HEADER HYDROLASE 06-MAR-03 1O31
TITLE ELABORATE MANIFOLD OF SHORT HYDROGEN BOND ARRAYS MEDIATING BINDING OF
TITLE 2 ACTIVE SITE-DIRECTED SERINE PROTEASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 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;
SOURCE 5 ORGAN: PANCREAS
KEYWDS SERINE PROTEASE, SHORT HYDROGEN BOND, INHIBITION MECHANISM, SHIFT OF
KEYWDS 2 PKA, TRYPSIN, THROMBIN, UROKINASE, FACTOR XA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.KATZ,K.ELROD,E.VERNER,R.L.MACKMAN,C.LUONG,W.D.SHRADER,M.SENDZIK,
AUTHOR 2 J.R.SPENCER,P.A.SPRENGELER,A.KOLESNIKOV,V.W.TAI,H.C.HUI,
AUTHOR 3 J.G.BREITENBUCHER,D.ALLEN,J.W.JANC
REVDAT 4 27-DEC-23 1O31 1 REMARK LINK
REVDAT 3 04-OCT-17 1O31 1 REMARK
REVDAT 2 24-FEB-09 1O31 1 VERSN
REVDAT 1 02-SEP-03 1O31 0
JRNL AUTH B.A.KATZ,K.ELROD,E.VERNER,R.L.MACKMAN,C.LUONG,W.D.SHRADER,
JRNL AUTH 2 M.SENDZIK,J.R.SPENCER,P.A.SPRENGELER,A.KOLESNIKOV,V.W.TAI,
JRNL AUTH 3 H.C.HUI,J.G.BREITENBUCHER,D.ALLEN,J.W.JANC
JRNL TITL ELABORATE MANIFOLD OF SHORT HYDROGEN BOND ARRAYS MEDIATING
JRNL TITL 2 BINDING OF ACTIVE SITE-DIRECTED SERINE PROTEASE INHIBITORS.
JRNL REF J.MOL.BIOL. V. 329 93 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12742021
JRNL DOI 10.1016/S0022-2836(03)00399-1
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.3
REMARK 3 NUMBER OF REFLECTIONS : 23216
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2326
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
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 : 20
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 3.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES SIMULTANEOUSLY REFINED IN TWO OR MORE CONFORMATIONS ARE:
REMARK 3 VAL53, LEU66, SER86, LYS87, SER110, SE113, SER130, LYS159, ASP165,
REMARK 3 SER166
REMARK 3 SER170, SER217, LYS230, SER236, SER244, 801246 (INHIBITOR)
REMARK 3
REMARK 3 HOH383 MAKES SHORT H-BONDS WITH OGSER195 (CONFORMATION 1)
REMARK 3 AND O6' (CONFORMATION 1)OF THE INHIBITOR
REMARK 3
REMARK 3 OGSER195 (CONFORMATION 1) MAKES A NORMAL H-BOND WITH
REMARK 3 O6' (CONFORMATION 1) OF THE INHIBITOR
REMARK 3
REMARK 3 CONFORMATION 2 OF THE INHIBITOR IS ROTATED ~ 180 DEG ABOUT
REMARK 3 THE BENZIMIDAZOLE-PHENOL BOND AND DISENGAGED FROM THE ACTIVE SITE
REMARK 3
REMARK 3 HIS40 AND HIS91 ARE MONOPROTONATED ON THE EPSILON NITROGEN.
REMARK 3 HIS57 IS DOUBLY PROTONATED.
REMARK 4
REMARK 4 1O31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000001741.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.10
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX 1.2
REMARK 200 DATA SCALING SOFTWARE : BIOTEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24334
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 46.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 72.4
REMARK 200 DATA REDUNDANCY : 1.890
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: QUANTA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE SOAK AT TARGET PH
REMARK 280 (10.05). VAPOR DIFFUSION AT 298 K, PH 8.10
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 31.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.05500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.05500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.97000
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 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 236 H2 HOH A 292 1.48
REMARK 500 OG SER A 166 H2 HOH A 378 1.51
REMARK 500 OG SER A 116 H1 HOH A 539 1.51
REMARK 500 O GLN A 221A H2 HOH A 650 1.54
REMARK 500 OG1 THR A 134 H2 HOH A 480 1.55
REMARK 500 OH TYR A 20 H1 HOH A 348 1.56
REMARK 500 O GLY A 203 H1 HOH A 351 1.57
REMARK 500 OH TYR A 228 H1 HOH A 281 1.59
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 40 NE2 HIS A 40 CD2 -0.077
REMARK 500 HIS A 91 NE2 HIS A 91 CD2 -0.075
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 189 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 VAL A 199 N - CA - C ANGL. DEV. = -19.0 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 ASN A 25 29.96 47.01
REMARK 500 ASP A 71 -68.30 -139.52
REMARK 500 ASN A 79 -5.32 84.02
REMARK 500 ASN A 115 -158.82 -159.14
REMARK 500 ASN A 223 12.58 58.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 65A 0.10 SIDE CHAIN
REMARK 500 ARG A 117 0.26 SIDE CHAIN
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 247 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE2
REMARK 620 2 ASN A 72 O 84.6
REMARK 620 3 VAL A 75 O 160.7 94.3
REMARK 620 4 GLU A 80 OE2 95.5 167.5 89.6
REMARK 620 5 HOH A 248 O 83.5 101.5 77.9 90.9
REMARK 620 6 HOH A 560 O 88.9 91.2 110.4 76.3 164.4
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 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 801 A 246
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C5R RELATED DB: PDB
REMARK 900 BOVINE TRYPSIN COMPLEX WITH DIFFERENT INHIBITOR
DBREF 1O31 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 247 1
HET 801 A 246 60
HETNAM CA CALCIUM ION
HETNAM 801 2-{5-[AMINO(IMINIO)METHYL]-1H-BENZIMIDAZOL-2-
HETNAM 2 801 YL}PYRIDIN-3-OLATE
HETSYN 801 CRA_1801
FORMUL 2 CA CA 2+
FORMUL 3 801 C13 H11 N5 O
FORMUL 4 HOH *127(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 SER A 244 1 11
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 GLN A 210 N VAL A 199
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 66 -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 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.01
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.02
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.01
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.00
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.01
LINK OE2 GLU A 70 CA CA A 247 1555 1555 2.47
LINK O ASN A 72 CA CA A 247 1555 1555 2.25
LINK O VAL A 75 CA CA A 247 1555 1555 2.20
LINK OE2 GLU A 80 CA CA A 247 1555 1555 2.60
LINK CA CA A 247 O HOH A 248 1555 1555 2.42
LINK CA CA A 247 O HOH A 560 1555 1555 2.43
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A 248 HOH A 560
SITE 1 AC2 13 HIS A 57 ASP A 189 SER A 190 CYS A 191
SITE 2 AC2 13 GLN A 192 SER A 195 VAL A 213 TRP A 215
SITE 3 AC2 13 GLY A 216 GLY A 219 GLY A 226 HOH A 282
SITE 4 AC2 13 HOH A 383
CRYST1 63.900 61.940 70.110 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 0.015649 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016145 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014263 0.00000
(ATOM LINES ARE NOT SHOWN.)
END