Header list of 1te4.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 24-MAY-04 1TE4
TITLE SOLUTION STRUCTURE OF MTH187. ONTARIO CENTRE FOR STRUCTURAL PROTEOMICS
TITLE 2 TARGET MTH0187_1_111; NORTHEAST STRUCTURAL GENOMICS TARGET TT740
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED PROTEIN MTH187;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 GENE: MT0187;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-15B;
SOURCE 9 OTHER_DETAILS: THE PROTEIN WAS PURIFIED ON A NICKEL COLUMN.
KEYWDS MTH187, METHANOBACTERIUM THERMOAUTOTROPHICUM, STRUCTURAL PROTEOMICS,
KEYWDS 2 HEAT-LIKE REPEAT, STRUCTURAL GENOMICS, OCSP, NESG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR I.GIGNAC,O.JULIEN,A.YEE,C.H.ARROWSMITH,S.M.GAGNE,NORTHEAST STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (NESG)
REVDAT 6 02-MAR-22 1TE4 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1TE4 1 VERSN
REVDAT 4 10-OCT-06 1TE4 1 JRNL
REVDAT 3 25-JAN-05 1TE4 1 AUTHOR KEYWDS
REVDAT 2 12-OCT-04 1TE4 1 KEYWDS REMARK TITLE
REVDAT 1 13-JUL-04 1TE4 0
JRNL AUTH O.JULIEN,I.GIGNAC,A.HUTTON,A.YEE,C.H.ARROWSMITH,S.M.GAGNE
JRNL TITL MTH187 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM HAS THREE
JRNL TITL 2 HEAT-LIKE REPEATS.
JRNL REF J.BIOMOL.NMR V. 35 149 2006
JRNL REFN ISSN 0925-2738
JRNL PMID 16819590
JRNL DOI 10.1007/S10858-006-0029-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2546 CONSTRAINTS: 2363 NOE-DERIVED DISTANCE RESTRAINTS, 47 FROM
REMARK 3 COUPLING CONSTANTS, 127 DIHEDRAL ANGLE RESTRAINTS AND 9 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1TE4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022574.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 321.2
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 0.06
REMARK 210 PRESSURE : 101.3 KPA
REMARK 210 SAMPLE CONTENTS : 0.47 MM MTH187 U-15N, 25 MM
REMARK 210 POTASSIUM PHOSPHATE, 22 MM CHAPS,
REMARK 210 10 MM NACL, 0.5 MM DSS, 90% H2O,
REMARK 210 10% D2O; 0.47 MM MTH187 U-15N,
REMARK 210 13C, 25 MM POTASSIUM PHOSPHATE,
REMARK 210 22 MM CHAPS, 10 MM NACL, 0.5 MM
REMARK 210 DSS, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-TOCSY-HSQC; 15N-NOESY-HSQC;
REMARK 210 CBCA(CO)NH; HNCACB; HNCO; HCCH-
REMARK 210 TOCSY; HN(CA)CO; HCA(CO)N; HN(CO)
REMARK 210 CA; CC(CO)NH; HCACO
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
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: 15N-TOCSY-HSQC ACQUIRED AT 500MHZ, MIX=100MS; 15N-NOESY
REMARK 210 -HSQC ACQUIRED AT 800MHZ, MIX=100MS; OTHERS ACQUIRED AT 600MHZ
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 1-40
REMARK 465 RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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: 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 ALA A 2 146.82 66.08
REMARK 500 1 VAL A 8 104.72 -175.71
REMARK 500 1 ARG A 9 19.02 59.49
REMARK 500 1 ASP A 11 -10.89 72.41
REMARK 500 1 SER A 13 -24.69 -156.79
REMARK 500 1 ALA A 15 -67.67 -94.87
REMARK 500 1 ARG A 18 96.43 -174.75
REMARK 500 1 MET A 19 -43.16 -133.70
REMARK 500 1 ASP A 21 -59.29 -170.14
REMARK 500 2 ALA A 2 76.01 -111.61
REMARK 500 2 ASP A 3 82.98 51.34
REMARK 500 2 GLU A 4 -63.39 -163.12
REMARK 500 2 ASP A 11 -3.86 68.31
REMARK 500 2 SER A 13 -18.85 -164.39
REMARK 500 2 LEU A 16 -17.09 -46.94
REMARK 500 2 ARG A 18 100.34 -173.47
REMARK 500 2 GLN A 50 35.02 -74.67
REMARK 500 3 ASP A 3 -71.14 -92.90
REMARK 500 3 VAL A 8 -141.20 49.60
