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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-DEC-04 1YCD
TITLE CRYSTAL STRUCTURE OF YEAST FSH1/YHR049W, A MEMBER OF THE
TITLE 2 SERINE HYDROLASE FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL 27.3 KDA PROTEIN IN AAP1-SMF2
COMPND 3 INTERGENIC REGION;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: S. CEREVISIAE YHR049WP;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 GENE: YHR049W;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS ESTERASE, LIPASE, SERINE HYDROLASE, S. CEREVISIAE,
KEYWDS 2 STRUCTURAL GENOMICS, PARIS-SUD YEAST STRUCTURAL GENOMICS,
KEYWDS 3 YSG
EXPDTA X-RAY DIFFRACTION
AUTHOR N.LEULLIOT,M.GRAILLE,F.COSTE,S.QUEVILLON-CHERUEL,J.JANIN,
AUTHOR 2 H.VAN TILBEURGH,PARIS-SUD YEAST STRUCTURAL GENOMICS (YSG)
REVDAT 1 10-MAY-05 1YCD 0
JRNL AUTH S.QUEVILLON-CHERUEL,N.LEULLIOT,M.GRAILLE,
JRNL AUTH 2 N.HERVOUET,F.COSTE,C.ZELWER,J.JANIN,H.VAN TILBEURGH
JRNL TITL CRYSTAL STRUCTURE OF YEAST YHR049W/FSH1, A MEMBER
JRNL TITL 2 OF THE SERINE HYDROLASE FAMILY.
JRNL REF PROTEIN SCI. V. 14 1350 2005
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 54126
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2873
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3622
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4732
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.56000
REMARK 3 B22 (A**2) : 0.99000
REMARK 3 B33 (A**2) : -0.47000
REMARK 3 B12 (A**2) : 0.18000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : -0.39000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.958
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3880 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5242 ; 1.283 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 469 ; 5.071 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 171 ;32.863 ;25.205
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 697 ;12.056 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.767 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 574 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2887 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2007 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2669 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 694 ; 0.136 ; 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): 59 ; 0.152 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 65 ; 0.125 ; 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): 2439 ; 0.797 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3840 ; 1.260 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1623 ; 2.060 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1402 ; 3.358 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 1YCD COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-2005.
REMARK 100 THE RCSB ID CODE IS RCSB031371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 57009
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 1.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.16500
REMARK 200 FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG 4K, 0.1M MES, PH 5.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 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: 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
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 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 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 240
REMARK 465 ALA A 241
REMARK 465 SER A 242
REMARK 465 GLU A 243
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 VAL B 3
REMARK 465 SER B 242
REMARK 465 GLU B 243
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 LEU A 109 C SER A 110 N 0.156
REMARK 500 SER A 110 C GLN A 111 N 0.317
REMARK 500 LEU B 109 C SER B 110 N 0.217
REMARK 500 SER B 110 C GLN B 111 N 0.289
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 SER A 110 C - N - CA ANGL. DEV. = 8.5 DEGREES
REMARK 500 SER A 110 O - C - N ANGL. DEV. = -8.9 DEGREES
REMARK 500 SER B 110 O - C - N ANGL. DEV. =-10.1 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 SER A 110 -106.68 50.75
REMARK 500 SER B 110 -111.96 51.75
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 431 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH 542 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH 784 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH 806 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH 815 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH 831 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH 879 DISTANCE = 5.74 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE AUTHOR STATES THAT THE LI5 RESIDUE
REMARK 600 IN MOLECULE B DOES NOT CONTAIN C32 ATOM
REMARK 600 BECAUSE THIS ATOM WAS NOT DETECTED IN THE
REMARK 600 ELECTRON DENSITY FOR MOLECULE B BUT WAS
REMARK 600 DETECTED IN MOLECULE A.
