Header list of 1rkn.pdb file
Complete list - v 10 2 Bytes
HEADER HYDROLASE 22-NOV-03 1RKN
TITLE SOLUTION STRUCTURE OF 1-110 FRAGMENT OF STAPHYLOCOCCAL NUCLEASE WITH
TITLE 2 G88W MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMONUCLEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-110;
COMPND 5 SYNONYM: STAPHYLOCOCCAL NUCLEASE, TNASE;
COMPND 6 EC: 3.1.31.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS STAPHYLOCOCCAL NUCLEASE, FOLDING, G88W110, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR D.S.LIU,Y.G.FENG,K.Q.YE,L.SHAN,J.F.WANG
REVDAT 4 10-NOV-21 1RKN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1RKN 1 VERSN
REVDAT 2 17-JUL-07 1RKN 1 JRNL
REVDAT 1 07-DEC-04 1RKN 0
JRNL AUTH T.XIE,D.LIU,Y.FENG,L.SHAN,J.F.WANG
JRNL TITL FOLDING STABILITY AND COOPERATIVITY OF THE THREE FORMS OF
JRNL TITL 2 1-110 RESIDUES FRAGMENT OF STAPHYLOCOCCAL NUCLEASE
JRNL REF BIOPHYS.J. V. 92 2090 2007
JRNL REFN ISSN 0006-3495
JRNL PMID 17172296
JRNL DOI 10.1529/BIOPHYSJ.106.092155
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 702 LONG AND MEDIUM RANGE NOE RESTRAINTS, AND 169 PHY AND PSI
REMARK 3 DIHEDRAL ANGLE RESTRAINTS DRIVING FROM PROGRAME TALOS.
REMARK 4
REMARK 4 1RKN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020841.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-2MM G88W110-15N,13C LABELED;
REMARK 210 50MM ACETATE BUFFER, DSS, NAN3;
REMARK 210 90% H2O, 10% D2O; 1-2MM G88W110-
REMARK 210 13C LABELED; 50MM ACETATE BUFFER,
REMARK 210 DSS, NAN3; 100% D2O; 1-2MM
REMARK 210 G88W110-15N LABELED; 50MM
REMARK 210 ACETATE BUFFER, DSS, NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCA(CO)NH; HNCACB; HNCO; HNCA;
REMARK 210 HN(CO)CA; HNHA; HBHA(CO)NH; 3D_
REMARK 210 13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHB; HN(CA)CO;
REMARK 210 CCONH; HCCONH; HCCH-TOCSY; HNCA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 O LEU A 25 H MET A 32 1.58
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 ILE A 18 -76.07 -102.52
REMARK 500 1 ASP A 21 -66.26 -96.64
REMARK 500 1 LEU A 36 171.73 -47.19
REMARK 500 1 LEU A 38 91.37 -56.34
REMARK 500 1 ASP A 40 -167.53 -123.97
REMARK 500 1 GLU A 43 -13.31 84.09
REMARK 500 1 LYS A 45 -135.28 -62.28
REMARK 500 1 PRO A 47 -98.31 -100.60
REMARK 500 1 LYS A 49 54.54 171.67
REMARK 500 1 TYR A 54 -35.30 -135.85
REMARK 500 1 ALA A 58 -65.37 -91.41
REMARK 500 1 ARG A 81 88.29 -67.53
REMARK 500 1 LYS A 84 -68.69 -134.69
REMARK 500 1 TYR A 85 24.90 -169.72
