HEADER BLOOD CLOTTING 07-DEC-99 1C5G
TITLE PLASMINOGEN ACTIVATOR INHIBITOR-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR INHIBITOR-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PAI-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: LATENT FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPAIST-7HS
KEYWDS SERPIN, SERINE PROTEASE INHIBITOR, PLASMA, PLASMINOGEN ACTIVATION,
KEYWDS 2 GLYCOPROTEIN, POLYMORPHISM, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.GOLDSMITH
REVDAT 4 27-DEC-23 1C5G 1 REMARK
REVDAT 3 24-FEB-09 1C5G 1 VERSN
REVDAT 2 01-APR-03 1C5G 1 JRNL
REVDAT 1 17-DEC-99 1C5G 0
JRNL AUTH H.M.TUCKER,J.MOTTONEN,E.J.GOLDSMITH,R.D.GERARD
JRNL TITL ENGINEERING OF PLASMINOGEN ACTIVATOR INHIBITOR-1 TO REDUCE
JRNL TITL 2 THE RATE OF LATENCY TRANSITION.
JRNL REF NAT.STRUCT.BIOL. V. 2 442 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7664104
JRNL DOI 10.1038/NSB0695-442
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.MOTTENEN,A.STRAND,J.SYMERSKY,R.M.SWEET,D.E.DANLEY,
REMARK 1 AUTH 2 K.F.GEOGHEGAN,R.D.GERARD,E.J.GOLDSMITH
REMARK 1 TITL STRUCTURAL BASIS OF LATENCY IN PLASMINOGEN ACTIVATOR
REMARK 1 TITL 2 INHIBITOR-1
REMARK 1 REF NATURE V. 355 270 1992
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/355270A0
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.J.GOLDSMITH,C.SHENG-CHENG,D.E.DANLEY,R.D.GERARD,
REMARK 1 AUTH 2 K.F.GEOGHEGAN,J.MOTTENEN,A.STRAND
REMARK 1 TITL PRELIMINARY X-RAY ANALYSIS OF CRYSTALS OF PLASMINOGEN
REMARK 1 TITL 2 ACTIVATOR INHIBITOR-1
REMARK 1 REF PROTEINS V. 9 225 1991
REMARK 1 REFN ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 12239
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3013
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.38
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 : PAR19X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 PEPTIDE GEOMETRY TO GIVE RAMACHANDRAN ET AL BBA 359:298 (1974);
REMARK 3 PEPTIDE
REMARK 3 TORSIONS FROM HAGLER ET AL JACS 98:4600 (1976); NONBONDED TERMS
REMARK 3 JORGENSEN JACS
REMARK 3
REMARK 3 103:3976; W/ RC1-4 = 1.80 EC1-4 = 0.1
REMARK 4
REMARK 4 1C5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000001360.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS DETECTOR SYSTEM (NIELSEN)
REMARK 200 DATA SCALING SOFTWARE : FAST
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 X+1/2,Y+1/2,Z
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 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 78.79500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.92000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.79500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.92000
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 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 MET A 1
REMARK 465 GLN A 2
REMARK 465 MET A 3
REMARK 465 SER A 4
REMARK 465 PRO A 5
REMARK 465 ALA A 6
REMARK 465 LEU A 7
REMARK 465 THR A 8
REMARK 465 CYS A 9
REMARK 465 LEU A 10
REMARK 465 VAL A 11
REMARK 465 LEU A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 ALA A 15
REMARK 465 LEU A 16
REMARK 465 VAL A 17
REMARK 465 PHE A 18
REMARK 465 GLY A 19
REMARK 465 GLU A 20
REMARK 465 GLY A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
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 49 42.86 -83.10
REMARK 500 SER A 50 174.63 175.09
REMARK 500 LYS A 51 -81.49 -89.60
REMARK 500 ASP A 52 54.46 -118.25
REMARK 500 LYS A 111 -60.75 70.35
REMARK 500 ASN A 173 50.70 73.27
REMARK 500 PHE A 212 81.21 38.97
REMARK 500 HIS A 213 16.46 -68.79
REMARK 500 ASP A 216 82.53 -68.14
REMARK 500 SER A 218 -157.52 -160.70
REMARK 500 PRO A 239 -23.45 -38.78
REMARK 500 ARG A 291 89.06 -69.53
REMARK 500 MET A 318 78.10 -102.59
REMARK 500 SER A 367 112.76 59.68
REMARK 500 ALA A 368 -171.52 169.99
REMARK 500 PRO A 372 128.92 -25.86
