HEADER SERINE PROTEASE 07-FEB-01 1H8I
TITLE X-RAY CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN WITH A
TITLE 2 TRIPEPTIDE PHOSPHONATE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: THROMBIN LIGHT CHAIN;
COMPND 5 SYNONYM: COAGULATION FACTOR II;
COMPND 6 EC: 3.4.21.5;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: THROMBIN;
COMPND 9 CHAIN: H;
COMPND 10 FRAGMENT: THROMBIN HEAVY CHAIN;
COMPND 11 SYNONYM: COAGULATION FACTOR II;
COMPND 12 EC: 3.4.21.5;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: HIRUDIN I;
COMPND 15 CHAIN: I;
COMPND 16 FRAGMENT: RESIDUES 55 TO 64;
COMPND 17 SYNONYM: LEPIRUDIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 6 ORGANISM_COMMON: HUMAN;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 9 ORGANISM_COMMON: MEDICINAL LEECH
KEYWDS SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SKORDALAKES,G.G.DODSON,D.GREEN,J.DEADMAN
REVDAT 2 16-AUG-01 1H8I 1 JRNL
REVDAT 1 02-MAR-01 1H8I 0
JRNL AUTH E.SKORDALAKES,G.G.DODSON,D.S.GREEN,C.A.GOODWIN,
JRNL AUTH 2 M.F.SCULLY,H.R.HUDSON,V.V.KAKKAR,J.J.DEADMAN
JRNL TITL INHIBITION OF HUMAN ALPHA-THROMBIN BY A
JRNL TITL 2 PHOSPHONATE TRIPEPTIDE PROCEEDS VIA A METASTABLE
JRNL TITL 3 PENTACOORDINATED PHOSPHORUS INTERMEDIATE.
JRNL REF J.MOL.BIOL. V. 311 549 2001
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.BERTRAND,J.OLEKSYSZYN,C.M.KAM,B.BODUSZEK,
REMARK 1 AUTH 2 S.PRESNELL,R.R.PLASKON,F.L.SUDDATH,J.C.POWERS,
REMARK 1 AUTH 3 L.D.WILLIAMS
REMARK 1 TITL INHIBITION OF TRYPSIN AND THROMBIN BY AMINO
REMARK 1 TITL 2 (4-AMIDINOPHENYL)METHANEPHOSPHONATE DIPHENYL ESTER
REMARK 1 TITL 3 DERIVATIVES: X-RAY AND MOLECULAR MODELS
REMARK 1 REF BIOCHEMISTRY V. 35 3147 1996
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 35239
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2352
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : NULL
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.010 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.200 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H8I COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI.
REMARK 100 THE EBI ID CODE IS EBI-5850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.20
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 : NULL
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35239
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.07500
REMARK 200 FOR THE DATA SET : 16.0000
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) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : 0.28000
REMARK 200 FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMEN
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1HGT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.19650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.65050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.19650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.65050
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 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: L, H, I, K, O, P, R, S
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH R 13 LIES ON A SPECIAL POSITION.
REMARK 375 HOH S 100 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH O 47 O HOH O 47 2655 0.86
REMARK 500 O HOH S 102 O HOH S 102 2656 2.04
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 LEU L 14G CB - CA - C ANGL. DEV. = 23.3 DEGREES
REMARK 500 LEU L 14G CA - CB - CG ANGL. DEV. = 24.0 DEGREES
REMARK 500 LEU H 41 CA - CB - CG ANGL. DEV. = 27.3 DEGREES
REMARK 500 THR H 74 N - CA - CB ANGL. DEV. =-16.6 DEGREES
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: PHW BINDING SITE FOR CHAIN K
DBREF 1H8I L 1B 14K UNP P00734 THRB_HUMAN 334 360
DBREF 1H8I H 16 148 UNP P00734 THRB_HUMAN 364 622
DBREF 1H8I I 1 10 UNP P01050 ITH1_HIRME 55 64
SEQADV 1H8I TYS I 9 UNP P01050 TYR 63 MODIFIED RESIDUE
SEQRES 1 L 27 ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER
