HEADER HYDROLASE 04-AUG-08 3E1X
TITLE THE CRYSTAL STRUCTURE OF APO PROSTASIN AT 1.7 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTASIN;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: UNP RESIDUES 45-305;
COMPND 5 SYNONYM: SERINE PROTEASE 8, PROSTASIN LIGHT CHAIN, PROSTASIN HEAVY
COMPND 6 CHAIN;
COMPND 7 EC: 3.4.21.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PRSS8;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROSTASIN, ENAC, HCAP-1, CHANNEL ACTIVATING PROTEASE, CELL MEMBRANE,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, MEMBRANE, PROTEASE, SECRETED, SERINE
KEYWDS 3 PROTEASE, TRANSMEMBRANE, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SPRAGGON,M.HORNSBY,A.SHIPWAY,J.L.HARRIS,S.A.LESLEY
REVDAT 4 30-AUG-23 3E1X 1 REMARK
REVDAT 3 20-OCT-21 3E1X 1 REMARK SEQADV
REVDAT 2 13-JUL-11 3E1X 1 VERSN
REVDAT 1 05-MAY-09 3E1X 0
JRNL AUTH G.SPRAGGON,M.HORNSBY,A.SHIPWAY,D.C.TULLY,B.BURSULAYA,
JRNL AUTH 2 H.DANAHAY,J.L.HARRIS,S.A.LESLEY
JRNL TITL ACTIVE SITE CONFORMATIONAL CHANGES OF PROSTASIN PROVIDE A
JRNL TITL 2 NEW MECHANISM OF PROTEASE REGULATION BY DIVALENT CATIONS.
JRNL REF PROTEIN SCI. V. 18 1081 2009
JRNL REFN ISSN 0961-8368
JRNL PMID 19388054
JRNL DOI 10.1002/PRO.118
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 24014
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1206
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 1.7000 - 1.7000 0.00 0 86 0.2836 0.3605
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.50380
REMARK 3 B22 (A**2) : 3.02870
REMARK 3 B33 (A**2) : -4.87310
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3E1X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048771.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-06
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26345
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.62700
REMARK 200 R SYM FOR SHELL (I) : 0.62700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.080
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1EON
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG-6000 IN 0.1M MES BUFFER, PH
REMARK 280 6.0, VAPOR DIFFUSION, SITTING DROP, 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 26.77800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.33900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.03550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.33900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.77800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.03550
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL B 249
REMARK 465 VAL B 250
REMARK 465 PRO B 251
REMARK 465 GLN B 252
REMARK 465 THR B 253
REMARK 465 GLN B 254
REMARK 465 GLU B 255
REMARK 465 SER B 256
REMARK 465 GLN B 257
REMARK 465 PRO B 258
REMARK 465 ASP B 259
REMARK 465 SER B 260
REMARK 465 ASN B 261
REMARK 465 LEU B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG B 248 CG CD NE CZ NH1 NH2
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 OE1 GLU B 159 O HOH B 448 4455 2.03
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 HIS B 71 -60.66 -106.95
REMARK 500 GLN B 96 168.10 179.72
REMARK 500 SER B 144C 26.52 48.71
REMARK 500 LYS B 153 60.83 65.74
REMARK 500 GLU B 172H 78.59 -104.70
REMARK 500 GLN B 246 70.25 -155.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EON RELATED DB: PDB
REMARK 900 PROSTASIN IN COMPLEX WITH DFFR-CMK
REMARK 900 RELATED ID: 1EOP RELATED DB: PDB
REMARK 900 RELATED ID: 3E16 RELATED DB: PDB
DBREF 3E1X B 16 262 UNP Q16651 PRSS8_HUMAN 45 305
SEQADV 3E1X SER B 122 UNP Q16651 CYS 154 ENGINEERED MUTATION
SEQADV 3E1X GLN B 127 UNP Q16651 ASN 159 ENGINEERED MUTATION
SEQADV 3E1X SER B 170 UNP Q16651 CYS 203 ENGINEERED MUTATION
