HEADER HYDROLASE 14-APR-05 1ZDP
TITLE CRYSTAL STRUCTURE ANALYSIS OF THERMOLYSIN COMPLEXED WITH THE INHIBITOR
TITLE 2 (S)-THIORPHAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND 5 EC: 3.4.24.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS ENZYME-INHIBITOR COMPLEX; ZINC ENDOPEPTIDASE; GAMMA TURN;
KEYWDS 2 THERMOSTABLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.L.RODERICK,M.C.FOURNIE-ZALUSKI,B.P.ROQUES,B.W.MATTHEWS
REVDAT 4 23-AUG-23 1ZDP 1 REMARK SEQADV LINK
REVDAT 3 11-OCT-17 1ZDP 1 REMARK
REVDAT 2 24-FEB-09 1ZDP 1 VERSN
REVDAT 1 26-APR-05 1ZDP 0
JRNL AUTH S.L.RODERICK,M.C.FOURNIE-ZALUSKI,B.P.ROQUES,B.W.MATTHEWS
JRNL TITL THIORPHAN AND RETRO-THIORPHAN DISPLAY EQUIVALENT
JRNL TITL 2 INTERACTIONS WHEN BOUND TO CRYSTALLINE THERMOLYSIN
JRNL REF BIOCHEMISTRY V. 28 1493 1989
JRNL REFN ISSN 0006-2960
JRNL PMID 2719912
JRNL DOI 10.1021/BI00430A011
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 68.0
REMARK 3 NUMBER OF REFLECTIONS : 25988
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.183
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 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1830
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1830
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) : 25988
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2432
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 14.600
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.020 ; NULL ; 2508
REMARK 3 BOND ANGLES (DEGREES) : 3.530 ; NULL ; 3405
REMARK 3 TORSION ANGLES (DEGREES) : 16.712; NULL ; 1440
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.013 ; NULL ; 67
REMARK 3 GENERAL PLANES (A) : 0.015 ; NULL ; 376
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 4.228 ; NULL ; 2491
REMARK 3 NON-BONDED CONTACTS (A) : 0.062 ; NULL ; 13
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT VERSION 1.0
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : ISOTROPIC
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 35 CYCLES OF CONJUGATE GRADIENT
REMARK 3 REFINEMENT
REMARK 4
REMARK 4 1ZDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 1987
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 7.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-21
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : GRAPHITE MONOCHROMATOR,
REMARK 200 COLLIMATING SLITS
REMARK 200
REMARK 200 DETECTOR TYPE : FILM
REMARK 200 DETECTOR MANUFACTURER : KODAK
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ROTAVATA, OSCTST
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26142
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 68.0
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : 0.03800
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: PDB ENTRY 3TLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS ACETATE, CALCIUM ACETATE, DMSO,
REMARK 280 PH 7.20, DILUTION WITH H2O, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.03333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 88.06667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.05000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 110.08333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.01667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.03333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 88.06667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 110.08333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 66.05000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 22.01667
REMARK 290
REMARK 290 REMARK: NULL
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 300 REMARK: THE ENZYME ACTS AS A MONOMER.