REMARK 500 3 SER A 13 7.49 -160.87
REMARK 500 3 ARG A 18 -7.86 -176.39
REMARK 500 3 ASP A 21 -79.55 61.31
REMARK 500 4 ALA A 2 14.57 55.81
REMARK 500 4 GLU A 4 -86.12 62.45
REMARK 500 4 LYS A 6 -18.99 -167.90
REMARK 500 4 TRP A 7 21.68 -161.48
REMARK 500 4 SER A 13 -75.61 -168.80
REMARK 500 4 ALA A 15 -69.50 -96.15
REMARK 500 5 ALA A 2 -87.61 64.43
REMARK 500 5 GLU A 4 -168.62 -78.03
REMARK 500 5 ASN A 5 109.34 -55.91
REMARK 500 5 LYS A 6 -30.26 -139.06
REMARK 500 5 VAL A 8 -40.05 -164.78
REMARK 500 5 ARG A 9 -21.48 -173.85
REMARK 500 5 ASP A 11 -49.18 77.24
REMARK 500 5 VAL A 12 92.86 -67.68
REMARK 500 5 ALA A 15 -67.32 -95.58
REMARK 500 5 ARG A 18 122.48 -172.05
REMARK 500 5 ASP A 21 -4.99 65.99
REMARK 500 5 THR A 110 -61.13 -100.22
REMARK 500 6 ASP A 3 -83.54 63.06
REMARK 500 6 GLU A 4 85.35 -69.12
REMARK 500 6 ASN A 5 -63.32 179.35
REMARK 500 6 LYS A 6 -80.05 65.23
REMARK 500 6 ARG A 9 -75.41 67.32
REMARK 500 6 ARG A 10 161.40 -48.20
REMARK 500 6 ASP A 11 -5.65 73.33
REMARK 500 6 VAL A 12 -62.88 -138.04
REMARK 500 6 PRO A 26 -29.57 -38.16
REMARK 500 6 THR A 110 -63.49 -121.59
REMARK 500
REMARK 500 THIS ENTRY HAS 366 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TT740 RELATED DB: TARGETDB
DBREF 1TE4 A 1 111 UNP O26289 O26289_METTH 1 111
SEQADV 1TE4 MET A -19 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 GLY A -18 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 SER A -17 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 SER A -16 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A -15 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A -14 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A -13 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A -12 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A -11 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A -10 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 SER A -9 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 SER A -8 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 GLY A -7 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 LEU A -6 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 VAL A -5 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 PRO A -4 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 ARG A -3 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 GLY A -2 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 SER A -1 UNP O26289 EXPRESSION TAG
SEQADV 1TE4 HIS A 0 UNP O26289 EXPRESSION TAG
SEQRES 1 A 131 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 131 LEU VAL PRO ARG GLY SER HIS MET ALA ASP GLU ASN LYS
SEQRES 3 A 131 TRP VAL ARG ARG ASP VAL SER THR ALA LEU SER ARG MET
SEQRES 4 A 131 GLY ASP GLU ALA PHE GLU PRO LEU LEU GLU SER LEU SER
SEQRES 5 A 131 ASN GLU ASP TRP ARG ILE ARG GLY ALA ALA ALA TRP ILE
SEQRES 6 A 131 ILE GLY ASN PHE GLN ASP GLU ARG ALA VAL GLU PRO LEU
SEQRES 7 A 131 ILE LYS LEU LEU GLU ASP ASP SER GLY PHE VAL ARG SER
SEQRES 8 A 131 GLY ALA ALA ARG SER LEU GLU GLN ILE GLY GLY GLU ARG
SEQRES 9 A 131 VAL ARG ALA ALA MET GLU LYS LEU ALA GLU THR GLY THR
SEQRES 10 A 131 GLY PHE ALA ARG LYS VAL ALA VAL ASN TYR LEU GLU THR
SEQRES 11 A 131 HIS
HELIX 1 1 GLU A 25 SER A 32 5 8
HELIX 2 2 ARG A 37 ILE A 46 1 10
HELIX 3 3 GLU A 52 LEU A 61 1 10
HELIX 4 4 PHE A 68 ILE A 80 1 13
HELIX 5 5 GLU A 83 ALA A 93 1 11
HELIX 6 6 PHE A 99 TYR A 107 1 9
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