DBREF 1YCD A 1 243 SWS P38777 YHK9_YEAST 1 243
DBREF 1YCD B 1 243 SWS P38777 YHK9_YEAST 1 243
SEQADV 1YCD LEU A 109 SWS P38777 PHE 109 ENGINEERED
SEQADV 1YCD LEU B 109 SWS P38777 PHE 109 ENGINEERED
SEQRES 1 A 243 MET THR VAL GLN ILE PRO LYS LEU LEU PHE LEU HIS GLY
SEQRES 2 A 243 PHE LEU GLN ASN GLY LYS VAL PHE SER GLU LYS SER SER
SEQRES 3 A 243 GLY ILE ARG LYS LEU LEU LYS LYS ALA ASN VAL GLN CYS
SEQRES 4 A 243 ASP TYR ILE ASP ALA PRO VAL LEU LEU GLU LYS LYS ASP
SEQRES 5 A 243 LEU PRO PHE GLU MET ASP ASP GLU LYS TRP GLN ALA THR
SEQRES 6 A 243 LEU ASP ALA ASP VAL ASN ARG ALA TRP PHE TYR HIS SER
SEQRES 7 A 243 GLU ILE SER HIS GLU LEU ASP ILE SER GLU GLY LEU LYS
SEQRES 8 A 243 SER VAL VAL ASP HIS ILE LYS ALA ASN GLY PRO TYR ASP
SEQRES 9 A 243 GLY ILE VAL GLY LEU SER GLN GLY ALA ALA LEU SER SER
SEQRES 10 A 243 ILE ILE THR ASN LYS ILE SER GLU LEU VAL PRO ASP HIS
SEQRES 11 A 243 PRO GLN PHE LYS VAL SER VAL VAL ILE SER GLY TYR SER
SEQRES 12 A 243 PHE THR GLU PRO ASP PRO GLU HIS PRO GLY GLU LEU ARG
SEQRES 13 A 243 ILE THR GLU LYS PHE ARG ASP SER PHE ALA VAL LYS PRO
SEQRES 14 A 243 ASP MET LYS THR LYS MET ILE PHE ILE TYR GLY ALA SER
SEQRES 15 A 243 ASP GLN ALA VAL PRO SER VAL ARG SER LYS TYR LEU TYR
SEQRES 16 A 243 ASP ILE TYR LEU LYS ALA GLN ASN GLY ASN LYS GLU LYS
SEQRES 17 A 243 VAL LEU ALA TYR GLU HIS PRO GLY GLY HIS MET VAL PRO
SEQRES 18 A 243 ASN LYS LYS ASP ILE ILE ARG PRO ILE VAL GLU GLN ILE
SEQRES 19 A 243 THR SER SER LEU GLN GLU ALA SER GLU
SEQRES 1 B 243 MET THR VAL GLN ILE PRO LYS LEU LEU PHE LEU HIS GLY
SEQRES 2 B 243 PHE LEU GLN ASN GLY LYS VAL PHE SER GLU LYS SER SER
SEQRES 3 B 243 GLY ILE ARG LYS LEU LEU LYS LYS ALA ASN VAL GLN CYS
SEQRES 4 B 243 ASP TYR ILE ASP ALA PRO VAL LEU LEU GLU LYS LYS ASP
SEQRES 5 B 243 LEU PRO PHE GLU MET ASP ASP GLU LYS TRP GLN ALA THR
SEQRES 6 B 243 LEU ASP ALA ASP VAL ASN ARG ALA TRP PHE TYR HIS SER
SEQRES 7 B 243 GLU ILE SER HIS GLU LEU ASP ILE SER GLU GLY LEU LYS
SEQRES 8 B 243 SER VAL VAL ASP HIS ILE LYS ALA ASN GLY PRO TYR ASP
SEQRES 9 B 243 GLY ILE VAL GLY LEU SER GLN GLY ALA ALA LEU SER SER
SEQRES 10 B 243 ILE ILE THR ASN LYS ILE SER GLU LEU VAL PRO ASP HIS
SEQRES 11 B 243 PRO GLN PHE LYS VAL SER VAL VAL ILE SER GLY TYR SER
SEQRES 12 B 243 PHE THR GLU PRO ASP PRO GLU HIS PRO GLY GLU LEU ARG
SEQRES 13 B 243 ILE THR GLU LYS PHE ARG ASP SER PHE ALA VAL LYS PRO
SEQRES 14 B 243 ASP MET LYS THR LYS MET ILE PHE ILE TYR GLY ALA SER
SEQRES 15 B 243 ASP GLN ALA VAL PRO SER VAL ARG SER LYS TYR LEU TYR
SEQRES 16 B 243 ASP ILE TYR LEU LYS ALA GLN ASN GLY ASN LYS GLU LYS
