HEADER ISOMERASE 15-JAN-06 2FP2
TITLE SECRETED CHORISMATE MUTASE FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHORISMATE MUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 34-199;
COMPND 5 EC: 5.4.99.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: KA29;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKTU3-HT
KEYWDS ALPHA-HELICAL, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.OKVIST,R.DEY,S.SASSO,E.GRAHN,P.KAST,U.KRENGEL
REVDAT 5 30-AUG-23 2FP2 1 REMARK
REVDAT 4 07-MAR-18 2FP2 1 REMARK
REVDAT 3 24-FEB-09 2FP2 1 VERSN
REVDAT 2 04-APR-06 2FP2 1 JRNL
REVDAT 1 28-MAR-06 2FP2 0
JRNL AUTH M.OKVIST,R.DEY,S.SASSO,E.GRAHN,P.KAST,U.KRENGEL
JRNL TITL 1.6A CRYSTAL STRUCTURE OF THE SECRETED CHORISMATE MUTASE
JRNL TITL 2 FROM MYCOBACTERIUM TUBERCULOSIS: NOVEL FOLD TOPOLOGY
JRNL TITL 3 REVEALED
JRNL REF J.MOL.BIOL. V. 357 1483 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16499927
JRNL DOI 10.1016/J.JMB.2006.01.069
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 42905
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2284
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2978
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2557
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 416
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : -0.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2750 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1904 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3773 ; 1.397 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4626 ; 0.912 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 4.803 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 139 ;34.821 ;23.381
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 455 ;12.827 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;20.752 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 419 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3122 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 564 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 657 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2080 ; 0.210 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1396 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1352 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 272 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 25 ; 0.155 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 54 ; 0.357 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.145 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2230 ; 1.827 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 650 ; 0.269 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2761 ; 1.570 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1195 ; 2.794 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1000 ; 4.249 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2FP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036138.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.087
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45129
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 38.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.15400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2FP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-15% PEG 4000, 0.2 M SODIUM ACETATE,
REMARK 280 0.1 M CACODYLATE BUFFER, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 36.40000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: PROPOSED TO BE THE DIMER IN THE ASYMMETRIC UNIT
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 34
REMARK 465 GLY A 35
REMARK 465 PRO A 125
REMARK 465 GLU A 126
REMARK 465 ASP B 34
REMARK 465 GLY B 35
REMARK 465 THR B 36
