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HEADER HYDROLASE 06-FEB-05 1YS1
TITLE BURKHOLDERIA CEPACIA LIPASE COMPLEXED WITH HEXYLPHOSPHONIC
TITLE 2 ACID (R)-2-METHYL-3-PHENYLPROPYL ESTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: RESIDUES 45-364;
COMPND 5 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 6 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CEPACIA;
SOURCE 3 ORGANISM_COMMON: BACTERIA
KEYWDS CIS PEPTIDE LEU 234, CA2+ ION, INHIBITOR HEXYLPHOSPHONIC
KEYWDS 2 ACID (R) 2-METHYL-3-PHENYLPROPYL ESTER
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MEZZETTI,J.D.SCHRAG,C.S.CHEONG,R.J.KAZLAUSKAS
REVDAT 1 17-MAY-05 1YS1 0
JRNL AUTH A.MEZZETTI,J.D.SCHRAG,C.S.CHEONG,R.J.KAZLAUSKAS
JRNL TITL MIRROR-IMAGE PACKING IN ENANTIOMER DISCRIMINATION
JRNL TITL 2 MOLECULAR BASIS FOR THE ENANTIOSELECTIVITY OF
JRNL TITL 3 B.CEPACIA LIPASE TOWARD
JRNL TITL 4 2-METHYL-3-PHENYL-1-PROPANOL.
JRNL REF CHEM.BIOL. V. 12 427 2005
JRNL REFN ASTM CBOLE2 UK ISSN 1074-5521
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 100662
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.158
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5326
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.10
REMARK 3 BIN RESOLUTION RANGE LOW : 1.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3160
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1690
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.1950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2498
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 5.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.029
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.016
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.325
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2395 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2140 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3277 ; 1.287 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4964 ; 0.773 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 319 ; 5.716 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 391 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2742 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 460 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 504 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2502 ; 0.249 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1284 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 93 ; 0.068 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.087 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 1 ; 0.074 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.217 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.054 ; 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): 1577 ; 0.532 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2524 ; 0.943 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 818 ; 1.355 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 753 ; 2.107 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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 1YS1 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-2005.
REMARK 100 THE RCSB ID CODE IS RCSB031865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105990
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 44.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 4.680
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 FOR THE DATA SET : 20.9900
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 3LIP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM IMIDAZOLE, 30% N-PROPANOL, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 44.42400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.09250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.42400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.09250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: X
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: 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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO X 131 CB PRO X 131 CG -0.044
REMARK 500 MET X 255 SD MET X 255 CE -0.055
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR X 20 N - CA - C ANGL. DEV. = -7.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 LEU X 234 -52.77 68.04
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LIP RELATED DB: PDB
REMARK 900 OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE
REMARK 900 RELATED ID: 1YS2 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICTS WITH THE DATABASE ARE DUE TO USING
REMARK 999 A DIFFERENT STRAIN OF BURKHOLDERIA CEPACIA (M-12-33).
REMARK 999 THE INFORMATION REGARDING THE SEQUENCE CAN BE FOUND IN
REMARK 999 NAKANISHI, J., KURONO, Y., KOLDE, Y., AND BEPPU, T.
REMARK 999 (1989) RECOMBINANT DNA, BACTERIUM OF THE GENUS
REMARK 999 PSEUDOMONAS CONTAINING IT, AND PROCESS FOR PREPARING
REMARK 999 LIPASE USING IT. EUROPEAN PATENT 0331376.
