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HEADER HYDROLASE 28-MAR-11 3RAR
TITLE X-RAY STRUCTURE OF A BOUND PHOSPHONATE TRANSITION STATE ANALOG AND
TITLE 2 ENANTIOSELECTIVITY OF CANDIDA RUGOSA LIPASE TOWARD CHIRAL CARBOXYLIC
TITLE 3 ACIDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 16-549;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA RUGOSA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5481;
SOURCE 5 GENE: LIP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE, CALCIUM BINDING, (RC,RP)-
KEYWDS 2 METHYL[1-(METHOXY)PHENYLMETHYL]PHOSPHONYL ADDUCT AT O OF SERINE 209
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GROCHULSKI,R.KAZLAUSKAS
REVDAT 1 27-APR-11 3RAR 0
JRNL AUTH P.GROCHULSKI,R.KAZLAUSKAS
JRNL TITL X-RAY STRUCTURE OF A BOUND PHOSPHONATE TRANSITION STATE
JRNL TITL 2 ANALOG AND ENANTIOSELECTIVITY OF CANDIDA RUGOSA LIPASE
JRNL TITL 3 TOWARD CHIRAL CARBOXYLIC ACIDS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 564032.690
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.9
REMARK 3 NUMBER OF REFLECTIONS : 23670
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 SET) : 0.171
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2334
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2716
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 297
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4022
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.62000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 1.42000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.76
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.160 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.630 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 76.86
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : IAN.PAR
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : IAN.TOP
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RAR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064700.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-95; NULL
REMARK 200 TEMPERATURE (KELVIN) : 298; NULL
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; NULL
REMARK 200 RADIATION SOURCE : ROTATING ANODE; NULL
REMARK 200 BEAMLINE : NULL; NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU; OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; NULL
REMARK 200 MONOCHROMATOR : GRAPHITE; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; NULL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : RAXIS
REMARK 200 DATA SCALING SOFTWARE : RAXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23670
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 54.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1LPP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% (V/V) 2-METHYL-2,4-PENTANEDIOL, 30
REMARK 280 MM SODIUM ACETATE BUFFER AND 30 MM CACL2., PH 5.3, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.05000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.05000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.75000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.75000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 88.05000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.50000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.75000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 88.05000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.50000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.75000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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: 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 130.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -88.05000
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 ILE A 18 -61.94 74.28
REMARK 500 PRO A 32 50.46 -69.69
