HEADER ISOMERASE 15-JAN-06 2FP1
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 3 24-FEB-09 2FP1 1 VERSN
REVDAT 2 04-APR-06 2FP1 1 JRNL
REVDAT 1 28-MAR-06 2FP1 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
JRNL TITL 2 MUTASE FROM MYCOBACTERIUM TUBERCULOSIS: NOVEL FOLD
JRNL TITL 3 TOPOLOGY 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 1
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 50407
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2659
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3663
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 212
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2702
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 427
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.391
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2774 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1916 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3804 ; 1.367 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4653 ; 0.944 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 4.105 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 140 ;34.090 ;23.429
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 461 ;13.613 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;22.051 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 422 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3165 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 567 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 717 ; 0.237 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2088 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1433 ; 0.182 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1437 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 285 ; 0.149 ; 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): 16 ; 0.286 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 60 ; 0.321 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.153 ; 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): 1736 ; 0.882 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 660 ; 0.258 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2814 ; 1.614 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1128 ; 2.676 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 983 ; 4.312 ; 4.500
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 : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2FP1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-06.
REMARK 100 THE RCSB ID CODE IS RCSB036137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393, 0.9506, 0.9393
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53094
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 31.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-15% PEG 4000, 0.2 M SODIUM
REMARK 280 ACETATE, 0.1 M CACODYLATE BUFFER, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 36.33650
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 ASP B 34
REMARK 465 GLY B 35
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR B 36 OG1 CG2
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 94.26 -160.94
REMARK 500 ASP A 129 -179.78 -70.00
REMARK 500 ASP B 69 72.62 -153.81
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 PB B 501 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 38 OE1
REMARK 620 2 HIS B 151 NE2 124.7
REMARK 620 3 HOH B 564 O 47.1 79.4
REMARK 620 4 GLN B 38 O 84.9 71.2 80.1
REMARK 620 5 GLU B 41 OE1 137.6 78.3 146.1 68.7
REMARK 620 6 GLU B 41 OE2 150.6 82.7 149.4 117.1 50.1
REMARK 620 7 HOH B 540 O 76.4 143.8 122.0 83.5 68.4 86.5
REMARK 620 8 GLU A 41 OE1 78.7 126.0 95.1 161.3 118.7 75.8 83.9
REMARK 620 9 GLU A 41 OE2 95.6 77.6 73.0 141.8 125.7 79.1 133.8 50.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB B 502 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 48 OE2
REMARK 620 2 GLU B 51 OE1 103.8
REMARK 620 3 GLU B 51 OE2 70.9 46.9
REMARK 620 4 GLU B 48 OE1 51.7 75.9 80.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FP2 RELATED DB: PDB
DBREF 2FP1 A 34 199 UNP O07746 O07746_MYCTU 34 199
DBREF 2FP1 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 PB B 501 1
HET PB B 502 1
HETNAM PB LEAD (II) ION
FORMUL 3 PB 2(PB 2+)
FORMUL 5 HOH *427(H2 O)
HELIX 1 1 LEU A 39 VAL A 52 1 14
HELIX 2 2 VAL A 52 GLN A 64 1 13
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 ARG A 175 1 17
HELIX 9 9 ASP A 178 THR A 189 1 12
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 GLN B 190 1 13
HELIX 19 19 SER B 191 ALA B 195 5 5
SSBOND 1 CYS A 160 CYS A 193 1555 1555 2.10
SSBOND 2 CYS B 160 CYS B 193 1555 1555 2.06
LINK PB PB B 501 OE1 GLN B 38 1555 1555 3.02
LINK PB PB B 501 NE2 HIS B 151 1555 1555 2.47
LINK PB PB B 501 O HOH B 564 1555 1555 2.82
LINK PB PB B 501 O GLN B 38 1555 1555 2.79
LINK PB PB B 501 OE1 GLU B 41 1555 1555 2.66
LINK PB PB B 501 OE2 GLU B 41 1555 1555 2.52
LINK PB PB B 501 O HOH B 540 1555 1555 3.08
LINK PB PB B 502 OE2 GLU B 48 1555 1555 2.58
LINK PB PB B 502 OE1 GLU B 51 1555 1555 2.78
LINK PB PB B 502 OE2 GLU B 51 1555 1555 2.75
LINK PB PB B 502 OE1 GLU B 48 1555 1555 2.54
LINK PB PB B 501 OE1 GLU A 41 1555 1454 2.62
LINK PB PB B 501 OE2 GLU A 41 1555 1454 2.50
SITE 1 AC1 6 GLU A 41 GLN B 38 GLU B 41 HIS B 151
SITE 2 AC1 6 HOH B 540 HOH B 564
SITE 1 AC2 2 GLU B 48 GLU B 51
CRYST1 42.644 72.673 62.060 90.00 104.52 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 0.023450 0.000000 0.006074 0.00000
SCALE2 0.000000 0.013760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016645 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
