK 500 3 SER A 38 -86.13 -110.49 REMARK 500 3 ALA A 45 -51.12 72.04 REMARK 500 3 ASP A 56 -51.48 78.97 REMARK 500 3 LEU A 64 53.77 -169.58 REMARK 500 3 ASN A 66 88.53 61.78 REMARK 500 3 PHE A 72 34.06 -80.18 REMARK 500 3 ASN A 124 -9.86 77.10 REMARK 500 4 HIS A 35 -61.29 -130.84 REMARK 500 4 SER A 38 -79.26 -97.56 REMARK 500 4 LEU A 53 -164.93 -78.48 REMARK 500 4 LYS A 54 -70.35 -66.38 REMARK 500 4 ASN A 55 15.53 -144.73 REMARK 500 4 ASP A 56 -72.24 -80.41 REMARK 500 4 LYS A 74 86.55 -157.54 REMARK 500 4 ILE A 91 -95.76 -72.49 REMARK 500 5 SER A 38 -85.08 -97.07 REMARK 500 5 HIS A 39 142.47 -174.66 REMARK 500 5 THR A 46 -3.28 -142.39 REMARK 500 5 ASN A 55 35.74 -168.79 REMARK 500 5 ASP A 56 -72.82 -104.64 REMARK 500 5 LEU A 64 -75.69 -110.87 REMARK 500 5 LYS A 65 -64.23 -178.74 REMARK 500 REMARK 500 THIS ENTRY HAS 204 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ER251 RELATED DB: TARGETDB DBREF 2HH8 A 6 141 UNP P76156 YDFO_ECOLI 1 136 SEQADV 2HH8 MET A 1 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 GLU A 2 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 GLY A 3 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 LEU A 4 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 SER A 5 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 PHE A 139 UNP P76156 LEU 134 CLONING ARTIFACT SEQADV 2HH8 LEU A 142 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 GLU A 143 UNP P76156 CLONING ARTIFACT SEQADV 2HH8 HIS A 144 UNP P76156 EXPRESSION TAG SEQADV 2HH8 HIS A 145 UNP P76156 EXPRESSION TAG SEQADV 2HH8 HIS A 146 UNP P76156 EXPRESSION TAG SEQADV 2HH8 HIS A 147 UNP P76156 EXPRESSION TAG SEQADV 2HH8 HIS A 148 UNP P76156 EXPRESSION TAG SEQADV 2HH8 HIS A 149 UNP P76156 EXPRESSION TAG SEQRES 1 A 149 MET GLU GLY LEU SER MET ASP GLN VAL VAL ILE PHE LYS SEQRES 2 A 149 GLN ILE PHE ASP LYS VAL ARG ASN ASP LEU ASN TYR GLN SEQRES 3 A 149 TRP PHE TYR SER GLU LEU LYS ARG HIS ASN VAL SER HIS SEQRES 4 A 149 TYR ILE TYR TYR LEU ALA THR GLU ASN VAL HIS ILE VAL SEQRES 5 A 149 LEU LYS ASN ASP ASN THR VAL LEU LEU LYS GLY LEU LYS SEQRES 6 A 149 ASN ILE VAL SER VAL LYS PHE SER LYS ASP ARG HIS LEU SEQRES 7 A 149 ILE GLU THR THR SER ASN LYS LEU LYS SER ARG GLU ILE SEQRES 8 A 149 THR PHE GLN GLU TYR ARG ARG ASN LEU ALA LYS ALA GLY SEQRES 9 A 149 VAL PHE ARG TRP VAL THR ASN ILE HIS GLU GLN LYS ARG SEQRES 10 A 149 TYR TYR TYR THR PHE ASP ASN SER LEU LEU PHE THR GLU SEQRES 11 A 149 SER ILE GLN LYS THR THR GLN ILE PHE PRO ARG LEU GLU SEQRES 12 A 149 HIS HIS HIS HIS HIS HIS HELIX 1 1 ASP A 7 LEU A 23 1 17 HELIX 2 2 TYR A 25 ASN A 36 1 12 HELIX 3 3 ASP A 75 ARG A 89 1 15 HELIX 4 4 THR A 92 ALA A 103 1 12 SHEET 1 A 6 THR A 58 LYS A 62 0 SHEET 2 A 6 ASN A 48 VAL A 52 -1 N ILE A 51 O VAL A 59 SHEET 3 A 6 HIS A 39 TYR A 43 -1 N TYR A 43 O ASN A 48 SHEET 4 A 6 ARG A 107 ASN A 111 -1 O TRP A 108 N TYR A 42 SHEET 5 A 6 LYS A 116 TYR A 120 -1 O TYR A 118 N VAL A 109 SHEET 6 A 6 LEU A 126 SER A 131 -1 O LEU A 127 N TYR A 119 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