HEADER SERINE PROTEASE 01-OCT-98 4PRO
TITLE ALPHA-LYTIC PROTEASE COMPLEXED WITH PRO REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-LYTIC PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CHAIN A, B, MATURE PROTEASE. CHAIN C, D, PRO REGION;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ALPHA-LYTIC PROTEASE;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: CHAIN A, B, MATURE PROTEASE. CHAIN C, D, PRO REGION;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 FRAGMENT: CHAIN C, D;
SOURCE 3 ORGANISM_SCIENTIFIC: LYSOBACTER ENZYMOGENES;
SOURCE 4 ORGANISM_TAXID: 69;
SOURCE 5 GENE: T7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INCLUSION BODIES;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 EXPRESSION SYSTEM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7PRO;
SOURCE 11 EXPRESSION_SYSTEM_GENE: T7;
SOURCE 12 MOL_ID: 2;
SOURCE 13 FRAGMENT: CHAIN C, D;
SOURCE 14 ORGANISM_SCIENTIFIC: LYSOBACTER ENZYMOGENES;
SOURCE 15 ORGANISM_TAXID: 69;
SOURCE 16 GENE: T7;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INCLUSION BODIES;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 EXPRESSION SYSTEM;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PT7PRO;
SOURCE 22 EXPRESSION_SYSTEM_GENE: T7
KEYWDS PRO REGION, FOLDASE, PROTEIN FOLDING, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.K.SAUTER,T.MAU,S.D.RADER,D.A.AGARD
REVDAT 5 09-AUG-23 4PRO 1 REMARK
REVDAT 4 22-JAN-20 4PRO 1 REMARK
REVDAT 3 13-JUL-11 4PRO 1 VERSN
REVDAT 2 24-FEB-09 4PRO 1 VERSN
REVDAT 1 18-MAY-99 4PRO 0
JRNL AUTH N.K.SAUTER,T.MAU,S.D.RADER,D.A.AGARD
JRNL TITL STRUCTURE OF ALPHA-LYTIC PROTEASE COMPLEXED WITH ITS PRO
JRNL TITL 2 REGION.
JRNL REF NAT.STRUCT.BIOL. V. 5 945 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9808037
JRNL DOI 10.1038/2919
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.854
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 31292
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 SET) : 0.191
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3090
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 : 5017
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 69
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) : -1.70600
REMARK 3 B22 (A**2) : -2.00100
REMARK 3 B33 (A**2) : 3.70700
REMARK 3 B12 (A**2) : -0.21600
REMARK 3 B13 (A**2) : -0.95900
REMARK 3 B23 (A**2) : 2.13900
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-95
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.5
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 RUH2R
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104427
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 28.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.37100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 3PRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 ALA C 1
REMARK 465 ASP C 2
REMARK 465 GLN C 3
REMARK 465 VAL C 4
REMARK 465 ASP C 5
REMARK 465 ARG C 105
REMARK 465 VAL C 106
REMARK 465 LYS C 107
REMARK 465 GLY C 108
REMARK 465 VAL C 109
REMARK 465 SER C 110
REMARK 465 LYS C 111
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 GLN D 3
REMARK 465 VAL D 4
REMARK 465 VAL D 106
REMARK 465 LYS D 107
REMARK 465 GLY D 108
REMARK 465 VAL D 109
REMARK 465 SER D 110
REMARK 465 LYS D 111
REMARK 465 PRO D 112
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 PHE A 85 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 165 OG
