Header list of 1m7t.pdb file
Complete list - t 27 2 Bytes
HEADER ELECTRON TRANSPORT 22-JUL-02 1M7T
TITLE SOLUTION STRUCTURE AND DYNAMICS OF THE HUMAN-ESCHERICHIA COLI
TITLE 2 THIOREDOXIN CHIMERA: INSIGHTS INTO THERMODYNAMIC STABILITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIMERA OF HUMAN AND E. COLI THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: CHIMERA CONSISTS OF RESIDUES 1-66 FROM HUMAN, RESIDUES
COMPND 6 67-107 FROM E. COLI.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 9606,562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET 11A
KEYWDS CHIMERA, HUMAN, E. COLI, DYNAMICS, STABILITY, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR B.DANGI,A.V.DOBRODUMOV,J.M.LOUIS,A.M.GRONENBORN
REVDAT 3 27-OCT-21 1M7T 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1M7T 1 VERSN
REVDAT 1 25-SEP-02 1M7T 0
JRNL AUTH B.DANGI,A.V.DOBRODUMOV,J.M.LOUIS,A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE HUMAN-ESCHERICHIA
JRNL TITL 2 COLI THIOREDOXIN CHIMERA: INSIGHTS INTO THERMODYNAMIC
JRNL TITL 3 STABILITY
JRNL REF BIOCHEMISTRY V. 41 9376 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12135359
JRNL DOI 10.1021/BI0258501
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, XPLOR
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M7T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016703.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN IN 100 MM SODIUM
REMARK 210 PHOSPHATE BUFFER (PH 7.0), 20 M
REMARK 210 EDTA, 0.02% SODIUM AZIDE, AND 10%
REMARK 210 D2O.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCO; HNCACB; 15N TOCSY-HSQC;
REMARK 210 HCCH-TOCSY; H(CCO)NH-TOCSY; C(CO)
REMARK 210 NH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 600 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SEE PUBLICATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
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 O LEU A 102 H LEU A 106 1.59
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 VAL A 2 144.95 63.87
REMARK 500 1 SER A 50 34.41 36.43
REMARK 500 1 ASN A 51 -41.36 -151.10
REMARK 500 1 ALA A 62 43.35 -95.89
REMARK 500 1 ALA A 87 139.62 -175.96
REMARK 500 2 SER A 28 -168.34 -119.79
REMARK 500 2 SER A 50 49.55 -90.22
REMARK 500 2 ASN A 51 -43.21 -153.23
REMARK 500 2 ALA A 62 41.11 -95.10
REMARK 500 2 ARG A 72 51.22 -151.58
REMARK 500 2 ALA A 87 142.19 -174.16
REMARK 500 2 LEU A 106 93.34 -51.51
REMARK 500 3 VAL A 2 144.42 63.69
REMARK 500 3 SER A 28 -168.94 -119.53
REMARK 500 3 SER A 50 48.45 -93.93
REMARK 500 3 ASN A 51 -41.00 -151.87
REMARK 500 3 ALA A 62 43.47 -96.24
REMARK 500 3 ALA A 87 140.23 -173.18
REMARK 500 3 LEU A 106 99.08 -69.64
REMARK 500 4 SER A 28 -169.44 -115.69
REMARK 500 4 SER A 50 49.06 -88.58
REMARK 500 4 ASN A 51 -41.17 -153.79
REMARK 500 4 ALA A 62 43.68 -95.91
REMARK 500 4 ALA A 87 141.82 -172.26
REMARK 500 5 SER A 28 -167.91 -121.39
REMARK 500 5 SER A 50 43.98 -96.10