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: E
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 IN SAME ASYMMETRIC UNIT
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 NH1 ARG E 269 OD2 ASP E 294 2.16
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 SER E 53 CB SER E 53 OG -0.086
REMARK 500 GLU E 160 CD GLU E 160 OE2 0.075
REMARK 500 GLU E 187 CD GLU E 187 OE2 0.103
REMARK 500 GLU E 190 CD GLU E 190 OE2 0.077
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 THR E 4 OG1 - CB - CG2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 THR E 6 OG1 - CB - CG2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASP E 16 CB - CG - OD1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASP E 16 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 TYR E 24 CG - CD1 - CE1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 THR E 26 N - CA - CB ANGL. DEV. = 12.3 DEGREES
REMARK 500 TYR E 42 CZ - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 SER E 53 CB - CA - C ANGL. DEV. = -14.7 DEGREES
REMARK 500 ASP E 57 CB - CG - OD1 ANGL. DEV. = 14.8 DEGREES
REMARK 500 ASP E 57 CB - CG - OD2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 GLN E 61 CA - CB - CG ANGL. DEV. = -15.0 DEGREES
REMARK 500 TYR E 66 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TYR E 75 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TYR E 75 CG - CD1 - CE1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP E 82 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ASP E 82 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 TYR E 93 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG E 101 CG - CD - NE ANGL. DEV. = -15.2 DEGREES
REMARK 500 SER E 103 N - CA - CB ANGL. DEV. = 9.8 DEGREES
REMARK 500 ALA E 113 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 TYR E 122 CG - CD1 - CE1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 TYR E 122 CG - CD2 - CE2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TYR E 122 CD1 - CE1 - CZ ANGL. DEV. = 7.2 DEGREES
REMARK 500 TYR E 122 CZ - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP E 124 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 GLN E 128 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 ILE E 156 CA - CB - CG2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 ASP E 185 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP E 185 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 GLY E 196 C - N - CA ANGL. DEV. = -14.1 DEGREES
REMARK 500 ASP E 200 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP E 200 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG E 203 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP E 207 CB - CG - OD1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 ASP E 207 CB - CG - OD2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 TYR E 211 CB - CG - CD2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 TYR E 211 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 PRO E 214 N - CA - CB ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG E 220 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG E 220 CD - NE - CZ ANGL. DEV. = 11.7 DEGREES
REMARK 500 ARG E 220 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG E 220 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TYR E 221 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP E 226 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP E 226 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR E 242 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 THR E 249 CA - CB - CG2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 TYR E 251 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG E 260 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG E 260 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 SER E 25 84.18 -160.48
REMARK 500 THR E 26 -58.18 78.05
