Header list of 1rhx.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 14-NOV-03 1RHX
TITLE HIGH-RESOLUTION NMR STRUCTURE OF A PUTATIVE SULFUR TRANSFERASE
TITLE 2 (TM0979) FROM THERMOTOGA MARITIMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN TM0979;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DSRH, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 2 JCSG, PROTEIN STRUCTURE INITIATIVE, PSI, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.PETI,T.HERRMANN,K.WUTHRICH,JOINT CENTER FOR STRUCTURAL GENOMICS
AUTHOR 2 (JCSG)
REVDAT 5 02-MAR-22 1RHX 1 REMARK
REVDAT 4 28-JUL-10 1RHX 1 HEADER TITLE KEYWDS
REVDAT 3 24-FEB-09 1RHX 1 VERSN
REVDAT 2 12-APR-05 1RHX 1 JRNL
REVDAT 1 21-DEC-04 1RHX 0
JRNL AUTH W.PETI,T.HERRMANN,O.ZAGNITKO,S.K.GRZECHNIK,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE CONSERVED HYPOTHETICAL PROTEIN TM0979
JRNL TITL 2 FROM THERMOTOGA MARITIMA.
JRNL REF PROTEINS V. 59 387 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15723348
JRNL DOI 10.1002/PROT.20352
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, DYANA 6.0
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RHX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020756.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313; 313
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 50 MM NACL; 50 MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM U-15N TM0979; 10 MM U
REMARK 210 -15N/13C TM0979
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, XEASY 1
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 : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 2 ASP A 77 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 5 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 TYR A 49 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 TYR A 72 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 15 ASP A 77 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 17 LEU A 78 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 18 ASP A 77 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
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 LEU A 5 136.14 171.18
REMARK 500 1 VAL A 6 47.74 -145.22
REMARK 500 1 TYR A 8 36.97 -144.09
REMARK 500 1 ASP A 11 38.42 -150.26
REMARK 500 1 VAL A 14 -50.70 163.71
REMARK 500 1 GLU A 15 42.20 -149.64
REMARK 500 1 LYS A 16 -72.33 -177.75
REMARK 500 1 GLU A 25 38.38 -84.53
REMARK 500 1 GLN A 32 -107.76 27.61
REMARK 500 1 ALA A 38 38.28 -79.81
REMARK 500 1 LEU A 39 42.67 174.16
REMARK 500 1 LEU A 42 -153.50 -154.94
REMARK 500 1 LYS A 66 35.96 -81.93
REMARK 500 1 LEU A 79 -100.84 -72.29
REMARK 500 1 LYS A 84 38.33 -155.62
REMARK 500 1 PHE A 85 37.48 -154.13
REMARK 500 2 LEU A 5 123.72 -171.13
REMARK 500 2 TYR A 8 37.89 -150.81
REMARK 500 2 ASP A 11 38.06 -149.94
REMARK 500 2 VAL A 14 -33.27 164.62
REMARK 500 2 GLU A 15 -14.20 -141.05
REMARK 500 2 LYS A 16 -60.33 -145.95
REMARK 500 2 GLN A 32 -106.34 28.81
REMARK 500 2 ALA A 38 39.62 -83.56
REMARK 500 2 LEU A 39 49.70 -177.82
REMARK 500 2 LEU A 42 -172.61 -170.65
REMARK 500 2 GLU A 80 98.47 -66.36
REMARK 500 2 GLU A 83 59.46 -162.54
REMARK 500 2 LYS A 84 37.74 -142.73
REMARK 500 2 PHE A 85 51.05 -177.41
REMARK 500 3 VAL A 6 52.00 -145.24