REMARK 500 5 ASN A 51 11.37 -156.26
REMARK 500 5 ALA A 62 45.96 -95.17
REMARK 500 5 ARG A 72 54.43 -150.72
REMARK 500 5 ALA A 87 138.91 -175.37
REMARK 500 6 VAL A 2 144.48 63.75
REMARK 500 6 SER A 50 47.26 -93.66
REMARK 500 6 ASN A 51 -42.83 -150.15
REMARK 500 6 ALA A 62 44.22 -94.59
REMARK 500 6 ALA A 87 137.24 -175.07
REMARK 500 6 SER A 94 -178.17 -68.77
REMARK 500 7 SER A 28 -166.64 -122.82
REMARK 500 7 ASN A 51 -41.21 -153.30
REMARK 500 7 ALA A 62 43.34 -96.67
REMARK 500 7 ALA A 87 138.16 -173.17
REMARK 500 7 SER A 94 -177.92 -64.41
REMARK 500 8 SER A 28 -168.76 -121.14
REMARK 500 8 SER A 50 43.16 -78.62
REMARK 500 8 ASN A 51 -29.17 -154.60
REMARK 500 8 ALA A 87 148.94 -177.05
REMARK 500 8 LEU A 106 0.52 -64.61
REMARK 500 9 SER A 50 46.64 -86.55
REMARK 500 9 ASN A 51 -29.96 -154.93
REMARK 500 9 ALA A 62 47.35 -90.55
REMARK 500 9 ALA A 87 149.26 -172.89
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M7T A 1 66 UNP P10599 THIO_HUMAN 0 65
DBREF 1M7T A 67 106 UNP P00274 THIO_ECOLI 68 107
SEQADV 1M7T ALA A 62 UNP P10599 CYS 61 ENGINEERED MUTATION
SEQADV 1M7T VAL A 107 UNP P00274 CLONING ARTIFACT
SEQRES 1 A 107 MET VAL LYS GLN ILE GLU SER LYS THR ALA PHE GLN GLU
SEQRES 2 A 107 ALA LEU ASP ALA ALA GLY ASP LYS LEU VAL VAL VAL ASP
SEQRES 3 A 107 PHE SER ALA THR TRP CYS GLY PRO CYS LYS MET ILE LYS
SEQRES 4 A 107 PRO PHE PHE HIS SER LEU SER GLU LYS TYR SER ASN VAL
SEQRES 5 A 107 ILE PHE LEU GLU VAL ASP VAL ASP ASP ALA GLN ASP VAL
SEQRES 6 A 107 ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU LEU
SEQRES 7 A 107 LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL GLY
SEQRES 8 A 107 ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP ALA
SEQRES 9 A 107 ASN LEU VAL
HELIX 1 1 SER A 7 GLY A 19 1 13
HELIX 2 2 CYS A 32 SER A 50 1 19
HELIX 3 3 VAL A 65 GLY A 70 1 6
HELIX 4 4 SER A 94 LEU A 106 1 13
SHEET 1 A 5 GLN A 4 ILE A 5 0
SHEET 2 A 5 ILE A 53 ASP A 58 1 O GLU A 56 N ILE A 5
SHEET 3 A 5 VAL A 23 SER A 28 1 N ASP A 26 O VAL A 57
SHEET 4 A 5 THR A 76 LYS A 81 -1 O PHE A 80 N VAL A 23
SHEET 5 A 5 GLU A 84 LYS A 89 -1 O LYS A 89 N LEU A 77
SSBOND 1 CYS A 32 CYS A 35 1555 1555 2.03
CISPEP 1 ILE A 74 PRO A 75 1 0.05
CISPEP 2 ILE A 74 PRO A 75 2 -0.01
CISPEP 3 ILE A 74 PRO A 75 3 -0.08
CISPEP 4 ILE A 74 PRO A 75 4 0.15
CISPEP 5 ILE A 74 PRO A 75 5 -0.04
CISPEP 6 ILE A 74 PRO A 75 6 -0.17
CISPEP 7 ILE A 74 PRO A 75 7 0.11
CISPEP 8 ILE A 74 PRO A 75 8 0.54
CISPEP 9 ILE A 74 PRO A 75 9 0.32
CISPEP 10 ILE A 74 PRO A 75 10 -0.01
CISPEP 11 ILE A 74 PRO A 75 11 0.12
CISPEP 12 ILE A 74 PRO A 75 12 0.07
CISPEP 13 ILE A 74 PRO A 75 13 0.16
CISPEP 14 ILE A 74 PRO A 75 14 -0.02
CISPEP 15 ILE A 74 PRO A 75 15 0.23
CISPEP 16 ILE A 74 PRO A 75 16 0.00
CISPEP 17 ILE A 74 PRO A 75 17 0.13
CISPEP 18 ILE A 74 PRO A 75 18 0.04
CISPEP 19 ILE A 74 PRO A 75 19 0.20
CISPEP 20 ILE A 74 PRO A 75 20 0.02
CISPEP 21 ILE A 74 PRO A 75 21 -0.01
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 - t 27 2 Bytes