Header list of 4trx.pdb file
Complete list - r 16 2 Bytes
HEADER ELECTRON TRANSPORT 17-DEC-90 4TRX
TITLE HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED RECOMBINANT
TITLE 2 HUMAN THIOREDOXIN IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 33
AUTHOR J.D.FORMAN-KAY,G.M.CLORE,A.M.GRONENBORN
REVDAT 4 16-MAR-22 4TRX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 4TRX 1 VERSN
REVDAT 2 15-JAN-93 4TRX 1 HEADER COMPND
REVDAT 1 15-JAN-92 4TRX 0
JRNL AUTH J.D.FORMAN-KAY,G.M.CLORE,P.T.WINGFIELD,A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED
JRNL TITL 2 RECOMBINANT HUMAN THIOREDOXIN IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 30 2685 1991
JRNL REFN ISSN 0006-2960
JRNL PMID 2001356
JRNL DOI 10.1021/BI00224A017
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.D.FORMAN-KAY,A.M.GRONENBORN,L.E.KAY,P.T.WINGFIELD,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL STUDIES ON THE SOLUTION CONFORMATION OF HUMAN THIOREDOXIN
REMARK 1 TITL 2 USING HETERONUCLEAR 15N-1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 29 1566 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.D.FORMAN-KAY,G.M.CLORE,P.C.DRISCOLL,P.WINGFIELD,
REMARK 1 AUTH 2 F.M.RICHARDS,A.M.GRONENBORN
REMARK 1 TITL A PROTON NUCLEAR MAGNETIC RESONANCE ASSIGNMENT AND SECONDARY
REMARK 1 TITL 2 STRUCTURE DETERMINATION OF RECOMBINANT HUMAN THIOREDOXIN
REMARK 1 REF BIOCHEMISTRY V. 28 7088 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES DETERMINED BY THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD OF M. NILGES, G. M. CLORE, AND A. M. GRONENBORN
REMARK 3 (FEBS LETT. 229, 317 (1988)). THE STRUCTURES ARE BASED
REMARK 3 ON 1983 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE
REMARK 3 MEASUREMENTS; 52 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR
REMARK 3 26 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND
REMARK 3 AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL
REMARK 3 STRUCTURE CALCULATIONS; AND 98 PHI AND 71 PSI BACKBONE
REMARK 3 TORSION ANGLE RESTRAINTS AND 72 CHI1 SIDE-CHAIN TORSION
REMARK 3 ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE
REMARK 3 DATA.
REMARK 3
REMARK 3 A TOTAL OF 33 STRUCTURES WERE CALCULATED. THIS ENTRY
REMARK 3 REPRESENTS THE ENTIRE SET OF 33 STRUCTURES. THE MINIMIZED
REMARK 3 AVERAGE STRUCTURE CAN BE FOUND IN PDB ENTRY 3TRX. THIS
REMARK 3 AVERAGED STRUCTURE IS OBTAINED BY AVERAGING THE COORDINATES
REMARK 3 OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING
REMARK 3 COORDINATES TO RESTRAINED MINIMIZATION.
REMARK 3
REMARK 3 THE NUMBERS IN THE LAST COLUMN OF THIS COORDINATE FILE ARE
REMARK 3 MEANINGLESS.
REMARK 4
REMARK 4 4TRX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179438.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 33
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 1 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 1 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 2 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 2 HIS A 43 CG HIS A 43 ND1 -0.115
REMARK 500 3 TRP A 31 CG TRP A 31 CD2 -0.109
REMARK 500 3 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 4 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 4 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 5 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 5 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 6 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 6 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 7 TRP A 31 CG TRP A 31 CD2 -0.109
REMARK 500 7 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 8 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 8 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 9 TRP A 31 CG TRP A 31 CD2 -0.106
REMARK 500 9 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 10 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 10 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 11 TRP A 31 CG TRP A 31 CD2 -0.106
REMARK 500 11 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 12 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 12 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 13 TRP A 31 CG TRP A 31 CD2 -0.109
REMARK 500 13 HIS A 43 CG HIS A 43 ND1 -0.115
REMARK 500 14 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 14 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 15 TRP A 31 CG TRP A 31 CD2 -0.109
REMARK 500 15 HIS A 43 CG HIS A 43 ND1 -0.115
REMARK 500 16 TRP A 31 CG TRP A 31 CD2 -0.109
REMARK 500 16 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 17 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 17 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 18 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 18 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 19 TRP A 31 CG TRP A 31 CD2 -0.110
REMARK 500 19 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 20 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 20 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 21 TRP A 31 CG TRP A 31 CD2 -0.106
REMARK 500 21 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 22 TRP A 31 CG TRP A 31 CD2 -0.110
REMARK 500 22 HIS A 43 CG HIS A 43 ND1 -0.117
REMARK 500 23 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 23 HIS A 43 CG HIS A 43 ND1 -0.114
REMARK 500 24 TRP A 31 CG TRP A 31 CD2 -0.108
REMARK 500 24 HIS A 43 CG HIS A 43 ND1 -0.116
REMARK 500 25 TRP A 31 CG TRP A 31 CD2 -0.107
REMARK 500 25 HIS A 43 CG HIS A 43 ND1 -0.118
REMARK 500
REMARK 500 THIS ENTRY HAS 66 BOND DEVIATIONS.
