Header list of 1t3v.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 27-APR-04 1T3V
TITLE THE NMR SOLUTION STRUCTURE OF TM1816
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN;
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: TM1816;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 RIL(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-25B
KEYWDS ALPHA-BETA, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR L.COLUMBUS,W.PETI,T.HERRMANN,T.ETAZADY,H.KLOCK,S.LESLEY,K.WUTHRICH,
AUTHOR 2 JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 02-MAR-22 1T3V 1 REMARK
REVDAT 3 24-FEB-09 1T3V 1 VERSN
REVDAT 2 18-JAN-05 1T3V 1 REMARK
REVDAT 1 14-DEC-04 1T3V 0
JRNL AUTH L.COLUMBUS,W.PETI,T.ETEZADY-ESFARJANI,T.HERRMANN,K.WUTHRICH
JRNL TITL NMR STRUCTURE DETERMINATION OF THE CONSERVED HYPOTHETICAL
JRNL TITL 2 PROTEIN TM1816 FROM THERMOTOGA MARITIMA.
JRNL REF PROTEINS V. 60 552 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15937903
JRNL DOI 10.1002/PROT.20465
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T3V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022278.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHPSHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM TM1816 U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 : DYANA, XWINNMR, XEASY
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 ARG A 71 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 2 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 19 TYR A 113 CB - CG - CD2 ANGL. DEV. = -3.8 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 SER A 15 109.01 -52.99
REMARK 500 1 ARG A 23 48.02 -142.59
REMARK 500 1 ASN A 34 -86.79 54.58
REMARK 500 1 ALA A 38 -51.73 59.13
REMARK 500 1 LEU A 47 39.65 -147.78
REMARK 500 1 GLN A 49 63.36 -168.60
REMARK 500 1 ASP A 50 -105.73 -144.29
REMARK 500 1 VAL A 52 84.43 49.97
REMARK 500 1 LYS A 63 38.42 -84.15
REMARK 500 1 GLU A 66 -53.32 -144.10
REMARK 500 1 ARG A 71 -62.14 -95.08
REMARK 500 1 ILE A 73 -168.16 44.26
REMARK 500 1 SER A 111 -135.03 49.34
REMARK 500 1 TYR A 113 14.82 -151.29
REMARK 500 1 HIS A 121 173.65 54.23
REMARK 500 1 GLU A 122 -73.42 -71.53
REMARK 500 1 HIS A 123 112.17 66.42
REMARK 500 2 LYS A 13 -45.70 80.19
REMARK 500 2 SER A 15 102.34 -33.36
REMARK 500 2 ARG A 23 39.09 -142.79
REMARK 500 2 LYS A 31 -164.21 -126.82
REMARK 500 2 ASN A 34 -82.98 55.28
REMARK 500 2 ASN A 35 34.54 -140.03
REMARK 500 2 ALA A 38 -68.68 54.40
REMARK 500 2 ASP A 50 97.60 -53.44
REMARK 500 2 HIS A 51 26.53 41.76
REMARK 500 2 VAL A 52 55.14 33.12
REMARK 500 2 LYS A 63 38.13 -82.48
REMARK 500 2 GLU A 66 -37.88 -141.56
REMARK 500 2 ARG A 71 -100.50 -97.36
REMARK 500 2 ILE A 73 172.44 -57.96
REMARK 500 2 ASP A 110 69.80 -153.56
REMARK 500 2 GLU A 114 99.24 -43.58
REMARK 500 2 ASP A 117 98.39 -34.13
REMARK 500 2 GLU A 122 71.63 50.34
REMARK 500 3 SER A 15 107.70 -45.79
REMARK 500 3 ARG A 23 45.99 -145.04
REMARK 500 3 ASN A 34 61.12 37.69
REMARK 500 3 ASN A 35 14.40 52.54
REMARK 500 3 ALA A 38 -73.45 54.50
REMARK 500 3 GLN A 49 22.53 -145.05
REMARK 500 3 HIS A 51 -40.04 61.06
REMARK 500 3 HIS A 53 -70.48 -64.23