REMARK 470 GLN A 185 CG CD OE1 NE2
REMARK 470 GLN C 7 CG CD OE1 NE2
REMARK 470 GLN C 47 CG CD OE1 NE2
REMARK 470 ARG C 71 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 72 CG CD CE NZ
REMARK 470 LEU C 76 CG CD1 CD2
REMARK 470 LYS C 89 CG CD CE NZ
REMARK 470 ASN C 103 CG OD1 ND2
REMARK 470 ASP C 114 CG OD1 OD2
REMARK 470 LEU C 146 CG CD1 CD2
REMARK 470 LYS C 162 CG CD CE NZ
REMARK 470 SER B 165 OG
REMARK 470 GLN B 185 CG CD OE1 NE2
REMARK 470 LEU D 16 CG CD1 CD2
REMARK 470 GLN D 47 CG CD OE1 NE2
REMARK 470 THR D 67 OG1 CG2
REMARK 470 ARG D 71 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 72 CG CD CE NZ
REMARK 470 LEU D 76 CG CD1 CD2
REMARK 470 LYS D 89 CG CD CE NZ
REMARK 470 ASN D 103 CG OD1 ND2
REMARK 470 ARG D 105 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 146 CG CD1 CD2
REMARK 470 SER D 147 OG
REMARK 470 GLU D 157 CG CD OE1 OE2
REMARK 470 LYS D 162 CG CD CE NZ
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 13 23.68 44.31
REMARK 500 ASN A 41 -15.71 75.40
REMARK 500 PHE A 59 128.11 179.22
REMARK 500 PRO A 60 -157.32 -78.15
REMARK 500 ALA C 70 -71.93 -79.35
REMARK 500 ARG C 71 -71.63 55.07
REMARK 500 LYS C 72 -34.20 69.58
REMARK 500 ARG C 85 -71.72 -60.83
REMARK 500 ASN C 103 9.34 -64.60
REMARK 500 LEU C 113 54.87 -115.43
REMARK 500 ASN C 126 54.92 39.71
REMARK 500 ASP C 150 103.87 -54.93
REMARK 500 SER C 151 -8.96 -58.50
REMARK 500 ASN B 13 11.13 59.06
REMARK 500 THR B 33 -173.87 -170.57
REMARK 500 ASN B 41 -5.98 84.94
REMARK 500 PHE B 59 128.35 -176.80
REMARK 500 PRO B 60 -155.95 -77.50
REMARK 500 ASP B 63 74.49 -153.01
REMARK 500 SER B 71 -0.74 -58.53
REMARK 500 SER B 159 -60.44 -103.17
REMARK 500 ARG D 71 130.85 -36.64
REMARK 500 ARG D 85 -74.07 -60.09
REMARK 500 ASN D 103 6.20 -65.08
REMARK 500 ALA D 104 -87.90 -110.01
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 TYR C 26 0.08 SIDE CHAIN
REMARK 500 TYR D 26 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4PRO A 1 198 UNP P00778 PRLA_LYSEN 200 397
DBREF 4PRO C 1 166 UNP P00778 PRLA_LYSEN 34 199
DBREF 4PRO B 1 198 UNP P00778 PRLA_LYSEN 200 397
DBREF 4PRO D 1 166 UNP P00778 PRLA_LYSEN 34 199
SEQADV 4PRO ALA A 158 UNP P00778 MET 357 SEE REMARK 999
SEQADV 4PRO ALA B 158 UNP P00778 MET 357 SEE REMARK 999
SEQRES 1 A 198 ALA ASN ILE VAL GLY GLY ILE GLU TYR SER ILE ASN ASN
SEQRES 2 A 198 ALA SER LEU CYS SER VAL GLY PHE SER VAL THR ARG GLY
SEQRES 3 A 198 ALA THR LYS GLY PHE VAL THR ALA GLY HIS CYS GLY THR
SEQRES 4 A 198 VAL ASN ALA THR ALA ARG ILE GLY GLY ALA VAL VAL GLY
SEQRES 5 A 198 THR PHE ALA ALA ARG VAL PHE PRO GLY ASN ASP ARG ALA
SEQRES 6 A 198 TRP VAL SER LEU THR SER ALA GLN THR LEU LEU PRO ARG
SEQRES 7 A 198 VAL ALA ASN GLY SER SER PHE VAL THR VAL ARG GLY SER
SEQRES 8 A 198 THR GLU ALA ALA VAL GLY ALA ALA VAL CYS ARG SER GLY
SEQRES 9 A 198 ARG THR THR GLY TYR GLN CYS GLY THR ILE THR ALA LYS
SEQRES 10 A 198 ASN VAL THR ALA ASN TYR ALA GLU GLY ALA VAL ARG GLY
SEQRES 11 A 198 LEU THR GLN GLY ASN ALA CYS MET GLY ARG GLY ASP SER
SEQRES 12 A 198 GLY GLY SER TRP ILE THR SER ALA GLY GLN ALA GLN GLY
SEQRES 13 A 198 VAL ALA SER GLY GLY ASN VAL GLN SER ASN GLY ASN ASN
SEQRES 14 A 198 CYS GLY ILE PRO ALA SER GLN ARG SER SER LEU PHE GLU
SEQRES 15 A 198 ARG LEU GLN PRO ILE LEU SER GLN TYR GLY LEU SER LEU
SEQRES 16 A 198 VAL THR GLY
SEQRES 1 C 166 ALA ASP GLN VAL ASP PRO GLN LEU LYS PHE ALA MET GLN
