HEADER ELECTRON TRANSPORT 19-MAR-90 2TRX
TITLE CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT 1.68
TITLE 2 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.KATTI,D.M.LEMASTER,H.EKLUND
REVDAT 6 29-NOV-17 2TRX 1 HELIX
REVDAT 5 13-JUL-11 2TRX 1 VERSN
REVDAT 4 24-FEB-09 2TRX 1 VERSN
REVDAT 3 01-APR-03 2TRX 1 JRNL
REVDAT 2 15-JAN-93 2TRX 1 HEADER COMPND
REVDAT 1 15-OCT-91 2TRX 0
JRNL AUTH S.K.KATTI,D.M.LEMASTER,H.EKLUND
JRNL TITL CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT
JRNL TITL 2 1.68 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 212 167 1990
JRNL REFN ISSN 0022-2836
JRNL PMID 2181145
JRNL DOI 10.1016/0022-2836(90)90313-B
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.HOLMGREN,B.-O.SODERBERG,H.EKLUND,C.-I.BRANDEN
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI
REMARK 1 TITL 2 THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 72 2305 1975
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.-O.SODERBERG,A.HOLMGREN,C.-I.BRANDEN
REMARK 1 TITL STRUCTURE OF OXIDIZED THIOREDOXIN TO 4.5 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 90 143 1974
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.HOLMGREN,B.-O.SODERBERG
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA FOR
REMARK 1 TITL 2 THIOREDOXIN FROM ESCHERICHIA COLI B
REMARK 1 REF J.MOL.BIOL. V. 54 387 1970
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 25969
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.015 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.035 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.055 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.021 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.131 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.165 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.174 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.180 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.000 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 16.300; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.280 ; 1.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.270 ; 1.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2TRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178704.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.53000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.75000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.53000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 89.50000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 65.39562
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.43628
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 ASP A 13 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 47 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TYR A 70 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLU A 85 OE1 - CD - OE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLU A 101 OE1 - CD - OE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 PHE B 12 CB - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 ASP B 20 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 GLU B 85 CA - CB - CG ANGL. DEV. = 13.6 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 ASP B 13 20.75 144.15
REMARK 500 THR B 14 -88.88 -162.21
REMARK 500 VAL B 16 -40.16 -132.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 109 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 1 N
REMARK 620 2 ASP A 2 N 86.5
REMARK 620 3 ASP A 2 OD1 172.6 86.0
REMARK 620 4 HOH A 405 O 89.2 92.0 91.5
REMARK 620 5 ASP A 10 OD1 96.3 174.7 91.1 92.5
REMARK 620 6 ASP A 10 OD2 98.6 120.4 84.8 146.9 54.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 109 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 2 N
REMARK 620 2 HOH B 478 O 88.9
REMARK 620 3 ASP B 2 OD1 89.5 87.8
REMARK 620 4 SER B 1 N 86.9 87.8 174.4
REMARK 620 5 ASP B 10 OD1 172.0 97.4 85.7 98.3
REMARK 620 6 ASP B 10 OD2 117.6 151.2 81.6 103.9 55.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 607
DBREF 2TRX A 1 108 UNP P0AA25 THIO_ECOLI 1 108