REMARK 500 PHE A 38 -4.65 62.44
REMARK 500 THR A 68 156.90 179.34
REMARK 500 PHE A 125 19.66 59.45
REMARK 500 SER A 159 -154.00 66.06
REMARK 500 SER A 209 -116.90 55.70
REMARK 500 SER A 241 75.18 66.04
REMARK 500 ALA A 243 -121.76 -116.37
REMARK 500 SER A 301 -121.97 43.24
REMARK 500 VAL A 313 -59.36 -125.47
REMARK 500 ASP A 317 -178.53 -171.41
REMARK 500 ASP A 340 69.50 -112.57
REMARK 500 ASP A 384 106.47 -29.74
REMARK 500 PHE A 415 -71.91 -138.71
REMARK 500 VAL A 444 -46.00 67.96
REMARK 500 ASN A 468 -80.60 -117.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 IAN A 560
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 A 590 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 326 O
REMARK 620 2 HOH A 538 O 128.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 589 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 260 OD1
REMARK 620 2 HOH A 682 O 82.2
REMARK 620 3 ASP A 260 OD2 45.4 101.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 991
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 992
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 994
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 589
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 590
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IAN A 560
DBREF 3RAR A 1 534 UNP P20261 LIP1_CANRU 16 549
SEQRES 1 A 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 A 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE
SEQRES 3 A 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS
SEQRES 4 A 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASP GLY GLN LYS
SEQRES 5 A 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO
SEQRES 6 A 534 GLU GLY THR TYR GLU GLU ASN LEU PRO LYS ALA ALA LEU
SEQRES 7 A 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLU ALA VAL SER
SEQRES 8 A 534 PRO SER SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG
SEQRES 9 A 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET
SEQRES 10 A 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU VAL GLY GLY THR
SEQRES 11 A 534 SER THR PHE PRO PRO ALA GLN MET ILE THR LYS SER ILE
SEQRES 12 A 534 ALA MET GLY LYS PRO ILE ILE HIS VAL SER VAL ASN TYR
SEQRES 13 A 534 ARG VAL SER SER TRP GLY PHE LEU ALA GLY ASP GLU ILE
SEQRES 14 A 534 LYS ALA GLU GLY SER ALA ASN ALA GLY LEU LYS ASP GLN
SEQRES 15 A 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA ALA
SEQRES 16 A 534 PHE GLY GLY ASP PRO THR LYS VAL THR ILE PHE GLY GLU
SEQRES 17 A 534 SER ALA GLY SER MET SER VAL MET CYS HIS ILE LEU TRP
SEQRES 18 A 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE
SEQRES 19 A 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER
SEQRES 20 A 534 ASP ALA VAL ASP GLY ILE TYR GLY ASN GLU ILE PHE ASP
SEQRES 21 A 534 LEU LEU ALA SER ASN ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 A 534 LYS LEU ALA CYS LEU ARG GLY VAL SER SER ASP THR LEU
SEQRES 23 A 534 GLU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR
SEQRES 24 A 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 A 534 VAL ASN ILE THR ASP ASP MET TYR ALA LEU VAL ARG GLU
SEQRES 26 A 534 GLY LYS TYR ALA ASN ILE PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 A 534 ASN ASP GLU GLY THR PHE PHE GLY THR SER SER LEU ASN
SEQRES 28 A 534 VAL THR THR ASP ALA GLN ALA ARG GLU TYR PHE LYS GLN
SEQRES 29 A 534 SER PHE VAL HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 A 534 MET THR ALA TYR PRO GLY ASP ILE THR GLN GLY SER PRO
SEQRES 31 A 534 PHE ASP THR GLY ILE LEU ASN ALA LEU THR PRO GLN PHE
SEQRES 32 A 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU GLY PHE THR
SEQRES 33 A 534 LEU ALA ARG ARG TYR PHE LEU ASN HIS TYR THR GLY GLY
SEQRES 34 A 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 A 534 PRO VAL LEU GLY THR PHE HIS SER ASN ASP ILE VAL PHE
SEQRES 36 A 534 GLN ASP TYR LEU LEU GLY SER GLY SER LEU ILE TYR ASN
