HEADER HYDROLASE 17-MAY-16 5K0H
TITLE HUMAN FACTOR XA IN COMPLEX WITH SYNTHETIC INHIBITOR BENZYLSULFONYL-
TITLE 2 DSER(BENZYL)-GLY-4-AMIDINOBENZYLAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR X;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: STUART FACTOR,STUART-PROWER FACTOR;
COMPND 5 EC: 3.4.21.6;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: COAGULATION FACTOR X;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: STUART FACTOR,STUART-PROWER FACTOR;
COMPND 10 EC: 3.4.21.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS HUMAN FACTOR XA, INHIBITOR COMPLEX, BENZAMIDINE INHIBITOR, HYDROLASE,
KEYWDS 2 CLOTTING FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.STEINMETZER
REVDAT 2 10-JAN-24 5K0H 1 REMARK
REVDAT 1 06-JUL-16 5K0H 0
JRNL AUTH A.SCHWEINITZ,A.STURZEBECHER,U.STURZEBECHER,O.SCHUSTER,
JRNL AUTH 2 J.STURZEBECHER,T.STEINMETZER
JRNL TITL NEW SUBSTRATE ANALOGUE INHIBITORS OF FACTOR XA CONTAINING
JRNL TITL 2 4-AMIDINOBENZYLAMIDE AS P1 RESIDUE: PART 1.
JRNL REF MEDICINAL CHEMISTRY V. 2 349 2006
JRNL REFN ISSN 1573-4064
JRNL PMID 16848746
JRNL DOI 10.2174/157340606777724040
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,MOLECULAR
REMARK 3 : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1177536.280
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 16160
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1631
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2356
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 263
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2229
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.87000
REMARK 3 B22 (A**2) : -15.71000
REMARK 3 B33 (A**2) : 23.58000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.32
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 1.600 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.200 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 41.51
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 : MSI_CNX_TOPPAR/PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : MSI_CNX_TOPPAR/WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : MSI_CNX_TOPPAR/ION.PARAM
REMARK 3 PARAMETER FILE 4 : ../../../INH/CU1/INH.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : MSI_CNX_TOPPAR/PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : MSI_CNX_TOPPAR/WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : MSI_CNX_TOPPAR/ION.TOP
REMARK 3 TOPOLOGY FILE 4 : ../../../INH/CU1/INH.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 5K0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2-5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16187
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1EQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 12-18 % PEG6000, 5 MM
REMARK 280 CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 28.14000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.56500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.56500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.14000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.20000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ALA A 61A 148.31 -170.91
REMARK 500 LYS A 62 -83.26 -60.93
REMARK 500 ARG A 115 -170.90 -176.07
REMARK 500 GLN B 10 -113.61 -131.02
REMARK 500 GLU B 14 70.87 -102.22
REMARK 500 LYS B 34 -52.57 -125.91
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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 70 OD1
REMARK 620 2 ASN A 72 O 77.7
REMARK 620 3 GLN A 75 O 142.1 88.6
REMARK 620 4 GLU A 80 OE2 99.8 165.4 84.8
REMARK 620 5 HOH A 410 O 76.0 83.9 67.4 81.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 185 O
REMARK 620 2 ASP A 185A O 89.8
REMARK 620 3 ARG A 222 O 161.2 82.8
REMARK 620 4 LYS A 224 O 88.1 106.1 77.5
REMARK 620 5 HOH A 460 O 93.3 165.5 89.9 60.0
REMARK 620 N 1 2 3 4
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6PK A 303
DBREF 5K0H A 16 244 UNP P00742 FA10_HUMAN 235 468
DBREF 5K0H B 0 50 UNP P00742 FA10_HUMAN 128 178
SEQRES 1 A 234 ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO
SEQRES 2 A 234 TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE