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 1 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 1 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 2 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 2 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 3 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 4 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 5 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 5 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 5 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 6 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 6 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 6 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 6 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 7 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 7 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 7 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 7 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 8 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 8 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 8 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 8 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 9 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 9 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 9 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 9 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 10 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 10 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 10 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 10 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 11 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 11 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 11 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 11 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 12 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 12 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 12 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 12 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 13 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 13 TRP A 31 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 129 ANGLE DEVIATIONS.
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 ILE A 5 -178.45 -68.76
REMARK 500 1 GLU A 6 -47.30 -138.32
REMARK 500 1 ILE A 38 31.14 -96.13
REMARK 500 1 LYS A 48 -70.54 -56.10
REMARK 500 1 VAL A 59 35.29 -73.97
REMARK 500 1 ASP A 60 -45.74 -132.68
REMARK 500 1 CYS A 73 124.39 179.64
REMARK 500 1 LYS A 82 8.01 57.88
REMARK 500 1 ALA A 92 34.63 -73.14
REMARK 500 1 GLU A 98 -73.41 -43.17
REMARK 500 2 VAL A 2 152.03 -45.74
REMARK 500 2 GLU A 6 -34.93 -146.47
REMARK 500 2 LYS A 21 153.14 -44.44
REMARK 500 2 CYS A 32 172.04 -47.70
REMARK 500 2 PRO A 40 -13.21 -46.53
REMARK 500 2 VAL A 59 10.74 -69.46
REMARK 500 2 CYS A 62 45.85 -98.99
REMARK 500 2 LYS A 72 22.69 -145.09
REMARK 500 2 GLU A 88 123.50 -170.13
REMARK 500 2 ALA A 92 24.79 -71.21
REMARK 500 2 GLU A 98 -75.25 -44.50
REMARK 500 3 GLU A 6 -35.08 -144.32
REMARK 500 3 LYS A 21 160.85 -44.57
REMARK 500 3 CYS A 32 164.38 -44.18
REMARK 500 3 VAL A 59 20.86 -69.76
REMARK 500 3 CYS A 62 32.36 -95.98
REMARK 500 3 CYS A 73 131.46 179.26