SEQRES 37 A 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN
SEQRES 38 A 534 THR ALA GLY LEU LEU VAL LYS TRP PRO GLU TYR THR SER
SEQRES 39 A 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA
SEQRES 40 A 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA
SEQRES 41 A 534 GLY TYR ASP ALA LEU PHE SER ASN PRO PRO SER PHE PHE
SEQRES 42 A 534 VAL
MODRES 3RAR ASN A 351 ASN GLYCOSYLATION SITE
MODRES 3RAR ASN A 314 ASN GLYCOSYLATION SITE
HET NAG A 991 14
HET NAG A 992 14
HET NAG A 994 14
HET CA A 589 1
HET CA A 590 1
HET IAN A 560 13
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CA CALCIUM ION
HETNAM IAN METHYL HYDROGEN (R)-[(R)-METHOXY(PHENYL)
HETNAM 2 IAN METHYL]PHOSPHONATE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 4 CA 2(CA 2+)
FORMUL 6 IAN C9 H13 O4 P
FORMUL 7 HOH *174(H2 O)
HELIX 1 1 VAL A 33 ARG A 37 5 5
HELIX 2 2 ASN A 72 GLN A 83 1 12
HELIX 3 3 SER A 84 SER A 91 1 8
HELIX 4 4 GLY A 129 PHE A 133 5 5
HELIX 5 5 PRO A 135 MET A 145 1 11
HELIX 6 6 SER A 159 LEU A 164 1 6
HELIX 7 7 GLY A 166 GLY A 173 1 8
HELIX 8 8 ASN A 176 ILE A 193 1 18
HELIX 9 9 ALA A 194 PHE A 196 5 3
HELIX 10 10 SER A 209 TRP A 221 1 13
HELIX 11 11 ASN A 222 ASP A 225 5 4
HELIX 12 12 GLY A 252 ALA A 266 1 15
HELIX 13 13 ASP A 273 ARG A 279 1 7
HELIX 14 14 SER A 282 ASN A 291 1 10
HELIX 15 15 ASP A 318 GLU A 325 1 8
HELIX 16 16 GLY A 342 THR A 347 1 6
HELIX 17 17 SER A 348 LEU A 350 5 3
HELIX 18 18 THR A 354 PHE A 366 1 13
HELIX 19 19 SER A 370 TYR A 381 1 12
HELIX 20 20 ASP A 384 GLY A 388 5 5
HELIX 21 21 GLN A 402 PHE A 415 1 14
HELIX 22 22 PHE A 415 ASN A 424 1 10
HELIX 23 23 SER A 450 TYR A 458 1 9
HELIX 24 24 GLY A 463 ASN A 468 1 6
HELIX 25 25 ASN A 468 LEU A 478 1 11
HELIX 26 26 ASP A 479 GLY A 484 5 6
HELIX 27 27 ARG A 518 SER A 527 1 10
HELIX 28 28 ASN A 528 PHE A 533 5 6
SHEET 1 A 2 THR A 3 THR A 5 0
SHEET 2 A 2 THR A 11 THR A 13 -1 O ILE A 12 N ALA A 4
SHEET 1 B11 LEU A 15 ASN A 16 0
SHEET 2 B11 GLU A 21 PRO A 27 -1 O ALA A 22 N LEU A 15
SHEET 3 B11 THR A 99 ARG A 104 -1 O ILE A 100 N ILE A 26
SHEET 4 B11 ILE A 150 VAL A 154 -1 O HIS A 151 N VAL A 103
SHEET 5 B11 LEU A 114 ILE A 120 1 N TRP A 119 O VAL A 152
SHEET 6 B11 GLY A 198 GLU A 208 1 O LYS A 202 N VAL A 116
SHEET 7 B11 ALA A 236 GLN A 240 1 O ALA A 236 N ILE A 205
SHEET 8 B11 VAL A 333 GLN A 338 1 O ILE A 334 N MET A 239
SHEET 9 B11 LYS A 431 SER A 436 1 O SER A 436 N ASP A 337
SHEET 10 B11 LEU A 502 ILE A 505 1 O MET A 503 N SER A 433
SHEET 11 B11 LEU A 510 GLY A 513 -1 O TYR A 511 N MET A 504
SHEET 1 C 2 THR A 227 TYR A 228 0
SHEET 2 C 2 LYS A 231 PRO A 232 -1 O LYS A 231 N TYR A 228
SSBOND 1 CYS A 60 CYS A 97 1555 1555 2.03
SSBOND 2 CYS A 268 CYS A 277 1555 1555 2.03
LINK O4 NAG A 992 C1 NAG A 994 1555 1555 1.40
LINK ND2 ASN A 351 C1 NAG A 992 1555 1555 1.45
LINK ND2 ASN A 314 C1 NAG A 991 1555 1555 1.46
LINK O GLY A 326 CA CA A 590 1555 1555 2.72
LINK OD1 ASP A 260 CA CA A 589 1555 1555 2.77
LINK CA CA A 590 O HOH A 538 1555 1555 2.81
LINK CA CA A 589 O HOH A 682 1555 1555 2.86
LINK OD2 ASP A 260 CA CA A 589 1555 1555 2.91
LINK OG SER A 209 P1 IAN A 560 1555 1555 1.65
CISPEP 1 SER A 389 PRO A 390 0 0.02
SITE 1 AC1 5 TRP A 221 ASN A 222 VAL A 313 ASN A 314
SITE 2 AC1 5 HOH A 709
SITE 1 AC2 5 GLU A 70 TYR A 299 ASN A 351 GLN A 357
SITE 2 AC2 5 NAG A 994
SITE 1 AC3 3 TYR A 69 GLU A 70 NAG A 992
SITE 1 AC4 2 ASP A 260 HOH A 682
SITE 1 AC5 2 GLY A 326 HOH A 538
SITE 1 AC6 11 GLY A 122 GLY A 123 GLY A 124 SER A 209
SITE 2 AC6 11 ALA A 210 MET A 213 PHE A 296 LEU A 302
SITE 3 AC6 11 LEU A 304 PHE A 345 HIS A 449
CRYST1 65.000 97.500 176.100 90.00 90.00 90.00 C 2 2 21 8
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 0.015385 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005679 0.00000
TER 4023 VAL A 534
MASTER 336 0 6 28 15 0 10 6 4253 1 69 42
END |