REMARK 500 PHE E 62 64.86 -117.27
REMARK 500 SER E 92 -171.11 57.61
REMARK 500 SER E 107 -159.97 56.85
REMARK 500 ASN E 111 46.47 -93.95
REMARK 500 SER E 118 -19.36 -140.30
REMARK 500 THR E 152 -101.20 -110.85
REMARK 500 ASN E 159 -143.34 56.66
REMARK 500 THR E 194 71.71 35.23
REMARK 500 ASP E 207 85.30 -152.19
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 CA E1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 57 OD1
REMARK 620 2 ASP E 57 OD2 49.9
REMARK 620 3 ASP E 59 OD1 118.5 68.9
REMARK 620 4 GLN E 61 O 95.3 90.3 90.8
REMARK 620 5 HOH E 419 O 84.4 133.1 156.9 83.2
REMARK 620 6 HOH E 482 O 164.7 145.1 76.2 88.7 81.4
REMARK 620 7 HOH E 503 O 86.9 88.8 85.5 176.3 100.0 89.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 138 OD1
REMARK 620 2 GLU E 177 OE1 76.8
REMARK 620 3 GLU E 177 OE2 121.7 46.3
REMARK 620 4 ASP E 185 OD2 162.0 120.8 76.4
REMARK 620 5 GLU E 187 O 86.6 141.4 144.3 76.8
REMARK 620 6 GLU E 190 OE1 85.0 132.5 121.2 84.9 79.1
REMARK 620 7 GLU E 190 OE2 99.0 87.2 70.8 86.6 130.2 52.6
REMARK 620 8 HOH E 346 O 96.9 74.8 81.8 85.2 72.9 151.7 152.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E1005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 142 NE2
REMARK 620 2 HIS E 146 NE2 100.8
REMARK 620 3 GLU E 166 OE1 126.4 97.2
REMARK 620 4 TIO E1006 SG1 116.3 112.8 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 177 OE2
REMARK 620 2 ASN E 183 O 92.8
REMARK 620 3 ASP E 185 OD1 94.6 93.0
REMARK 620 4 GLU E 190 OE2 84.0 174.9 83.3
REMARK 620 5 HOH E 353 O 90.9 91.3 172.8 92.7
REMARK 620 6 HOH E 475 O 164.1 91.2 100.6 92.9 73.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 193 O
REMARK 620 2 THR E 194 OG1 75.3
REMARK 620 3 THR E 194 O 77.5 65.5
REMARK 620 4 ILE E 197 O 148.2 107.4 75.4
REMARK 620 5 ASP E 200 OD1 125.2 77.3 129.6 85.4
REMARK 620 6 HOH E 354 O 81.5 125.1 152.8 117.7 77.0
REMARK 620 7 HOH E 480 O 87.6 147.1 83.6 73.2 134.5 78.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TIO E 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z9G RELATED DB: PDB
DBREF 1ZDP E 1 316 UNP P00800 THER_BACTH 233 548
SEQADV 1ZDP ASP E 37 UNP P00800 ASN 269 CONFLICT
SEQADV 1ZDP GLU E 119 UNP P00800 GLN 351 CONFLICT
SEQADV 1ZDP GLU E 177 UNP P00800 LYS 409 SEE REMARK 999
SEQRES 1 E 316 ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES 2 E 316 LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES 3 E 316 TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE
SEQRES 4 E 316 PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES 5 E 316 SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES 6 E 316 TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES 7 E 316 VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES 8 E 316 SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES 9 E 316 HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES 10 E 316 SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES 11 E 316 ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES 12 E 316 LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES 13 E 316 TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES 14 E 316 ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES 15 E 316 ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES 16 E 316 GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES 17 E 316 ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES 18 E 316 THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES 19 E 316 GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES 20 E 316 GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES 21 E 316 ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES 22 E 316 TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES 23 E 316 ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES 24 E 316 SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES 25 E 316 VAL GLY VAL LYS
HET CA E1001 1