DBREF 2TRX B 1 108 UNP P0AA25 THIO_ECOLI 1 108
SEQRES 1 A 108 SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP
SEQRES 2 A 108 THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP
SEQRES 3 A 108 PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA
SEQRES 4 A 108 PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS
SEQRES 5 A 108 LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY
SEQRES 6 A 108 THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU
SEQRES 7 A 108 LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL
SEQRES 8 A 108 GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP
SEQRES 9 A 108 ALA ASN LEU ALA
SEQRES 1 B 108 SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP
SEQRES 2 B 108 THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP
SEQRES 3 B 108 PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA
SEQRES 4 B 108 PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS
SEQRES 5 B 108 LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY
SEQRES 6 B 108 THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU
SEQRES 7 B 108 LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL
SEQRES 8 B 108 GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP
SEQRES 9 B 108 ALA ASN LEU ALA
HET CU A 109 1
HET MPD A 601 8
HET MPD A 605 8
HET MPD A 606 8
HET MPD A 607 8
HET CU B 109 1
HET MPD B 602 8
HET MPD B 603 8
HET MPD B 604 8
HETNAM CU COPPER (II) ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 CU 2(CU 2+)
FORMUL 4 MPD 7(C6 H14 O2)
FORMUL 12 HOH *140(H2 O)
HELIX 1 A1A SER A 11 LEU A 17 1DISORDERED IN MOLECULE B 7
HELIX 2 A2A CYS A 32 TYR A 49 1BENT BY 30 DEGREES AT RES 39 18
HELIX 3 A3A ASN A 59 ASN A 63 1 5
HELIX 4 31A THR A 66 TYR A 70 5DISTORTED H-BONDING C-TERMINS 5
HELIX 5 A4A SER A 95 LEU A 107 1 13
HELIX 6 A1B SER B 11 LEU B 17 1DISORDERED IN MOLECULE B 7
HELIX 7 A2B CYS B 32 TYR B 49 1BENT BY 30 DEGREES AT RES 39 18
HELIX 8 A3B ASN B 59 ASN B 63 1 5
HELIX 9 31B THR B 66 TYR B 70 5DISTORTED H-BONDING C-TERMINS 5
HELIX 10 A4B SER B 95 LEU B 107 1 13
SHEET 1 B1A 5 LYS A 3 THR A 8 0
SHEET 2 B1A 5 LEU A 53 ASN A 59 1 O VAL A 55 N ILE A 5
SHEET 3 B1A 5 GLY A 21 TRP A 28 1 N TRP A 28 O LEU A 58
SHEET 4 B1A 5 PRO A 76 LYS A 82 -1 O THR A 77 N PHE A 27
SHEET 5 B1A 5 VAL A 86 GLY A 92 -1 O ALA A 87 N LEU A 80
SHEET 1 B1B 5 LYS B 3 THR B 8 0
SHEET 2 B1B 5 LEU B 53 ASN B 59 1 O VAL B 55 N ILE B 5
SHEET 3 B1B 5 GLY B 21 TRP B 28 1 N TRP B 28 O LEU B 58
SHEET 4 B1B 5 PRO B 76 LYS B 82 -1 O THR B 77 N PHE B 27
SHEET 5 B1B 5 VAL B 86 GLY B 92 -1 O ALA B 87 N LEU B 80
SSBOND 1 CYS A 32 CYS A 35 1555 1555 2.09
SSBOND 2 CYS B 32 CYS B 35 1555 1555 2.05
LINK CU CU A 109 N SER A 1 1555 1555 2.05
LINK CU CU A 109 N ASP A 2 1555 1555 2.06
LINK CU CU A 109 OD1 ASP A 2 1555 1555 2.00
LINK CU CU A 109 O HOH A 405 1555 1555 2.65
LINK CU CU B 109 N ASP B 2 1555 1555 2.05
LINK CU CU B 109 O HOH B 478 1555 1555 2.63
LINK CU CU B 109 OD1 ASP B 2 1555 1555 2.06
LINK CU CU B 109 N SER B 1 1555 1555 2.09
LINK CU CU A 109 OD1 ASP A 10 1555 4545 1.97
LINK CU CU A 109 OD2 ASP A 10 1555 4545 2.62
LINK CU CU B 109 OD1 ASP B 10 1555 4546 2.08
LINK CU CU B 109 OD2 ASP B 10 1555 4546 2.54
CISPEP 1 ILE A 75 PRO A 76 0 0.60
CISPEP 2 ILE B 75 PRO B 76 0 -2.42
SITE 1 AC1 5 SER A 1 ASP A 2 LYS A 3 ASP A 10
SITE 2 AC1 5 HOH A 405
SITE 1 AC2 5 SER B 1 ASP B 2 LYS B 3 ASP B 10
SITE 2 AC2 5 HOH B 478
SITE 1 AC3 4 ASP A 10 ASP A 43 GLU A 44 HOH A 442
SITE 1 AC4 6 GLU A 44 HOH A 524 GLU B 30 TRP B 31
SITE 2 AC4 6 GLY B 33 LYS B 36
SITE 1 AC5 5 TYR B 70 ILE B 72 THR B 77 THR B 89
SITE 2 AC5 5 VAL B 91
SITE 1 AC6 3 ILE B 60 ALA B 67 ILE B 72
SITE 1 AC7 4 MET A 37 ILE A 38 ALA A 93 LEU A 94
SITE 1 AC8 4 TYR A 70 GLY A 71 THR A 89 VAL A 91
SITE 1 AC9 8 ILE A 60 ALA A 67 ILE A 72 ARG A 73
SITE 2 AC9 8 GLY A 74 ILE A 75 HOH A 494 HOH B 528
CRYST1 89.500 51.060 60.450 90.00 113.50 90.00 C 1 2 1 8
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 0.011173 0.000000 0.004858 0.00000
SCALE2 0.000000 0.019585 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END