DBREF 1YS1 X 1 320 SWS P22088 LIP_BURCE 45 364
SEQADV 1YS1 ASP X 2 SWS P22088 ALA 46 SEE REMARK 999
SEQADV 1YS1 ASN X 3 SWS P22088 GLY 47 SEE REMARK 999
SEQADV 1YS1 THR X 18 SWS P22088 SER 62 SEE REMARK 999
SEQADV 1YS1 ARG X 40 SWS P22088 ASN 84 SEE REMARK 999
SEQADV 1YS1 THR X 92 SWS P22088 SER 136 SEE REMARK 999
SEQADV 1YS1 GLY X 125 SWS P22088 ASP 169 SEE REMARK 999
SEQADV 1YS1 THR X 137 SWS P22088 SER 181 SEE REMARK 999
SEQADV 1YS1 ASN X 154 SWS P22088 HIS 198 SEE REMARK 999
SEQADV 1YS1 LYS X 165 SWS P22088 GLN 209 SEE REMARK 999
SEQADV 1YS1 GLN X 171 SWS P22088 ARG 215 SEE REMARK 999
SEQADV 1YS1 ILE X 218 SWS P22088 LEU 262 SEE REMARK 999
SEQADV 1YS1 GLY X 221 SWS P22088 PHE 265 SEE REMARK 999
SEQADV 1YS1 ILE X 232 SWS P22088 LEU 276 SEE REMARK 999
SEQADV 1YS1 ALA X 240 SWS P22088 VAL 284 SEE REMARK 999
SEQADV 1YS1 PRO X 243 SWS P22088 LEU 287 SEE REMARK 999
SEQADV 1YS1 VAL X 256 SWS P22088 ILE 300 SEE REMARK 999
SEQADV 1YS1 VAL X 266 SWS P22088 LEU 310 SEE REMARK 999
SEQADV 1YS1 GLN X 276 SWS P22088 LYS 320 SEE REMARK 999
SEQADV 1YS1 ASN X 300 SWS P22088 TYR 344 SEE REMARK 999
SEQRES 1 X 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 X 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 X 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 X 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 X 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 X 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 X 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 X 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 X 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 X 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 X 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 X 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 X 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 X 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 X 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 X 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 X 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL GLY
SEQRES 18 X 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 X 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 X 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 X 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 X 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 X 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 X 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 X 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA X 400 1
HET 2HR X 600 19
HETNAM CA CALCIUM ION
HETNAM 2HR HEXYLPHOSPHONIC ACID (R)-2-METHYL-3-PHENYLPROPYL ESTER
FORMUL 2 CA CA1 2+
FORMUL 3 2HR C16 H27 O3 P1
FORMUL 4 HOH *147(H2 O1)
HELIX 1 1 ALA X 24 VAL X 26 5 3
HELIX 2 2 GLY X 32 ARG X 40 1 9
HELIX 3 3 GLY X 60 GLY X 77 1 18
HELIX 4 4 SER X 87 ALA X 100 1 14
HELIX 5 5 SER X 117 ALA X 128 1 12
HELIX 6 6 GLY X 133 SER X 151 1 19
HELIX 7 7 ASP X 159 THR X 168 1 10
HELIX 8 8 THR X 168 TYR X 179 1 12
HELIX 9 9 PRO X 237 ASP X 242 1 6
HELIX 10 10 PRO X 243 ASN X 257 1 15
HELIX 11 11 SER X 268 LEU X 273 1 6
HELIX 12 12 LEU X 287 ASN X 291 5 5
HELIX 13 13 ASP X 303 ALA X 318 1 16
SHEET 1 A 6 VAL X 44 VAL X 46 0
SHEET 2 A 6 ILE X 11 VAL X 14 1 N ILE X 11 O TYR X 45
SHEET 3 A 6 VAL X 81 HIS X 86 1 O VAL X 84 N VAL X 14
SHEET 4 A 6 VAL X 104 ILE X 110 1 O ALA X 105 N VAL X 81
SHEET 5 A 6 ASN X 202 GLY X 211 1 O TYR X 207 N VAL X 107
SHEET 6 A 6 THR X 196 VAL X 199 -1 N GLU X 197 O HIS X 204
SHEET 1 B 6 VAL X 44 VAL X 46 0
SHEET 2 B 6 ILE X 11 VAL X 14 1 N ILE X 11 O TYR X 45
SHEET 3 B 6 VAL X 81 HIS X 86 1 O VAL X 84 N VAL X 14
SHEET 4 B 6 VAL X 104 ILE X 110 1 O ALA X 105 N VAL X 81
SHEET 5 B 6 ASN X 202 GLY X 211 1 O TYR X 207 N VAL X 107
SHEET 6 B 6 GLN X 276 TYR X 282 1 O LEU X 278 N SER X 208
SHEET 1 C 2 LYS X 22 TYR X 23 0
SHEET 2 C 2 LEU X 27 GLU X 28 -1 O LEU X 27 N TYR X 23
SHEET 1 D 2 ILE X 214 VAL X 220 0
SHEET 2 D 2 VAL X 223 ASP X 228 -1 O GLY X 225 N THR X 217
SSBOND 1 CYS X 190 CYS X 270
LINK OG SER X 87 P 2HR X 600
LINK CA CA X 400 OD2 ASP X 242
LINK CA CA X 400 O GLN X 292
LINK CA CA X 400 O VAL X 296
LINK CA CA X 400 OD2 ASP X 288
CISPEP 1 GLN X 292 LEU X 293 0 -7.86
CRYST1 88.848 46.185 84.626 90.00 121.27 90.00 C 1 2 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 0.011255 0.000000 0.006836 0.00000
SCALE2 0.000000 0.021652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013825 0.00000
TER 2332 VAL X 320
MASTER 284 0 2 13 16 0 0 6 2498 1 27 25
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