HET CA E1002 1
HET CA E1003 1
HET CA E1004 1
HET ZN E1005 1
HET TIO E1006 17
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
HETNAM TIO (2-MERCAPTOMETHYL-3-PHENYL-PROPIONYL)-GLYCINE
HETSYN TIO THIORPHAN
FORMUL 2 CA 4(CA 2+)
FORMUL 6 ZN ZN 2+
FORMUL 7 TIO C12 H15 N O3 S
FORMUL 8 HOH *161(H2 O)
HELIX 1 1 ASP E 67 ASN E 89 1 23
HELIX 2 2 PRO E 132 GLY E 135 5 4
HELIX 3 3 GLY E 136 THR E 152 1 17
HELIX 4 4 GLN E 158 ASN E 181 1 24
HELIX 5 5 ASP E 207 GLY E 212 5 6
HELIX 6 6 HIS E 216 ARG E 220 5 5
HELIX 7 7 GLN E 225 VAL E 230 1 6
HELIX 8 8 ASN E 233 GLY E 247 1 15
HELIX 9 9 GLY E 259 TYR E 274 1 16
HELIX 10 10 ASN E 280 GLY E 297 1 18
HELIX 11 11 SER E 300 VAL E 313 1 14
SHEET 1 A 5 ALA E 56 ASP E 57 0
SHEET 2 A 5 TYR E 28 TYR E 29 -1 N TYR E 28 O ASP E 57
SHEET 3 A 5 GLN E 17 TYR E 24 -1 N THR E 23 O TYR E 29
SHEET 4 A 5 THR E 4 ARG E 11 -1 N THR E 4 O TYR E 24
SHEET 5 A 5 GLN E 61 PHE E 62 1 O PHE E 62 N VAL E 9
SHEET 1 B 3 GLN E 31 ASP E 32 0
SHEET 2 B 3 ILE E 39 ASP E 43 -1 O ILE E 39 N ASP E 32
SHEET 3 B 3 SER E 53 LEU E 54 -1 O SER E 53 N ASP E 43
SHEET 1 C 5 GLN E 31 ASP E 32 0
SHEET 2 C 5 ILE E 39 ASP E 43 -1 O ILE E 39 N ASP E 32
SHEET 3 C 5 ILE E 100 VAL E 104 1 O SER E 102 N TYR E 42
SHEET 4 C 5 MET E 120 TYR E 122 1 O TYR E 122 N SER E 103
SHEET 5 C 5 ALA E 113 TRP E 115 -1 N PHE E 114 O VAL E 121
SHEET 1 D 2 GLU E 187 ILE E 188 0
SHEET 2 D 2 ARG E 203 SER E 204 -1 O ARG E 203 N ILE E 188
SHEET 1 E 2 GLY E 248 HIS E 250 0
SHEET 2 E 2 VAL E 253 VAL E 255 -1 O VAL E 255 N GLY E 248
LINK OD1 ASP E 57 CA CA E1003 1555 1555 2.14
LINK OD2 ASP E 57 CA CA E1003 1555 1555 2.68
LINK OD1 ASP E 59 CA CA E1003 1555 1555 2.42
LINK O GLN E 61 CA CA E1003 1555 1555 2.19
LINK OD1 ASP E 138 CA CA E1001 1555 1555 2.41
LINK NE2 HIS E 142 ZN ZN E1005 1555 1555 2.14
LINK NE2 HIS E 146 ZN ZN E1005 1555 1555 2.10
LINK OE1 GLU E 166 ZN ZN E1005 1555 1555 2.00
LINK OE1 GLU E 177 CA CA E1001 1555 1555 2.55
LINK OE2 GLU E 177 CA CA E1001 1555 1555 2.87
LINK OE2 GLU E 177 CA CA E1002 1555 1555 2.29
LINK O ASN E 183 CA CA E1002 1555 1555 2.61
LINK OD2 ASP E 185 CA CA E1001 1555 1555 2.52
LINK OD1 ASP E 185 CA CA E1002 1555 1555 2.39
LINK O GLU E 187 CA CA E1001 1555 1555 2.29
LINK OE1 GLU E 190 CA CA E1001 1555 1555 2.58
LINK OE2 GLU E 190 CA CA E1001 1555 1555 2.48
LINK OE2 GLU E 190 CA CA E1002 1555 1555 2.36
LINK O TYR E 193 CA CA E1004 1555 1555 2.59
LINK OG1 THR E 194 CA CA E1004 1555 1555 2.50
LINK O THR E 194 CA CA E1004 1555 1555 2.60
LINK O ILE E 197 CA CA E1004 1555 1555 2.27
LINK OD1 ASP E 200 CA CA E1004 1555 1555 2.28
LINK O HOH E 346 CA CA E1001 1555 1555 2.69
LINK O HOH E 353 CA CA E1002 1555 1555 2.44
LINK O HOH E 354 CA CA E1004 1555 1555 2.56
LINK O HOH E 419 CA CA E1003 1555 1555 2.43
LINK O HOH E 475 CA CA E1002 1555 1555 1.89
LINK O HOH E 480 CA CA E1004 1555 1555 2.29
LINK O HOH E 482 CA CA E1003 1555 1555 2.21
LINK O HOH E 503 CA CA E1003 1555 1555 2.38
LINK ZN ZN E1005 SG1 TIO E1006 1555 1555 2.41
CISPEP 1 LEU E 50 PRO E 51 0 0.35
SITE 1 AC1 6 ASP E 138 GLU E 177 ASP E 185 GLU E 187
SITE 2 AC1 6 GLU E 190 HOH E 346
SITE 1 AC2 6 GLU E 177 ASN E 183 ASP E 185 GLU E 190
SITE 2 AC2 6 HOH E 353 HOH E 475
SITE 1 AC3 6 ASP E 57 ASP E 59 GLN E 61 HOH E 419
SITE 2 AC3 6 HOH E 482 HOH E 503
SITE 1 AC4 6 TYR E 193 THR E 194 ILE E 197 ASP E 200
SITE 2 AC4 6 HOH E 354 HOH E 480
SITE 1 AC5 5 HIS E 142 HIS E 146 TYR E 157 GLU E 166
SITE 2 AC5 5 TIO E1006
SITE 1 AC6 11 ASN E 112 ALA E 113 VAL E 139 GLU E 143
SITE 2 AC6 11 TYR E 157 GLU E 166 ILE E 188 LEU E 202
SITE 3 AC6 11 ARG E 203 HIS E 231 ZN E1005
CRYST1 94.000 94.000 132.100 90.00 90.00 120.00 P 61 2 2 12
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 0.010638 0.006142 0.000000 0.00000
SCALE2 0.000000 0.012284 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007570 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