REMARK 500 1 ALA A 90 164.61 173.02
REMARK 500 1 ALA A 102 -82.47 -54.53
REMARK 500 1 LEU A 108 98.91 42.24
REMARK 500 2 LYS A 9 110.59 63.83
REMARK 500 2 LYS A 16 173.17 179.87
REMARK 500 2 ILE A 18 -75.76 -53.30
REMARK 500 2 LYS A 28 28.27 49.18
REMARK 500 2 LEU A 36 -82.03 170.29
REMARK 500 2 LEU A 37 100.30 41.01
REMARK 500 2 LEU A 38 119.08 59.40
REMARK 500 2 GLU A 43 -43.79 69.28
REMARK 500 2 PRO A 47 83.36 -54.91
REMARK 500 2 PRO A 56 -19.11 -48.79
REMARK 500 2 ALA A 58 -65.40 -90.51
REMARK 500 2 ARG A 81 78.18 -63.55
REMARK 500 2 LYS A 84 -67.05 -138.44
REMARK 500 2 TYR A 85 25.33 -172.68
REMARK 500 2 ALA A 90 172.89 175.28
REMARK 500 2 TYR A 91 41.70 -141.78
REMARK 500 3 LYS A 16 173.23 178.99
REMARK 500 3 ILE A 18 -72.15 -102.71
REMARK 500 3 LEU A 36 -150.87 163.87
REMARK 500 3 LEU A 37 -78.67 72.89
REMARK 500 3 LEU A 38 92.89 -67.47
REMARK 500 3 GLU A 43 -60.19 77.03
REMARK 500 3 PRO A 47 35.94 -63.58
REMARK 500 3 LYS A 49 41.12 173.30
REMARK 500 3 TYR A 54 -35.61 -135.19
REMARK 500 3 GLU A 57 -16.45 -48.82
REMARK 500 3 ALA A 58 -62.31 -90.52
REMARK 500 3 GLU A 75 49.76 -86.89
REMARK 500 3 ARG A 81 65.18 -63.51
REMARK 500 3 ASP A 83 78.34 -108.26
REMARK 500 3 LYS A 84 -72.02 65.11
REMARK 500 3 TYR A 85 15.87 -144.94
REMARK 500 3 ARG A 87 108.39 154.87
REMARK 500
REMARK 500 THIS ENTRY HAS 219 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RKN A 1 110 UNP P00644 NUC_STAAU 83 192
SEQADV 1RKN TRP A 88 UNP P00644 GLY 170 ENGINEERED MUTATION
SEQRES 1 A 110 ALA THR SER THR LYS LYS LEU HIS LYS GLU PRO ALA THR
SEQRES 2 A 110 LEU ILE LYS ALA ILE ASP GLY ASP THR VAL LYS LEU MET
SEQRES 3 A 110 TYR LYS GLY GLN PRO MET THR PHE ARG LEU LEU LEU VAL
SEQRES 4 A 110 ASP THR PRO GLU THR LYS HIS PRO LYS LYS GLY VAL GLU
SEQRES 5 A 110 LYS TYR GLY PRO GLU ALA SER ALA PHE THR LYS LYS MET
SEQRES 6 A 110 VAL GLU ASN ALA LYS LYS ILE GLU VAL GLU PHE ASP LYS
SEQRES 7 A 110 GLY GLN ARG THR ASP LYS TYR GLY ARG TRP LEU ALA TYR
SEQRES 8 A 110 ILE TYR ALA ASP GLY LYS MET VAL ASN GLU ALA LEU VAL
SEQRES 9 A 110 ARG GLN GLY LEU ALA LYS
HELIX 1 1 PHE A 61 ALA A 69 1 9
SHEET 1 A 6 GLN A 30 ARG A 35 0
SHEET 2 A 6 THR A 22 TYR A 27 -1 N LEU A 25 O MET A 32
SHEET 3 A 6 GLU A 10 THR A 13 -1 N THR A 13 O MET A 26
SHEET 4 A 6 ILE A 72 VAL A 74 -1 O VAL A 74 N GLU A 10
SHEET 5 A 6 TYR A 93 ALA A 94 -1 O TYR A 93 N GLU A 73
SHEET 6 A 6 LYS A 97 MET A 98 -1 O LYS A 97 N ALA A 94
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 - v 10 2 Bytes