SEQRES 3 A 234 CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR
SEQRES 4 A 234 ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL
SEQRES 5 A 234 ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY
SEQRES 6 A 234 GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN
SEQRES 7 A 234 ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL
SEQRES 8 A 234 LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL
SEQRES 9 A 234 ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER
SEQRES 10 A 234 THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE
SEQRES 11 A 234 GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU
SEQRES 12 A 234 LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS
SEQRES 13 A 234 LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE
SEQRES 14 A 234 CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN
SEQRES 15 A 234 GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP
SEQRES 16 A 234 THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY
SEQRES 17 A 234 CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL
SEQRES 18 A 234 THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR
SEQRES 1 B 51 LEU CYS SER LEU ASP ASN GLY ASP CYS ASP GLN PHE CYS
SEQRES 2 B 51 HIS GLU GLU GLN ASN SER VAL VAL CYS SER CYS ALA ARG
SEQRES 3 B 51 GLY TYR THR LEU ALA ASP ASN GLY LYS ALA CYS ILE PRO
SEQRES 4 B 51 THR GLY PRO TYR PRO CYS GLY LYS GLN THR LEU GLU
HET CA A 301 1
HET CA A 302 1
HET 6PK A 303 38
HETNAM CA CALCIUM ION
HETNAM 6PK O-BENZYL-N-(BENZYLSULFONYL)-D-SERYL-N-[(4-
HETNAM 2 6PK CARBAMIMIDOYLPHENYL)METHYL]GLYCINAMIDE
FORMUL 3 CA 2(CA 2+)
FORMUL 5 6PK C27 H31 N5 O5 S
FORMUL 6 HOH *143(H2 O)
HELIX 1 AA1 ALA A 55 LEU A 59 5 5
HELIX 2 AA2 GLU A 124 LEU A 131A 1 9
HELIX 3 AA3 ASP A 164 SER A 172 1 9
HELIX 4 AA4 PHE A 234 THR A 244 1 11
HELIX 5 AA5 LEU B 3 CYS B 8 5 6
SHEET 1 AA1 7 GLN A 20 GLU A 21 0
SHEET 2 AA1 7 LYS A 156 PRO A 161 -1 O MET A 157 N GLN A 20
SHEET 3 AA1 7 THR A 135 GLY A 140 -1 N VAL A 138 O LEU A 158
SHEET 4 AA1 7 PRO A 198 PHE A 203 -1 O VAL A 200 N ILE A 137
SHEET 5 AA1 7 THR A 206 TRP A 215 -1 O THR A 210 N HIS A 199
SHEET 6 AA1 7 GLY A 226 LYS A 230 -1 O ILE A 227 N TRP A 215
SHEET 7 AA1 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 AA2 7 ALA A 81 HIS A 83 0
SHEET 2 AA2 7 LYS A 65 VAL A 68 -1 N VAL A 66 O HIS A 83
SHEET 3 AA2 7 GLN A 30 ILE A 34 -1 N LEU A 32 O ARG A 67
SHEET 4 AA2 7 GLY A 40 ILE A 46 -1 O CYS A 42 N LEU A 33
SHEET 5 AA2 7 TYR A 51 THR A 54 -1 O LEU A 53 N THR A 45
SHEET 6 AA2 7 ALA A 104 LEU A 108 -1 O LEU A 106 N ILE A 52
SHEET 7 AA2 7 VAL A 85 LYS A 90 -1 N VAL A 87 O ARG A 107
SHEET 1 AA3 2 PHE B 11 GLU B 15 0
SHEET 2 AA3 2 SER B 18 SER B 22 -1 O SER B 22 N PHE B 11
SHEET 1 AA4 2 TYR B 27 LEU B 29 0
SHEET 2 AA4 2 CYS B 36 PRO B 38 -1 O ILE B 37 N THR B 28
SSBOND 1 CYS A 22 CYS A 27 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 122 CYS B 44 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.02
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.03
SSBOND 6 CYS B 1 CYS B 12 1555 1555 2.03
SSBOND 7 CYS B 8 CYS B 21 1555 1555 2.02
SSBOND 8 CYS B 23 CYS B 36 1555 1555 2.04
LINK OD1 ASP A 70 CA CA A 301 1555 1555 2.47
LINK O ASN A 72 CA CA A 301 1555 1555 2.24
LINK O GLN A 75 CA CA A 301 1555 1555 2.43
LINK OE2 GLU A 80 CA CA A 301 1555 1555 2.17
LINK O TYR A 185 CA CA A 302 1555 1555 2.12
LINK O ASP A 185A CA CA A 302 1555 1555 2.82
LINK O ARG A 222 CA CA A 302 1555 1555 2.69
LINK O LYS A 224 CA CA A 302 1555 1555 2.53
LINK CA CA A 301 O HOH A 410 1555 1555 2.19
LINK CA CA A 302 O HOH A 460 1555 1555 3.15
SITE 1 AC1 5 ASP A 70 ASN A 72 GLN A 75 GLU A 80
SITE 2 AC1 5 HOH A 410
SITE 1 AC2 4 TYR A 185 ASP A 185A ARG A 222 LYS A 224
SITE 1 AC3 19 HIS A 57 GLU A 97 THR A 98 TYR A 99
SITE 2 AC3 19 ARG A 143 GLU A 147 PHE A 174 ASP A 189
SITE 3 AC3 19 ALA A 190 CYS A 191 SER A 195 VAL A 213
SITE 4 AC3 19 SER A 214 TRP A 215 GLY A 216 GLY A 219
SITE 5 AC3 19 CYS A 220 GLY A 226 HOH A 462
CRYST1 56.280 72.400 77.130 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 0.017768 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012965 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