REMARK 500 3 LYS A 63 36.55 -93.44
REMARK 500 3 GLU A 66 -35.95 -146.70
REMARK 500 3 ARG A 71 -67.56 -100.16
REMARK 500 3 ILE A 73 -174.26 -63.87
REMARK 500 3 SER A 111 152.06 -44.20
REMARK 500 3 VAL A 115 58.75 32.41
REMARK 500 3 HIS A 116 -77.09 57.88
REMARK 500
REMARK 500 THIS ENTRY HAS 375 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 HIS A 120 HIS A 121 1 -141.21
REMARK 500 HIS A 123 HIS A 124 2 140.48
REMARK 500 SER A 111 ASP A 112 3 -147.80
REMARK 500 HIS A 123 HIS A 124 5 138.61
REMARK 500 HIS A 51 VAL A 52 7 -145.64
REMARK 500 SER A 111 ASP A 112 7 148.97
REMARK 500 HIS A 123 HIS A 124 9 148.80
REMARK 500 HIS A 120 HIS A 121 10 -141.22
REMARK 500 HIS A 51 VAL A 52 19 -149.53
REMARK 500 ILE A 40 SER A 41 20 141.90
REMARK 500 HIS A 123 HIS A 124 21 -138.11
REMARK 500 SER A 111 ASP A 112 22 -147.80
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 2 ARG A 23 0.13 SIDE CHAIN
REMARK 500 2 TYR A 26 0.09 SIDE CHAIN
REMARK 500 4 ARG A 75 0.08 SIDE CHAIN
REMARK 500 6 TYR A 103 0.07 SIDE CHAIN
REMARK 500 7 ARG A 23 0.09 SIDE CHAIN
REMARK 500 7 TYR A 113 0.09 SIDE CHAIN
REMARK 500 9 ARG A 23 0.08 SIDE CHAIN
REMARK 500 9 TYR A 103 0.09 SIDE CHAIN
REMARK 500 11 TYR A 103 0.07 SIDE CHAIN
REMARK 500 11 TYR A 113 0.07 SIDE CHAIN
REMARK 500 12 TYR A 103 0.08 SIDE CHAIN
REMARK 500 13 ARG A 71 0.08 SIDE CHAIN
REMARK 500 14 TYR A 113 0.15 SIDE CHAIN
REMARK 500 15 ARG A 23 0.09 SIDE CHAIN
REMARK 500 16 ARG A 71 0.10 SIDE CHAIN
REMARK 500 16 TYR A 113 0.08 SIDE CHAIN
REMARK 500 17 ARG A 23 0.10 SIDE CHAIN
REMARK 500 17 ARG A 71 0.08 SIDE CHAIN
REMARK 500 18 ARG A 11 0.10 SIDE CHAIN
REMARK 500 20 ARG A 75 0.09 SIDE CHAIN
REMARK 500 21 ARG A 23 0.09 SIDE CHAIN
REMARK 500 21 ARG A 76 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 283669 RELATED DB: TARGETDB
DBREF 1T3V A 1 124 UNP Q9X2D6 Q9X2D6_THEMA 1 124
SEQRES 1 A 124 MET ILE ILE ALA ILE PRO VAL SER GLU ASN ARG GLY LYS
SEQRES 2 A 124 ASP SER PRO ILE SER GLU HIS PHE GLY ARG ALA PRO TYR
SEQRES 3 A 124 PHE ALA PHE VAL LYS VAL LYS ASN ASN ALA ILE ALA ASP
SEQRES 4 A 124 ILE SER VAL GLU GLU ASN PRO LEU ALA GLN ASP HIS VAL
SEQRES 5 A 124 HIS GLY ALA VAL PRO ASN PHE VAL LYS GLU LYS GLY ALA
SEQRES 6 A 124 GLU LEU VAL ILE VAL ARG GLY ILE GLY ARG ARG ALA ILE
SEQRES 7 A 124 ALA ALA PHE GLU ALA MET GLY VAL LYS VAL ILE LYS GLY
SEQRES 8 A 124 ALA SER GLY THR VAL GLU GLU VAL VAL ASN GLN TYR LEU
SEQRES 9 A 124 SER GLY GLN LEU LYS ASP SER ASP TYR GLU VAL HIS ASP
SEQRES 10 A 124 HIS HIS HIS HIS GLU HIS HIS
HELIX 1 1 ARG A 11 SER A 15 5 5
HELIX 2 2 HIS A 20 ALA A 24 5 5
HELIX 3 3 GLY A 54 LYS A 61 1 8
HELIX 4 4 GLY A 74 GLU A 82 1 9
HELIX 5 5 THR A 95 SER A 105 1 11
SHEET 1 A 3 PRO A 6 VAL A 7 0
SHEET 2 A 3 TYR A 26 LYS A 31 -1 O TYR A 26 N VAL A 7
SHEET 3 A 3 ILE A 40 GLU A 44 -1 O GLU A 43 N PHE A 27
SHEET 1 B 5 PRO A 6 VAL A 7 0
SHEET 2 B 5 TYR A 26 LYS A 31 -1 O TYR A 26 N VAL A 7
SHEET 3 B 5 ILE A 2 ALA A 4 -1 N ILE A 3 O VAL A 30
SHEET 4 B 5 LEU A 67 VAL A 70 1 O LEU A 67 N ILE A 2
SHEET 5 B 5 LYS A 87 LYS A 90 1 O ILE A 89 N VAL A 68
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