REMARK 500 ASP A 378 159.25 179.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B3K RELATED DB: PDB
REMARK 900 PAI-1 ACTIVE FORM
DBREF 1C5G A 1 402 UNP P05121 PAI1_HUMAN 1 402
SEQRES 1 A 402 MET GLN MET SER PRO ALA LEU THR CYS LEU VAL LEU GLY
SEQRES 2 A 402 LEU ALA LEU VAL PHE GLY GLU GLY SER ALA VAL HIS HIS
SEQRES 3 A 402 PRO PRO SER TYR VAL ALA HIS LEU ALA SER ASP PHE GLY
SEQRES 4 A 402 VAL ARG VAL PHE GLN GLN VAL ALA GLN ALA SER LYS ASP
SEQRES 5 A 402 ARG ASN VAL VAL PHE SER PRO TYR GLY VAL ALA SER VAL
SEQRES 6 A 402 LEU ALA MET LEU GLN LEU THR THR GLY GLY GLU THR GLN
SEQRES 7 A 402 GLN GLN ILE GLN ALA ALA MET GLY PHE LYS ILE ASP ASP
SEQRES 8 A 402 LYS GLY MET ALA PRO ALA LEU ARG HIS LEU TYR LYS GLU
SEQRES 9 A 402 LEU MET GLY PRO TRP ASN LYS ASP GLU ILE SER THR THR
SEQRES 10 A 402 ASP ALA ILE PHE VAL GLN ARG ASP LEU LYS LEU VAL GLN
SEQRES 11 A 402 GLY PHE MET PRO HIS PHE PHE ARG LEU PHE ARG SER THR
SEQRES 12 A 402 VAL LYS GLN VAL ASP PHE SER GLU VAL GLU ARG ALA ARG
SEQRES 13 A 402 PHE ILE ILE ASN ASP TRP VAL LYS THR HIS THR LYS GLY
SEQRES 14 A 402 MET ILE SER ASN LEU LEU GLY LYS GLY ALA VAL ASP GLN
SEQRES 15 A 402 LEU THR ARG LEU VAL LEU VAL ASN ALA LEU TYR PHE ASN
SEQRES 16 A 402 GLY GLN TRP LYS THR PRO PHE PRO ASP SER SER THR HIS
SEQRES 17 A 402 ARG ARG LEU PHE HIS LYS SER ASP GLY SER THR VAL SER
SEQRES 18 A 402 VAL PRO MET MET ALA GLN THR ASN LYS PHE ASN TYR THR
SEQRES 19 A 402 GLU PHE THR THR PRO ASP GLY HIS TYR TYR ASP ILE LEU
SEQRES 20 A 402 GLU LEU PRO TYR HIS GLY ASP THR LEU SER MET PHE ILE
SEQRES 21 A 402 ALA ALA PRO TYR GLU LYS GLU VAL PRO LEU SER ALA LEU
SEQRES 22 A 402 THR ASN ILE LEU SER ALA GLN LEU ILE SER HIS TRP LYS
SEQRES 23 A 402 GLY ASN MET THR ARG LEU PRO ARG LEU LEU VAL LEU PRO
SEQRES 24 A 402 LYS PHE SER LEU GLU THR GLU VAL ASP LEU ARG LYS PRO
SEQRES 25 A 402 LEU GLU ASN LEU GLY MET THR ASP MET PHE ARG GLN PHE
SEQRES 26 A 402 GLN ALA ASP PHE THR SER LEU SER ASP GLN GLU PRO LEU
SEQRES 27 A 402 HIS VAL ALA GLN ALA LEU GLN LYS VAL LYS ILE GLU VAL
SEQRES 28 A 402 ASN GLU SER GLY THR VAL ALA SER SER SER THR ALA VAL
SEQRES 29 A 402 ILE VAL SER ALA ARG MET ALA PRO GLU GLU ILE ILE MET
SEQRES 30 A 402 ASP ARG PRO PHE LEU PHE VAL VAL ARG HIS ASN PRO THR
SEQRES 31 A 402 GLY THR VAL LEU PHE MET GLY GLN VAL MET GLU PRO
HELIX 1 1 HIS A 26 ALA A 49 1 24
HELIX 2 2 SER A 58 LEU A 69 1 12
HELIX 3 3 GLY A 74 GLY A 86 1 13
HELIX 4 4 GLY A 93 MET A 106 1 14
HELIX 5 5 GLY A 107 LYS A 111 5 5
HELIX 6 6 GLY A 131 ARG A 141 1 11
HELIX 7 7 GLU A 151 THR A 167 1 17
HELIX 8 8 GLY A 176 VAL A 180 5 5
HELIX 9 9 LEU A 270 ASN A 275 1 6
HELIX 10 10 SER A 278 GLY A 287 1 10
HELIX 11 11 LEU A 309 GLY A 317 1 9
HELIX 12 12 THR A 319 ARG A 323 5 5
SHEET 1 A 3 THR A 290 PRO A 299 0
SHEET 2 A 3 SER A 221 THR A 238 -1 O MET A 225 N LEU A 298
SHEET 3 A 3 HIS A 208 LEU A 211 -1 O HIS A 208 N MET A 224
SHEET 1 A1 7 THR A 290 PRO A 299 0
SHEET 2 A1 7 SER A 221 THR A 238 -1 O MET A 225 N LEU A 298
SHEET 3 A1 7 HIS A 242 PRO A 250 -1 O HIS A 242 N THR A 238
SHEET 4 A1 7 LEU A 256 PRO A 263 -1 O MET A 258 N LEU A 249
SHEET 5 A1 7 PRO A 380 HIS A 387 -1 N LEU A 382 O ALA A 261
SHEET 6 A1 7 THR A 392 MET A 400 -1 O THR A 392 N HIS A 387
SHEET 7 A1 7 VAL A 56 PHE A 57 -1 N PHE A 57 O MET A 396
SHEET 1 B 6 LYS A 145 VAL A 147 0
SHEET 2 B 6 GLU A 113 GLN A 123 1 O ILE A 120 N LYS A 145
SHEET 3 B 6 LEU A 186 GLN A 197 -1 O VAL A 187 N PHE A 121
SHEET 4 B 6 GLY A 355 VAL A 366 -1 N THR A 356 O GLY A 196
SHEET 5 B 6 VAL A 340 VAL A 351 -1 N ALA A 341 O ILE A 365
SHEET 6 B 6 PHE A 301 ASP A 308 -1 O PHE A 301 N VAL A 351
CRYST1 157.590 47.840 62.880 90.00 107.78 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 0.006346 0.000000 0.002035 0.00000
SCALE2 0.000000 0.020903 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016701 0.00000
(ATOM LINES ARE NOT SHOWN.)
END