Header list of 1lkn.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 25-APR-02 1LKN
TITLE SOLUTION NMR STRUCTURE OF PROTEIN TM_1112 FROM THERMOTOGA MARITIMA.
TITLE 2 ONTARIO CENTRE FOR STRUCTURAL PROTEOMICS TARGET TM1112_1_89;
TITLE 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET VT74.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TM1112;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM1112;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3(MAGIC GOLD);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BETA BARREL, STRUCTURAL GENOMICS, OCSP, NESG, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.XIA,A.YEE,A.SEMESI,C.H.ARROWSMITH,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (NESG)
REVDAT 5 23-FEB-22 1LKN 1 REMARK
REVDAT 4 24-FEB-09 1LKN 1 VERSN
REVDAT 3 25-JAN-05 1LKN 1 AUTHOR KEYWDS
REVDAT 2 12-OCT-04 1LKN 1 KEYWDS REMARK TITLE
REVDAT 1 24-JUN-03 1LKN 0
JRNL AUTH Y.XIA,A.YEE,A.SEMESI,C.H.ARROWSMITH
JRNL TITL SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN TM1112
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, ARIA BASED ON XPLOR3.851
REMARK 3 AUTHORS : F. DELAGLIO (NMRPIPE), M. NILGES, A.T. BRUNGER
REMARK 3 (ARIA BASED ON XPLOR3.851)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2619 RESTRAINTS, IN WHICH
REMARK 3 2508 ARE NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 111 ARE DIHEDRAL ANGLE RESTRAINTS FROM TALOS
REMARK 3 ANALYSIS AND HNHA
REMARK 3 EXPERIMENT.
REMARK 4
REMARK 4 1LKN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000016032.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20UM ZN2+
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM TM1112 U-15N,13C; 25MM
REMARK 210 PHOSPHATE BUFFER NA; 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C/15N-SEPARATED_NOESY;
REMARK 210 3D_15N/15N-SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY SPARKY 3, ARIA BASED ON
REMARK 210 XPLOR3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED,BACK CALCULATED DATA
REMARK 210 AGREE WITH EXPERIMENTAL NOESY
REMARK 210 SPECTRUM,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 TYR A 42 H HIS A 85 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 10 TYR A 35 CE1 TYR A 35 CZ 0.078
REMARK 500 10 TYR A 35 CZ TYR A 35 CE2 -0.081
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 PRO A 10 -30.62 -37.37
REMARK 500 1 SER A 17 88.02 -28.68
REMARK 500 1 PRO A 22 -179.73 -53.74
REMARK 500 1 VAL A 28 62.97 -53.73
REMARK 500 1 SER A 29 -155.86 -94.93
REMARK 500 1 ASP A 36 26.16 -159.45
REMARK 500 1 THR A 37 141.56 170.31
REMARK 500 1 ASN A 38 93.61 -58.40
REMARK 500 1 GLU A 45 100.79 177.15
REMARK 500 1 LYS A 62 110.82 47.65
REMARK 500 1 PRO A 81 121.23 -34.53
REMARK 500 1 ASN A 87 73.24 -164.07
REMARK 500 2 PRO A 10 -30.13 -39.47
REMARK 500 2 SER A 17 88.65 -29.59
REMARK 500 2 PRO A 22 179.24 -49.90
REMARK 500 2 VAL A 28 45.57 -63.57
REMARK 500 2 GLU A 45 100.68 -169.55
REMARK 500 2 LYS A 62 115.77 49.78
REMARK 500 2 LEU A 72 93.39 -45.18
REMARK 500 2 PRO A 81 118.45 -35.07
REMARK 500 2 ASN A 87 54.19 -157.50
REMARK 500 3 GLU A 2 39.13 -174.50
REMARK 500 3 SER A 17 89.51 -26.22
REMARK 500 3 PRO A 22 -171.55 -52.38
REMARK 500 3 VAL A 28 43.22 26.54
REMARK 500 3 ASP A 36 20.14 -152.35
REMARK 500 3 GLU A 45 106.29 -172.03
REMARK 500 3 LYS A 62 106.71 58.57
REMARK 500 3 ASN A 87 73.43 -151.27
REMARK 500 4 PRO A 10 -29.64 -39.71
REMARK 500 4 SER A 17 88.66 -29.10
REMARK 500 4 PRO A 22 174.54 -48.32
REMARK 500 4 VAL A 28 47.65 -64.34
REMARK 500 4 ASP A 36 17.73 -152.09
REMARK 500 4 GLU A 45 137.05 179.16
REMARK 500 4 LYS A 62 111.59 25.77
REMARK 500 4 LEU A 72 91.53 -46.84
REMARK 500 4 PRO A 81 117.79 -35.01
REMARK 500 4 ASN A 87 60.56 -170.86
REMARK 500 5 SER A 17 88.28 -29.50
REMARK 500 5 PRO A 22 -174.62 -51.16
REMARK 500 5 VAL A 28 59.11 -49.06
REMARK 500 5 SER A 29 -158.65 -95.51
REMARK 500 5 ASP A 36 21.43 -150.15
REMARK 500 5 ASN A 38 97.12 -69.92
REMARK 500 5 GLU A 45 104.65 -171.87
REMARK 500 5 LYS A 62 110.82 30.96
REMARK 500 5 LYS A 70 107.96 -44.09
REMARK 500 5 PRO A 81 107.89 -42.37
REMARK 500 5 ASN A 87 57.05 -150.10
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: VT74 RELATED DB: TARGETDB
DBREF 1LKN A 1 89 UNP Q9X0J6 Q9X0J6_THEMA 1 89
SEQRES 1 A 89 MET GLU VAL LYS ILE GLU LYS PRO THR PRO GLU LYS LEU
SEQRES 2 A 89 LYS GLU LEU SER VAL GLU LYS TRP PRO ILE TRP GLU LYS
SEQRES 3 A 89 GLU VAL SER GLU PHE ASP TRP TYR TYR ASP THR ASN GLU
SEQRES 4 A 89 THR CYS TYR ILE LEU GLU GLY LYS VAL GLU VAL THR THR
SEQRES 5 A 89 GLU ASP GLY LYS LYS TYR VAL ILE GLU LYS GLY ASP LEU
SEQRES 6 A 89 VAL THR PHE PRO LYS GLY LEU ARG CYS ARG TRP LYS VAL
SEQRES 7 A 89 LEU GLU PRO VAL ARG LYS HIS TYR ASN LEU PHE
HELIX 1 1 THR A 9 LEU A 16 1 8
HELIX 2 2 SER A 17 TRP A 21 5 5
SHEET 1 A 8 ILE A 23 LYS A 26 0
SHEET 2 A 8 ARG A 73 LEU A 88 -1 N VAL A 82 O LYS A 26
SHEET 3 A 8 GLU A 30 TYR A 34 -1 O PHE A 31 N TRP A 76
SHEET 4 A 8 ARG A 73 LEU A 88 -1 O CYS A 74 N TRP A 33
SHEET 5 A 8 GLU A 39 THR A 52 -1 N THR A 40 O ASN A 87
SHEET 6 A 8 LYS A 57 GLU A 61 -1 O TYR A 58 N VAL A 50
SHEET 7 A 8 GLU A 39 THR A 52 -1 O VAL A 48 N ILE A 60
SHEET 8 A 8 LEU A 65 THR A 67 -1 N VAL A 66 O CYS A 41
CISPEP 1 THR A 9 PRO A 10 9 10.19
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 - b 23 2 Bytes