HEADER HYDROLASE 05-OCT-09 3A88
TITLE CRYSTAL STRUCTURE OF TRYPSIN COMPLEXED WITH (E)-4-((2-
TITLE 2 NICOTINOYLHYDRAZONO)METHYL)BENZIMIDAMIDE (SOAKING 30 MINUTES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN, ALPHA-TRYPSIN CHAIN 1, ALPHA-TRYPSIN CHAIN 2;
COMPND 5 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS IN-CRYSTAL CHEMICAL LIGATION, DISULFIDE BOND, HYDROLASE, METAL-
KEYWDS 2 BINDING, PROTEASE, SECRETED, SERINE PROTEASE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YAMANE,M.YAO,I.TANAKA
REVDAT 2 01-NOV-23 3A88 1 REMARK LINK
REVDAT 1 29-SEP-10 3A88 0
JRNL AUTH J.YAMANE,N.OOYABU,M.YAO,H.TAKEMOTO,I.TANAKA
JRNL TITL IN-CRYSTAL CHEMICAL LIGATION FOR DRUG DISCOVERY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 20574
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1087
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1333
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.2430
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 : 43
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.34000
REMARK 3 B22 (A**2) : -0.69000
REMARK 3 B33 (A**2) : 0.35000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.111
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.819
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1705 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2313 ; 1.198 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 222 ; 6.281 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 58 ;40.641 ;25.862
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 269 ;11.270 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;16.505 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 254 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1264 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 822 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1166 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 249 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.116 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 45 ; 0.217 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 41 ; 0.186 ; 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): 1126 ; 0.669 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1762 ; 1.120 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 673 ; 1.762 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 551 ; 2.591 ; 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): 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 : 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 3A88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000028934.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.13100
REMARK 200 R SYM FOR SHELL (I) : 0.13100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: LAFIRE
REMARK 200 STARTING MODEL: 3A7T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 30% PEG 3350, 0.2M
REMARK 280 LITHIUM SULFATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 27.23650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.29300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.15500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.29300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.23650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.15500
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 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 -82.36 -116.79
REMARK 500 SER A 145 -61.30 -102.87
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 CA A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 18 O
REMARK 620 2 GLU A 70 OE1 78.0
REMARK 620 3 ASN A 72 O 101.8 89.7
REMARK 620 4 VAL A 75 O 90.2 162.3 79.7
REMARK 620 5 GLU A 80 OE2 96.4 103.8 159.3 90.5
