HEADER HYDROLASE 09-SEP-05 2AYW
TITLE CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN TRYPSIN AND A DESIGNED
TITLE 2 SYNTHETIC HIGHLY POTENT INHIBITOR IN THE PRESENCE OF BENZAMIDINE AT
TITLE 3 0.97 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN;
COMPND 5 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS TRYPSIN, BENZAMIDINE, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SHERAWAT,P.KAUR,M.PERBANDT,C.BETZEL,W.A.SLUSARCHYK,G.S.BISACCHI,
AUTHOR 2 C.CHANG,B.L.JACOBSON,H.M.EINSPAHR,T.P.SINGH
REVDAT 7 25-OCT-23 2AYW 1 REMARK LINK
REVDAT 6 11-OCT-17 2AYW 1 REMARK
REVDAT 5 13-JUL-11 2AYW 1 VERSN
REVDAT 4 09-JUN-09 2AYW 1 REVDAT
REVDAT 3 24-FEB-09 2AYW 1 VERSN
REVDAT 2 20-JAN-09 2AYW 1 JRNL
REVDAT 1 17-JAN-06 2AYW 0
JRNL AUTH M.SHERAWAT,P.KAUR,M.PERBANDT,C.BETZEL,W.A.SLUSARCHYK,
JRNL AUTH 2 G.S.BISACCHI,C.CHANG,B.L.JACOBSON,H.M.EINSPAHR,T.P.SINGH
JRNL TITL STRUCTURE OF THE COMPLEX OF TRYPSIN WITH A HIGHLY POTENT
JRNL TITL 2 SYNTHETIC INHIBITOR AT 0.97 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 500 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17372355
JRNL DOI 10.1107/S090744490700697X
REMARK 2
REMARK 2 RESOLUTION. 0.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 0.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 114997
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) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1167
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) : 0.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8046
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1629
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.23000
REMARK 3 B12 (A**2) : -0.08000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.020
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.021
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.015
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.589
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1787 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1518 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2426 ; 1.660 ; 2.010
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3569 ; 2.908 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 222 ; 6.727 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 59 ;39.973 ;25.593
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 280 ;13.236 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;18.526 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 259 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1984 ; 0.019 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 343 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 367 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1502 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 913 ; 0.182 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 951 ; 0.094 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 262 ; 0.182 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.097 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 38 ; 0.244 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 96 ; 0.281 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 124 ; 0.243 ; 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): 1128 ; 1.284 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 468 ; 0.548 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1772 ; 1.794 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 841 ; 3.038 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 654 ; 3.270 ; 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): 3791 ; 1.945 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 450 ; 5.517 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3265 ; 2.546 ; 3.000
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 : 1.20
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2AYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116664
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.970
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1JRT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5MM MES, 1MM CACL2, 2.5MM BENZAMIDINE,
REMARK 280 PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.88667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.44333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 24.44333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 48.88667
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 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 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 A 117 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -3.9 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 71 -79.82 -121.28
REMARK 500 ASN A 97 -60.71 -90.65
REMARK 500 SER A 214 -68.47 -120.90
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 MES A 901
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 250 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 90.8
REMARK 620 3 VAL A 75 O 164.0 81.1
REMARK 620 4 GLU A 80 OE2 102.6 159.5 89.1
REMARK 620 5 HOH A 922 O 79.6 103.6 88.9 94.1
REMARK 620 6 HOH A 940 O 82.6 88.1 110.7 78.5 158.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ONO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ONO A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
DBREF 2AYW A 16 245 UNP P00760 TRY1_BOVIN 21 243
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A 250 1
HET ONO A 501 39
HET ONO A 601 39
HET BEN A 801 9
HET MES A 901 11
HET GOL A 701 6
HETNAM CA CALCIUM ION
HETNAM ONO 2-[2-({[4-(DIAMINOMETHYL)PHENYL]AMINO}CARBONYL)-6-
HETNAM 2 ONO METHOXYPYRIDIN-3-YL]-5-{[(1-FORMYL-2,2-
HETNAM 3 ONO DIMETHYLPROPYL)AMINO]CARBONYL}BENZOIC ACID
HETNAM BEN BENZAMIDINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CA CA 2+
FORMUL 3 ONO 2(C28 H31 N5 O6)
FORMUL 5 BEN C7 H8 N2
FORMUL 6 MES C6 H13 N O4 S
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *449(H2 O)
HELIX 1 1 ALA A 55 TYR A 59 5 5
HELIX 2 2 SER A 164 TYR A 172 1 9
HELIX 3 3 TYR A 234 ASN A 245 1 12
SHEET 1 A 7 TYR A 20 THR A 21 0
SHEET 2 A 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 A 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 A 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O MET A 104 N SER A 54
SHEET 5 B 7 GLN A 81 VAL A 90 -1 N ILE A 89 O LEU A 105
SHEET 6 B 7 GLN A 64 LEU A 67 -1 N VAL A 65 O ILE A 83
SHEET 7 B 7 GLN A 30 ASN A 34 -1 N ASN A 34 O GLN A 64
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.04
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.02
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.04
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.05
LINK OE1 GLU A 70 CA CA A 250 1555 1555 2.29
LINK O ASN A 72 CA CA A 250 1555 1555 2.32
LINK O VAL A 75 CA CA A 250 1555 1555 2.30
LINK OE2 GLU A 80 CA CA A 250 1555 1555 2.33
LINK CA CA A 250 O HOH A 922 1555 1555 2.35
LINK CA CA A 250 O HOH A 940 1555 1555 2.40
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A 922 HOH A 940
SITE 1 AC2 25 HIS A 40 HIS A 57 ALA A 132 GLY A 133
SITE 2 AC2 25 TYR A 151 ASP A 189 SER A 190 GLN A 192
SITE 3 AC2 25 GLY A 193 SER A 195 SER A 214 TRP A 215
SITE 4 AC2 25 GLY A 216 GLY A 219 CYS A 220 GLY A 226
SITE 5 AC2 25 ONO A 601 HOH A 955 HOH A1024 HOH A1093
SITE 6 AC2 25 HOH A1095 HOH A1160 HOH A1214 HOH A1327
SITE 7 AC2 25 HOH A1330
SITE 1 AC3 17 TYR A 20 THR A 21 ASN A 143 GLY A 148
SITE 2 AC3 17 LYS A 159 GLN A 192 GLY A 216 ONO A 501
SITE 3 AC3 17 BEN A 801 HOH A 956 HOH A 997 HOH A1047
SITE 4 AC3 17 HOH A1063 HOH A1074 HOH A1105 HOH A1229
SITE 5 AC3 17 HOH A1247
SITE 1 AC4 10 GLN A 135 ONO A 601 HOH A1000 HOH A1015
SITE 2 AC4 10 HOH A1092 HOH A1144 HOH A1159 HOH A1192
SITE 3 AC4 10 HOH A1248 HOH A1286
SITE 1 AC5 9 GLU A 80 GLN A 81 SER A 113 HOH A1077
SITE 2 AC5 9 HOH A1102 HOH A1142 HOH A1218 HOH A1264
SITE 3 AC5 9 HOH A1280
SITE 1 AC6 10 ALA A 85 SER A 86 LYS A 87 SER A 88
SITE 2 AC6 10 TYR A 94 ASN A 95 HOH A 918 HOH A 992
SITE 3 AC6 10 HOH A1104 HOH A1137
CRYST1 68.550 68.550 73.330 90.00 90.00 120.00 P 32 2 1 6
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 0.014588 0.008422 0.000000 0.00000
SCALE2 0.000000 0.016845 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013637 0.00000
(ATOM LINES ARE NOT SHOWN.)
END