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 ARG B 175 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 175 NE - CZ - NH2 ANGL. DEV. = -3.0 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 A 69 100.51 -161.78
REMARK 500 PRO A 128 -142.53 -77.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 127 PRO A 128 -52.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSA B 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FP1 RELATED DB: PDB
REMARK 900 LEAD DERIVATIVE OF THE SAME PROTEIN
DBREF 2FP2 A 34 199 UNP O07746 O07746_MYCTU 34 199
DBREF 2FP2 B 34 199 UNP O07746 O07746_MYCTU 34 199
SEQRES 1 A 166 ASP GLY THR SER GLN LEU ALA GLU LEU VAL ASP ALA ALA
SEQRES 2 A 166 ALA GLU ARG LEU GLU VAL ALA ASP PRO VAL ALA ALA PHE
SEQRES 3 A 166 LYS TRP ARG ALA GLN LEU PRO ILE GLU ASP SER GLY ARG
SEQRES 4 A 166 VAL GLU GLN GLN LEU ALA LYS LEU GLY GLU ASP ALA ARG
SEQRES 5 A 166 SER GLN HIS ILE ASP PRO ASP TYR VAL THR ARG VAL PHE
SEQRES 6 A 166 ASP ASP GLN ILE ARG ALA THR GLU ALA ILE GLU TYR SER
SEQRES 7 A 166 ARG PHE SER ASP TRP LYS LEU ASN PRO ALA SER ALA PRO
SEQRES 8 A 166 PRO GLU PRO PRO ASP LEU SER ALA SER ARG SER ALA ILE
SEQRES 9 A 166 ASP SER LEU ASN ASN ARG MET LEU SER GLN ILE TRP SER
SEQRES 10 A 166 HIS TRP SER LEU LEU SER ALA PRO SER CYS ALA ALA GLN
SEQRES 11 A 166 LEU ASP ARG ALA LYS ARG ASP ILE VAL ARG SER ARG HIS
SEQRES 12 A 166 LEU ASP SER LEU TYR GLN ARG ALA LEU THR THR ALA THR
SEQRES 13 A 166 GLN SER TYR CYS GLN ALA LEU PRO PRO ALA
SEQRES 1 B 166 ASP GLY THR SER GLN LEU ALA GLU LEU VAL ASP ALA ALA
SEQRES 2 B 166 ALA GLU ARG LEU GLU VAL ALA ASP PRO VAL ALA ALA PHE
SEQRES 3 B 166 LYS TRP ARG ALA GLN LEU PRO ILE GLU ASP SER GLY ARG
SEQRES 4 B 166 VAL GLU GLN GLN LEU ALA LYS LEU GLY GLU ASP ALA ARG
SEQRES 5 B 166 SER GLN HIS ILE ASP PRO ASP TYR VAL THR ARG VAL PHE
SEQRES 6 B 166 ASP ASP GLN ILE ARG ALA THR GLU ALA ILE GLU TYR SER
SEQRES 7 B 166 ARG PHE SER ASP TRP LYS LEU ASN PRO ALA SER ALA PRO
SEQRES 8 B 166 PRO GLU PRO PRO ASP LEU SER ALA SER ARG SER ALA ILE
SEQRES 9 B 166 ASP SER LEU ASN ASN ARG MET LEU SER GLN ILE TRP SER
SEQRES 10 B 166 HIS TRP SER LEU LEU SER ALA PRO SER CYS ALA ALA GLN
SEQRES 11 B 166 LEU ASP ARG ALA LYS ARG ASP ILE VAL ARG SER ARG HIS
SEQRES 12 B 166 LEU ASP SER LEU TYR GLN ARG ALA LEU THR THR ALA THR
SEQRES 13 B 166 GLN SER TYR CYS GLN ALA LEU PRO PRO ALA
HET TSA B 500 16
HETNAM TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-
HETNAM 2 TSA DICARBOXYLIC ACID
FORMUL 3 TSA C10 H12 O6
FORMUL 4 HOH *416(H2 O)
HELIX 1 1 LEU A 39 VAL A 52 1 14
HELIX 2 2 VAL A 52 ALA A 63 1 12
HELIX 3 3 ASP A 69 GLN A 87 1 19
HELIX 4 4 ASP A 90 ASN A 119 1 30
HELIX 5 5 PRO A 120 ALA A 123 5 4
HELIX 6 6 LEU A 130 HIS A 151 1 22
HELIX 7 7 HIS A 151 SER A 156 1 6
HELIX 8 8 SER A 159 HIS A 176 1 18
HELIX 9 9 ASP A 178 GLN A 190 1 13
HELIX 10 10 LEU B 39 VAL B 52 1 14
HELIX 11 11 VAL B 52 GLN B 64 1 13
HELIX 12 12 ASP B 69 GLN B 87 1 19
HELIX 13 13 ASP B 90 ASN B 119 1 30
HELIX 14 14 PRO B 120 ALA B 123 5 4
HELIX 15 15 ASP B 129 HIS B 151 1 23
HELIX 16 16 HIS B 151 SER B 156 1 6
HELIX 17 17 SER B 159 ARG B 175 1 17
HELIX 18 18 ASP B 178 THR B 189 1 12
HELIX 19 19 SER B 191 ALA B 195 5 5
SSBOND 1 CYS A 160 CYS A 193 1555 1555 2.05
SSBOND 2 CYS B 160 CYS B 193 1555 1555 2.04
SITE 1 AC1 13 ARG B 49 VAL B 56 LYS B 60 ILE B 67
SITE 2 AC1 13 GLU B 68 ASP B 69 GLN B 76 ILE B 102
SITE 3 AC1 13 THR B 105 GLU B 106 GLU B 109 ARG B 134
SITE 4 AC1 13 HOH B 607
CRYST1 42.906 72.800 61.716 90.00 103.99 90.00 P 1 21 1 4
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 0.023307 0.000000 0.005807 0.00000
SCALE2 0.000000 0.013736 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016699 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