SEQADV 3E1X HIS B 263 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 264 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 265 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 266 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 267 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 268 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 269 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 270 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 271 UNP Q16651 EXPRESSION TAG
SEQADV 3E1X HIS B 272 UNP Q16651 EXPRESSION TAG
SEQRES 1 B 271 ILE THR GLY GLY SER SER ALA VAL ALA GLY GLN TRP PRO
SEQRES 2 B 271 TRP GLN VAL SER ILE THR TYR GLU GLY VAL HIS VAL CYS
SEQRES 3 B 271 GLY GLY SER LEU VAL SER GLU GLN TRP VAL LEU SER ALA
SEQRES 4 B 271 ALA HIS CYS PHE PRO SER GLU HIS HIS LYS GLU ALA TYR
SEQRES 5 B 271 GLU VAL LYS LEU GLY ALA HIS GLN LEU ASP SER TYR SER
SEQRES 6 B 271 GLU ASP ALA LYS VAL SER THR LEU LYS ASP ILE ILE PRO
SEQRES 7 B 271 HIS PRO SER TYR LEU GLN GLU GLY SER GLN GLY ASP ILE
SEQRES 8 B 271 ALA LEU LEU GLN LEU SER ARG PRO ILE THR PHE SER ARG
SEQRES 9 B 271 TYR ILE ARG PRO ILE SER LEU PRO ALA ALA GLN ALA SER
SEQRES 10 B 271 PHE PRO ASN GLY LEU HIS CYS THR VAL THR GLY TRP GLY
SEQRES 11 B 271 HIS VAL ALA PRO SER VAL SER LEU LEU THR PRO LYS PRO
SEQRES 12 B 271 LEU GLN GLN LEU GLU VAL PRO LEU ILE SER ARG GLU THR
SEQRES 13 B 271 CYS ASN SER LEU TYR ASN ILE ASP ALA LYS PRO GLU GLU
SEQRES 14 B 271 PRO HIS PHE VAL GLN GLU ASP MET VAL CYS ALA GLY TYR
SEQRES 15 B 271 VAL GLU GLY GLY LYS ASP ALA CYS GLN GLY ASP SER GLY
SEQRES 16 B 271 GLY PRO LEU SER CYS PRO VAL GLU GLY LEU TRP TYR LEU
SEQRES 17 B 271 THR GLY ILE VAL SER TRP GLY ASP ALA CYS GLY ALA ARG
SEQRES 18 B 271 ASN ARG PRO GLY VAL TYR THR LEU ALA SER SER TYR ALA
SEQRES 19 B 271 SER TRP ILE GLN SER LYS VAL THR GLU LEU GLN PRO ARG
SEQRES 20 B 271 VAL VAL PRO GLN THR GLN GLU SER GLN PRO ASP SER ASN
SEQRES 21 B 271 LEU HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET GOL B 1 6
HET GOL B 2 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 HOH *199(H2 O)
HELIX 1 1 ALA B 55 PHE B 58A 5 5
HELIX 2 2 HIS B 58F GLU B 58H 5 3
HELIX 3 3 SER B 164 ASN B 172A 1 10
HELIX 4 4 TYR B 234 GLN B 246 1 13
SHEET 1 A 8 SER B 20 SER B 21 0
SHEET 2 A 8 GLN B 156 ILE B 163 -1 O GLN B 157 N SER B 20
SHEET 3 A 8 MET B 180 ALA B 183 -1 O CYS B 182 N ILE B 163
SHEET 4 A 8 GLY B 226 LEU B 230 -1 O TYR B 228 N VAL B 181
SHEET 5 A 8 LEU B 206 TRP B 215 -1 N SER B 214 O VAL B 227
SHEET 6 A 8 PRO B 198 VAL B 203 -1 N CYS B 201 O TYR B 208
SHEET 7 A 8 HIS B 135 GLY B 140 -1 N THR B 137 O SER B 200
SHEET 8 A 8 GLN B 156 ILE B 163 -1 O VAL B 160 N CYS B 136
SHEET 1 B 7 LYS B 81 SER B 83 0
SHEET 2 B 7 TYR B 64 LEU B 68 -1 N LEU B 68 O LYS B 81
SHEET 3 B 7 GLN B 30 TYR B 35 -1 N THR B 34 O GLU B 65
SHEET 4 B 7 VAL B 39 LEU B 46 -1 O CYS B 42 N ILE B 33
SHEET 5 B 7 TRP B 51 SER B 54 -1 O LEU B 53 N SER B 45
SHEET 6 B 7 ALA B 104 LEU B 108 -1 O LEU B 106 N VAL B 52
SHEET 7 B 7 LEU B 85 PRO B 90 -1 N ILE B 89 O LEU B 105
SSBOND 1 CYS B 42 CYS B 58 1555 1555 2.06
SSBOND 2 CYS B 136 CYS B 201 1555 1555 2.05
SSBOND 3 CYS B 168 CYS B 182 1555 1555 2.05
SSBOND 4 CYS B 191 CYS B 219 1555 1555 2.04
CISPEP 1 THR B 144H PRO B 144I 0 7.41
SITE 1 AC1 7 GLN B 26 TRP B 27 TRP B 29 TRP B 207
SITE 2 AC1 7 SER B 236 GLN B 239 HOH B 455
SITE 1 AC2 5 PRO B 120 SER B 122 LEU B 206 TRP B 207
SITE 2 AC2 5 HOH B 324
CRYST1 53.556 54.071 82.678 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 0.018672 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018494 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012095 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