SEQRES 2 L 27 LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR
SEQRES 3 L 27 ILE
SEQRES 1 H 253 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 H 253 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 H 253 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 H 253 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 H 253 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 H 253 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 H 253 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 H 253 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 H 253 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 H 253 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 H 253 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 H 253 LEU LYS GLU THR TRP GLY GLN PRO SER VAL LEU GLN VAL
SEQRES 13 H 253 VAL ASN LEU PRO ILE VAL GLU ARG PRO VAL CYS LYS ASP
SEQRES 14 H 253 SER THR ARG ILE ARG ILE THR ASP ASN MET PHE CYS ALA
SEQRES 15 H 253 GLY TYR LYS PRO ASP GLU GLY LYS ARG GLY ASP ALA CYS
SEQRES 16 H 253 GLU GLY ASP SER GLY GLY PRO PHE VAL MET LYS SER PRO
SEQRES 17 H 253 PHE ASN ASN ARG TRP TYR GLN MET GLY ILE VAL SER TRP
SEQRES 18 H 253 GLY GLU GLY CYS ASP ARG ASP GLY LYS TYR GLY PHE TYR
SEQRES 19 H 253 THR HIS VAL PHE ARG LEU LYS LYS TRP ILE GLN LYS VAL
SEQRES 20 H 253 ILE ASP GLN PHE GLY GLU
SEQRES 1 I 10 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU
MODRES 1H8I TYS I 9 TYR SULFONATED TYROSINE
HET TYS I 9 16
HET PHW K 1 44
HETNAM TYS SULFONATED TYROSINE
HETNAM PHW BETA-PHENYL-N-{[(PHENYLMETHYL)OXY]CARBONYL}-D-
HETNAM 2 PHW PHENYLALANYL-N- [(1S,3E)-1-[DIHYDROXY(METHYLOXY)
HETNAM 3 PHW (PHENYLOXY)-LAMBDA5-PHOSPHANYL]-4- (METHYLOXY)BUT-3-
HETNAM 4 PHW ENYL]-D-PROLINAMIDE
HETSYN PHW PHENYLMETHYL (1R)-2-[(2R)-2-({[(1S,3E)-1-
HETSYN 2 PHW [DIHYDROXY(METHYLOXY)(PHENYLOXY)- LAMBDA5-PHOSPHANYL]-
HETSYN 3 PHW 4-(METHYLOXY)BUT-3-ENYL]AMINO}CARBONYL)PYRROLIDIN-1-
HETSYN 4 PHW YL]- 1-(DIPHENYLMETHYL)-2-OXOETHYLCARBAMATE
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 PHW C40 H46 N3 O9 P
FORMUL 5 HOH *365(H2 O)
HELIX 1 8 PHE L 7 SER L 11 5 5
HELIX 2 9 THR L 14B TYR L 14J 1 9
HELIX 3 1 ALA H 55 CYS H 58 5 4
HELIX 4 2 PRO H 60B ASP H 60E 5 4
HELIX 5 3 THR H 60I ASN H 62 5 3
HELIX 6 4 ASP H 125 LEU H 130 1 9
HELIX 7 5 GLU H 164 SER H 171 1 8
HELIX 8 6 LYS H 185 GLY H 186C 5 5
HELIX 9 7 LEU H 234 GLY H 246 1 13
SHEET 1 HA 7 SER H 20 ASP H 21 0
SHEET 2 HA 7 GLN H 156 PRO H 161 -1 O VAL H 157 N SER H 20
SHEET 3 HA 7 LYS H 135 GLY H 140 -1 O GLY H 136 N LEU H 160
SHEET 4 HA 7 PRO H 198 LYS H 202 -1 O PRO H 198 N THR H 139
SHEET 5 HA 7 TRP H 207 TRP H 215 -1 O TYR H 208 N MET H 201
SHEET 6 HA 7 GLY H 226 HIS H 230 -1 O PHE H 227 N SER H 214
SHEET 7 HA 7 MET H 180 ALA H 183 -1 O PHE H 181 N TYR H 228
SHEET 1 HB 7 LYS H 81 SER H 83 0
SHEET 2 HB 7 LEU H 64 ILE H 68 -1 O VAL H 66 N SER H 83
SHEET 3 HB 7 GLN H 30 ARG H 35 -1 O MET H 32 N ARG H 67
SHEET 4 HB 7 GLU H 39 LEU H 46 -1 O GLU H 39 N ARG H 35
SHEET 5 HB 7 TRP H 51 THR H 54 -1 O LEU H 53 N SER H 45
SHEET 6 HB 7 ALA H 104 LEU H 108 -1 O ALA H 104 N THR H 54
SHEET 7 HB 7 LEU H 85 ILE H 90 -1 N GLU H 86 O LYS H 107
SHEET 1 HC 2 LEU H 60 TYR H 60A 0
SHEET 2 HC 2 LYS H 60F ASN H 60G 0
SSBOND 1 CYS H 42 CYS H 58
SSBOND 2 CYS H 122 CYS L 1
SSBOND 3 CYS H 168 CYS H 182
SSBOND 4 CYS H 191 CYS H 220
LINK C GLU I 8 N TYS I 9
LINK C TYS I 9 N LEU I 10
LINK P PHW K 1 OG SER H 195
CISPEP 1 SER H 36A PRO H 37 0 -0.57
SITE 1 AC1 19 HIS H 57 TRP H 60D TYR H 60A GLU H 97A
SITE 2 AC1 19 GLU H 146 ALA H 190 CYS H 191 GLU H 192
SITE 3 AC1 19 GLY H 193 ASP H 194 SER H 195 SER H 214
SITE 4 AC1 19 TRP H 215 GLY H 216 GLY H 219 HOH P 2
SITE 5 AC1 19 HOH P 3 HOH P 5 HOH S 189
CRYST1 70.393 71.301 72.416 90.00 100.87 90.00 C 1 2 1 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 0.014206 0.000000 0.002728 0.00000
SCALE2 0.000000 0.014025 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014061 0.00000