SEQRES 17 B 243 VAL LEU ALA TYR GLU HIS PRO GLY GLY HIS MET VAL PRO
SEQRES 18 B 243 ASN LYS LYS ASP ILE ILE ARG PRO ILE VAL GLU GLN ILE
SEQRES 19 B 243 THR SER SER LEU GLN GLU ALA SER GLU
HET LI5 A 800 14
HET LI5 B 800 13
HETNAM LI5 2-HYDROXY-4,5-DIOXOHEPTYL HYDROGEN PHOSPHONATE
FORMUL 3 LI5 2(C7 H12 O6 P1)
FORMUL 5 HOH *936(H2 O1)
HELIX 1 1 ASN A 17 SER A 25 1 9
HELIX 2 2 SER A 25 ALA A 35 1 11
HELIX 3 3 GLU A 49 LEU A 53 5 5
HELIX 4 4 ASP A 58 ALA A 68 1 11
HELIX 5 5 ILE A 80 LEU A 84 5 5
HELIX 6 6 ILE A 86 GLY A 101 1 16
HELIX 7 7 SER A 110 VAL A 127 1 18
HELIX 8 8 GLU A 159 ARG A 162 5 4
HELIX 9 9 PRO A 187 GLN A 202 1 16
HELIX 10 10 LYS A 223 GLN A 239 1 17
HELIX 11 11 ASN B 17 SER B 25 1 9
HELIX 12 12 SER B 25 ALA B 35 1 11
HELIX 13 13 GLU B 49 LEU B 53 5 5
HELIX 14 14 ASP B 58 ALA B 68 1 11
HELIX 15 15 ILE B 80 LEU B 84 5 5
HELIX 16 16 ILE B 86 GLY B 101 1 16
HELIX 17 17 SER B 110 VAL B 127 1 18
HELIX 18 18 GLU B 159 ARG B 162 5 4
HELIX 19 19 PRO B 187 GLN B 202 1 16
HELIX 20 20 LYS B 223 GLN B 239 1 17
SHEET 1 A 6 GLN A 38 ILE A 42 0
SHEET 2 A 6 LYS A 7 LEU A 11 1 N LEU A 8 O GLN A 38
SHEET 3 A 6 GLY A 105 LEU A 109 1 O VAL A 107 N LEU A 11
SHEET 4 A 6 VAL A 135 ILE A 139 1 O VAL A 137 N ILE A 106
SHEET 5 A 6 LYS A 174 GLY A 180 1 O ILE A 176 N SER A 136
SHEET 6 A 6 VAL A 209 HIS A 214 1 O LEU A 210 N PHE A 177
SHEET 1 B 2 VAL A 46 LEU A 47 0
SHEET 2 B 2 ARG A 72 ALA A 73 -1 O ALA A 73 N VAL A 46
SHEET 1 C 2 THR A 145 PRO A 147 0
SHEET 2 C 2 LEU A 155 ILE A 157 -1 O ARG A 156 N GLU A 146
SHEET 1 D 6 GLN B 38 ILE B 42 0
SHEET 2 D 6 LYS B 7 LEU B 11 1 N PHE B 10 O ASP B 40
SHEET 3 D 6 GLY B 105 LEU B 109 1 O VAL B 107 N LEU B 11
SHEET 4 D 6 VAL B 135 ILE B 139 1 O VAL B 137 N ILE B 106
SHEET 5 D 6 LYS B 174 GLY B 180 1 O ILE B 176 N VAL B 138
SHEET 6 D 6 VAL B 209 HIS B 214 1 O LEU B 210 N MET B 175
SHEET 1 E 2 VAL B 46 LEU B 47 0
SHEET 2 E 2 ARG B 72 ALA B 73 -1 O ALA B 73 N VAL B 46
SHEET 1 F 2 THR B 145 PRO B 147 0
SHEET 2 F 2 LEU B 155 ILE B 157 -1 O ARG B 156 N GLU B 146
LINK OG SER A 110 P LI5 A 800
LINK OG SER B 110 P LI5 B 800
CISPEP 1 VAL A 3 GLN A 4 0 -0.39
CISPEP 2 GLY A 101 PRO A 102 0 3.85
CISPEP 3 GLY B 101 PRO B 102 0 0.19
CRYST1 46.133 53.329 64.271 102.85 90.04 112.47 P 1 2
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 0.021676 0.008966 0.002239 0.00000
SCALE2 0.000000 0.020292 0.005036 0.00000
SCALE3 0.000000 0.000000 0.016031 0.00000
TER 1882 GLN A 239
TER 3771 ALA B 241
MASTER 309 0 2 20 20 0 0 6 4732 2 29 38
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