REMARK 500 3 LYS A 82 11.12 51.55
REMARK 500 3 GLU A 95 -17.96 -48.44
REMARK 500 3 GLU A 98 -71.46 -57.02
REMARK 500 4 GLU A 6 -35.88 -142.95
REMARK 500 4 ASP A 20 -18.64 -149.35
REMARK 500 4 LYS A 21 160.44 -43.84
REMARK 500 4 PRO A 40 1.52 -63.34
REMARK 500 4 VAL A 59 47.54 -77.45
REMARK 500 4 ASP A 60 -44.06 -142.38
REMARK 500 4 GLN A 63 -17.91 -48.20
REMARK 500 4 LYS A 72 21.62 -145.32
REMARK 500 4 CYS A 73 144.33 -175.03
REMARK 500 4 LYS A 82 11.93 51.99
REMARK 500 4 GLU A 95 -19.66 -47.01
REMARK 500 4 GLU A 98 -72.63 -46.01
REMARK 500 5 VAL A 2 158.22 -47.93
REMARK 500 5 GLU A 6 -57.04 -130.90
REMARK 500 5 ASP A 20 -29.92 -155.51
REMARK 500 5 LYS A 21 161.52 -42.64
REMARK 500 5 PRO A 34 -10.85 -49.31
REMARK 500 5 ILE A 38 41.88 -93.88
REMARK 500 5 PRO A 40 2.75 -62.62
REMARK 500 5 VAL A 59 21.29 -71.57
REMARK 500
REMARK 500 THIS ENTRY HAS 350 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TRX RELATED DB: PDB
DBREF 4TRX A 2 105 UNP P10599 THIO_HUMAN 1 104
SEQADV 4TRX THR A 74 UNP P10599 MET 73 CONFLICT
SEQRES 1 A 105 MET VAL LYS GLN ILE GLU SER LYS THR ALA PHE GLN GLU
SEQRES 2 A 105 ALA LEU ASP ALA ALA GLY ASP LYS LEU VAL VAL VAL ASP
SEQRES 3 A 105 PHE SER ALA THR TRP CYS GLY PRO CYS LYS MET ILE LYS
SEQRES 4 A 105 PRO PHE PHE HIS SER LEU SER GLU LYS TYR SER ASN VAL
SEQRES 5 A 105 ILE PHE LEU GLU VAL ASP VAL ASP ASP CYS GLN ASP VAL
SEQRES 6 A 105 ALA SER GLU CYS GLU VAL LYS CYS THR PRO THR PHE GLN
SEQRES 7 A 105 PHE PHE LYS LYS GLY GLN LYS VAL GLY GLU PHE SER GLY
SEQRES 8 A 105 ALA ASN LYS GLU LYS LEU GLU ALA THR ILE ASN GLU LEU
SEQRES 9 A 105 VAL
HELIX 1 1 SER A 7 ALA A 18 1 12
HELIX 2 2 CYS A 32 MET A 37 1 6
HELIX 3 3 ILE A 38 HIS A 43 1 6
HELIX 4 4 SER A 44 TYR A 49 1 6
HELIX 5 5 CYS A 62 SER A 67 1 6
HELIX 6 6 LYS A 94 VAL A 105 1 12
SHEET 1 A 5 LYS A 3 GLN A 4 0
SHEET 2 A 5 ILE A 53 ASP A 58 1 O PHE A 54 N LYS A 3
SHEET 3 A 5 VAL A 23 SER A 28 1 O VAL A 24 N LEU A 55
SHEET 4 A 5 THR A 76 LYS A 81 -1 N THR A 76 O PHE A 27
SHEET 5 A 5 GLN A 84 SER A 90 -1 O GLN A 84 N LYS A 81
CISPEP 1 THR A 74 PRO A 75 1 -0.92
CISPEP 2 THR A 74 PRO A 75 2 -0.91
CISPEP 3 THR A 74 PRO A 75 3 -1.00
CISPEP 4 THR A 74 PRO A 75 4 -1.07
CISPEP 5 THR A 74 PRO A 75 5 -1.08
CISPEP 6 THR A 74 PRO A 75 6 -1.34
CISPEP 7 THR A 74 PRO A 75 7 -0.93
CISPEP 8 THR A 74 PRO A 75 8 -1.11
CISPEP 9 THR A 74 PRO A 75 9 -0.79
CISPEP 10 THR A 74 PRO A 75 10 -1.10
CISPEP 11 THR A 74 PRO A 75 11 -1.12
CISPEP 12 THR A 74 PRO A 75 12 -0.81
CISPEP 13 THR A 74 PRO A 75 13 -1.00
CISPEP 14 THR A 74 PRO A 75 14 -0.88
CISPEP 15 THR A 74 PRO A 75 15 -1.07
CISPEP 16 THR A 74 PRO A 75 16 -1.02
CISPEP 17 THR A 74 PRO A 75 17 -0.65
CISPEP 18 THR A 74 PRO A 75 18 -1.02
CISPEP 19 THR A 74 PRO A 75 19 -0.82
CISPEP 20 THR A 74 PRO A 75 20 -0.91
CISPEP 21 THR A 74 PRO A 75 21 -1.13
CISPEP 22 THR A 74 PRO A 75 22 -1.10
CISPEP 23 THR A 74 PRO A 75 23 -0.77
CISPEP 24 THR A 74 PRO A 75 24 -1.13
CISPEP 25 THR A 74 PRO A 75 25 -0.71
CISPEP 26 THR A 74 PRO A 75 26 -0.97
CISPEP 27 THR A 74 PRO A 75 27 -0.92
CISPEP 28 THR A 74 PRO A 75 28 -0.59
CISPEP 29 THR A 74 PRO A 75 29 -1.05
CISPEP 30 THR A 74 PRO A 75 30 -0.97
CISPEP 31 THR A 74 PRO A 75 31 -0.99
CISPEP 32 THR A 74 PRO A 75 32 -0.97
CISPEP 33 THR A 74 PRO A 75 33 -0.86
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 16 2 Bytes