REMARK 620 6 HOH A 309 O 162.7 88.3 88.5 105.4 76.5
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H06 A 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A7T RELATED DB: PDB
REMARK 900 RELATED ID: 3A7V RELATED DB: PDB
REMARK 900 RELATED ID: 3A7W RELATED DB: PDB
REMARK 900 RELATED ID: 3A7X RELATED DB: PDB
REMARK 900 RELATED ID: 3A7Y RELATED DB: PDB
REMARK 900 RELATED ID: 3A7Z RELATED DB: PDB
REMARK 900 RELATED ID: 3A80 RELATED DB: PDB
REMARK 900 RELATED ID: 3A81 RELATED DB: PDB
REMARK 900 RELATED ID: 3A82 RELATED DB: PDB
REMARK 900 RELATED ID: 3A83 RELATED DB: PDB
REMARK 900 RELATED ID: 3A84 RELATED DB: PDB
REMARK 900 RELATED ID: 3A85 RELATED DB: PDB
REMARK 900 RELATED ID: 3A86 RELATED DB: PDB
REMARK 900 RELATED ID: 3A87 RELATED DB: PDB
REMARK 900 RELATED ID: 3A89 RELATED DB: PDB
REMARK 900 RELATED ID: 3A8A RELATED DB: PDB
REMARK 900 RELATED ID: 3A8B RELATED DB: PDB
REMARK 900 RELATED ID: 3A8C RELATED DB: PDB
REMARK 900 RELATED ID: 3A8D RELATED DB: PDB
DBREF 3A88 A 19 241 UNP P00760 TRY1_BOVIN 24 246
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 1 1
HET GOL A 2 6
HET GOL A 3 6
HET SO4 A 4 5
HET SO4 A 5 5
HET H06 A 6 20
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM H06 (E)-4-((2-NICOTINOYLHYDRAZONO)METHYL)BENZIMIDAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CA CA 2+
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 H06 C14 H13 N5 O
FORMUL 8 HOH *324(H2 O)
HELIX 1 1 ALA A 56 TYR A 60 5 5
HELIX 2 2 SER A 162 TYR A 170 1 9
HELIX 3 3 TYR A 230 SER A 240 1 11
SHEET 1 A 7 TYR A 23 THR A 24 0
SHEET 2 A 7 LYS A 154 PRO A 159 -1 O CYS A 155 N TYR A 23
SHEET 3 A 7 GLN A 133 GLY A 138 -1 N ILE A 136 O LEU A 156
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 135
SHEET 5 A 7 LYS A 204 TRP A 211 -1 O LYS A 204 N CYS A 201
SHEET 6 A 7 GLY A 222 LYS A 226 -1 O VAL A 223 N TRP A 211
SHEET 7 A 7 MET A 178 ALA A 181 -1 N PHE A 179 O TYR A 224
SHEET 1 B 7 GLN A 33 ASN A 37 0
SHEET 2 B 7 HIS A 41 ASN A 49 -1 O CYS A 43 N LEU A 36
SHEET 3 B 7 TRP A 52 SER A 55 -1 O VAL A 54 N SER A 46
SHEET 4 B 7 MET A 104 LEU A 108 -1 O MET A 104 N SER A 55
SHEET 5 B 7 GLN A 81 VAL A 90 -1 N SER A 86 O LYS A 107
SHEET 6 B 7 GLN A 65 LEU A 68 -1 N LEU A 68 O GLN A 81
SHEET 7 B 7 GLN A 33 ASN A 37 -1 N SER A 35 O ARG A 67
SSBOND 1 CYS A 25 CYS A 155 1555 1555 2.03
SSBOND 2 CYS A 43 CYS A 59 1555 1555 2.05
SSBOND 3 CYS A 127 CYS A 228 1555 1555 2.04
SSBOND 4 CYS A 134 CYS A 201 1555 1555 2.03
SSBOND 5 CYS A 166 CYS A 180 1555 1555 2.05
SSBOND 6 CYS A 191 CYS A 215 1555 1555 2.03
LINK CA CA A 1 O HOH A 18 1555 1555 2.51
LINK CA CA A 1 OE1 GLU A 70 1555 1555 2.27
LINK CA CA A 1 O ASN A 72 1555 1555 2.40
LINK CA CA A 1 O VAL A 75 1555 1555 2.24
LINK CA CA A 1 OE2 GLU A 80 1555 1555 2.34
LINK CA CA A 1 O HOH A 309 1555 1555 2.36
SITE 1 AC1 6 HOH A 18 GLU A 70 ASN A 72 VAL A 75
SITE 2 AC1 6 GLU A 80 HOH A 309
SITE 1 AC2 5 VAL A 76 GLU A 80 GLN A 81 PHE A 82
SITE 2 AC2 5 HOH A 264
SITE 1 AC3 9 ALA A 111 CYS A 127 LYS A 226 HOH A 277
SITE 2 AC3 9 HOH A 321 HOH A 367 HOH A 420 HOH A 455
SITE 3 AC3 9 HOH A 541
SITE 1 AC4 7 LYS A 167 PRO A 171 GLY A 172 HOH A 342
SITE 2 AC4 7 HOH A 478 HOH A 537 HOH A 550
SITE 1 AC5 8 SER A 162 ASP A 163 SER A 164 HOH A 253
SITE 2 AC5 8 HOH A 258 HOH A 261 HOH A 394 HOH A 525
SITE 1 AC6 13 THR A 132 GLN A 133 ASP A 189 SER A 190
SITE 2 AC6 13 GLN A 192 SER A 195 SER A 202 GLY A 212
SITE 3 AC6 13 GLY A 214 GLY A 222 HOH A 320 HOH A 521
SITE 4 AC6 13 HOH A 524
CRYST1 54.473 58.310 66.586 90.00 90.00 90.00 P 21 21 21 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 0.018358 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015018 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