REMARK 500 3 TYR A 8 37.79 -146.55
REMARK 500 3 VAL A 14 -49.51 164.00
REMARK 500 3 GLU A 15 23.72 -140.10
REMARK 500 3 LYS A 16 -60.81 -171.51
REMARK 500 3 SER A 21 91.14 -177.73
REMARK 500 3 GLU A 25 38.75 -87.26
REMARK 500 3 GLN A 32 -109.08 36.90
REMARK 500 3 ALA A 38 38.55 -83.80
REMARK 500 3 LEU A 39 60.62 174.02
REMARK 500 3 GLU A 40 -160.98 -121.49
REMARK 500 3 GLU A 41 41.26 -109.44
REMARK 500 3 ARG A 58 35.24 -98.58
REMARK 500 3 LYS A 84 36.50 -167.28
REMARK 500 3 PHE A 85 39.05 -169.44
REMARK 500 4 VAL A 6 60.62 -158.00
REMARK 500 4 TYR A 8 37.10 -148.70
REMARK 500 4 VAL A 14 -48.82 164.70
REMARK 500 4 LYS A 16 -65.25 -164.79
REMARK 500 4 SER A 21 91.17 164.35
REMARK 500
REMARK 500 THIS ENTRY HAS 350 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 86 GLY A 87 2 149.18
REMARK 500 ILE A 86 GLY A 87 3 145.41
REMARK 500 GLY A 81 GLU A 82 4 -145.08
REMARK 500 GLU A 82 GLU A 83 4 -141.14
REMARK 500 ILE A 86 GLY A 87 4 147.60
REMARK 500 GLY A 9 THR A 10 5 -148.32
REMARK 500 ILE A 86 GLY A 87 5 140.40
REMARK 500 ILE A 86 GLY A 87 6 147.97
REMARK 500 GLY A 9 THR A 10 7 -147.47
REMARK 500 ILE A 86 GLY A 87 7 148.21
REMARK 500 ILE A 86 GLY A 87 8 132.22
REMARK 500 GLY A 9 THR A 10 11 -146.23
REMARK 500 GLY A 9 THR A 10 12 -149.55
REMARK 500 GLY A 9 THR A 10 13 -140.71
REMARK 500 ILE A 86 GLY A 87 13 139.93
REMARK 500 GLY A 9 THR A 10 15 -143.73
REMARK 500 ILE A 86 GLY A 87 15 142.34
REMARK 500 ILE A 86 GLY A 87 16 142.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 3 TYR A 72 0.12 SIDE CHAIN
REMARK 500 4 ARG A 20 0.11 SIDE CHAIN
REMARK 500 4 TYR A 72 0.07 SIDE CHAIN
REMARK 500 6 ARG A 58 0.09 SIDE CHAIN
REMARK 500 7 ARG A 20 0.08 SIDE CHAIN
REMARK 500 7 PHE A 85 0.09 SIDE CHAIN
REMARK 500 8 ARG A 58 0.15 SIDE CHAIN
REMARK 500 9 ARG A 20 0.08 SIDE CHAIN
REMARK 500 9 ARG A 58 0.08 SIDE CHAIN
REMARK 500 11 ARG A 20 0.11 SIDE CHAIN
REMARK 500 12 TYR A 72 0.08 SIDE CHAIN
REMARK 500 12 PHE A 75 0.08 SIDE CHAIN
REMARK 500 13 ARG A 58 0.09 SIDE CHAIN
REMARK 500 14 TYR A 72 0.08 SIDE CHAIN
REMARK 500 15 ARG A 20 0.11 SIDE CHAIN
REMARK 500 15 TYR A 49 0.10 SIDE CHAIN
REMARK 500 15 TYR A 72 0.07 SIDE CHAIN
REMARK 500 17 TYR A 72 0.08 SIDE CHAIN
REMARK 500 18 ARG A 58 0.08 SIDE CHAIN
REMARK 500 18 TYR A 72 0.08 SIDE CHAIN
REMARK 500 19 ARG A 20 0.16 SIDE CHAIN
REMARK 500 19 ARG A 58 0.10 SIDE CHAIN
REMARK 500 20 ARG A 58 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 282848 RELATED DB: TARGETDB
DBREF 1RHX A 1 87 UNP Q9X074 Q9X074_THEMA 1 87
SEQRES 1 A 87 MET ALA LEU VAL LEU VAL LYS TYR GLY THR ASP HIS PRO
SEQRES 2 A 87 VAL GLU LYS LEU LYS ILE ARG SER ALA LYS ALA GLU ASP
SEQRES 3 A 87 LYS ILE VAL LEU ILE GLN ASN GLY VAL PHE TRP ALA LEU
SEQRES 4 A 87 GLU GLU LEU GLU THR PRO ALA LYS VAL TYR ALA ILE LYS
SEQRES 5 A 87 ASP ASP PHE LEU ALA ARG GLY TYR SER GLU GLU ASP SER
SEQRES 6 A 87 LYS VAL PRO LEU ILE THR TYR SER GLU PHE ILE ASP LEU
SEQRES 7 A 87 LEU GLU GLY GLU GLU LYS PHE ILE GLY
HELIX 1 1 LYS A 16 SER A 21 1 6
HELIX 2 2 ASN A 33 ALA A 38 5 6
HELIX 3 3 LYS A 52 ALA A 57 1 6
HELIX 4 4 THR A 71 GLU A 80 1 10
SHEET 1 A 2 ALA A 50 ILE A 51 0
SHEET 2 A 2 LEU A 69 ILE A 70 1 O ILE A 70 N ALA A 50
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 2 2 Bytes