SEQRES 2 C 166 ARG ASP LEU GLY ILE PHE PRO THR GLN LEU PRO GLN TYR
SEQRES 3 C 166 LEU GLN THR GLU LYS LEU ALA ARG THR GLN ALA ALA ALA
SEQRES 4 C 166 ILE GLU ARG GLU PHE GLY ALA GLN PHE ALA GLY SER TRP
SEQRES 5 C 166 ILE GLU ARG ASN GLU ASP GLY SER PHE LYS LEU VAL ALA
SEQRES 6 C 166 ALA THR SER GLY ALA ARG LYS SER SER THR LEU GLY GLY
SEQRES 7 C 166 VAL GLU VAL ARG ASN VAL ARG TYR SER LEU LYS GLN LEU
SEQRES 8 C 166 GLN SER ALA MET GLU GLN LEU ASP ALA GLY ALA ASN ALA
SEQRES 9 C 166 ARG VAL LYS GLY VAL SER LYS PRO LEU ASP GLY VAL GLN
SEQRES 10 C 166 SER TRP TYR VAL ASP PRO ARG SER ASN ALA VAL VAL VAL
SEQRES 11 C 166 LYS VAL ASP ASP GLY ALA THR ASP ALA GLY VAL ASP PHE
SEQRES 12 C 166 VAL ALA LEU SER GLY ALA ASP SER ALA GLN VAL ARG ILE
SEQRES 13 C 166 GLU SER SER PRO GLY LYS LEU GLN THR THR
SEQRES 1 B 198 ALA ASN ILE VAL GLY GLY ILE GLU TYR SER ILE ASN ASN
SEQRES 2 B 198 ALA SER LEU CYS SER VAL GLY PHE SER VAL THR ARG GLY
SEQRES 3 B 198 ALA THR LYS GLY PHE VAL THR ALA GLY HIS CYS GLY THR
SEQRES 4 B 198 VAL ASN ALA THR ALA ARG ILE GLY GLY ALA VAL VAL GLY
SEQRES 5 B 198 THR PHE ALA ALA ARG VAL PHE PRO GLY ASN ASP ARG ALA
SEQRES 6 B 198 TRP VAL SER LEU THR SER ALA GLN THR LEU LEU PRO ARG
SEQRES 7 B 198 VAL ALA ASN GLY SER SER PHE VAL THR VAL ARG GLY SER
SEQRES 8 B 198 THR GLU ALA ALA VAL GLY ALA ALA VAL CYS ARG SER GLY
SEQRES 9 B 198 ARG THR THR GLY TYR GLN CYS GLY THR ILE THR ALA LYS
SEQRES 10 B 198 ASN VAL THR ALA ASN TYR ALA GLU GLY ALA VAL ARG GLY
SEQRES 11 B 198 LEU THR GLN GLY ASN ALA CYS MET GLY ARG GLY ASP SER
SEQRES 12 B 198 GLY GLY SER TRP ILE THR SER ALA GLY GLN ALA GLN GLY
SEQRES 13 B 198 VAL ALA SER GLY GLY ASN VAL GLN SER ASN GLY ASN ASN
SEQRES 14 B 198 CYS GLY ILE PRO ALA SER GLN ARG SER SER LEU PHE GLU
SEQRES 15 B 198 ARG LEU GLN PRO ILE LEU SER GLN TYR GLY LEU SER LEU
SEQRES 16 B 198 VAL THR GLY
SEQRES 1 D 166 ALA ASP GLN VAL ASP PRO GLN LEU LYS PHE ALA MET GLN
SEQRES 2 D 166 ARG ASP LEU GLY ILE PHE PRO THR GLN LEU PRO GLN TYR
SEQRES 3 D 166 LEU GLN THR GLU LYS LEU ALA ARG THR GLN ALA ALA ALA
SEQRES 4 D 166 ILE GLU ARG GLU PHE GLY ALA GLN PHE ALA GLY SER TRP
SEQRES 5 D 166 ILE GLU ARG ASN GLU ASP GLY SER PHE LYS LEU VAL ALA
SEQRES 6 D 166 ALA THR SER GLY ALA ARG LYS SER SER THR LEU GLY GLY
SEQRES 7 D 166 VAL GLU VAL ARG ASN VAL ARG TYR SER LEU LYS GLN LEU
SEQRES 8 D 166 GLN SER ALA MET GLU GLN LEU ASP ALA GLY ALA ASN ALA
SEQRES 9 D 166 ARG VAL LYS GLY VAL SER LYS PRO LEU ASP GLY VAL GLN
SEQRES 10 D 166 SER TRP TYR VAL ASP PRO ARG SER ASN ALA VAL VAL VAL
SEQRES 11 D 166 LYS VAL ASP ASP GLY ALA THR ASP ALA GLY VAL ASP PHE
SEQRES 12 D 166 VAL ALA LEU SER GLY ALA ASP SER ALA GLN VAL ARG ILE
SEQRES 13 D 166 GLU SER SER PRO GLY LYS LEU GLN THR THR
FORMUL 5 HOH *69(H2 O)
HELIX 1 1 GLY A 35 CYS A 37 5 3
HELIX 2 2 ALA A 174 GLN A 176 5 3
HELIX 3 3 LEU A 184 GLN A 190 1 7
HELIX 4 4 GLN C 7 LEU C 16 1 10
HELIX 5 5 PRO C 20 GLN C 47 1 28
HELIX 6 6 LEU C 88 ALA C 102 1 15
HELIX 7 7 PRO C 123 SER C 125 5 3
HELIX 8 8 THR C 137 SER C 147 1 11
HELIX 9 9 SER C 151 GLN C 153 5 3
HELIX 10 10 GLY B 35 CYS B 37 5 3
HELIX 11 11 ALA B 174 GLN B 176 5 3
HELIX 12 12 LEU B 184 TYR B 191 1 8
HELIX 13 13 PRO D 6 LEU D 16 1 11
HELIX 14 14 PRO D 20 THR D 35 1 16
HELIX 15 15 ALA D 37 GLN D 47 1 11
HELIX 16 16 LEU D 88 ALA D 102 1 15
HELIX 17 17 PRO D 123 SER D 125 5 3
HELIX 18 18 THR D 137 SER D 147 1 11
HELIX 19 19 SER D 151 GLN D 153 5 3
SHEET 1 A 2 GLU A 8 ILE A 11 0
SHEET 2 A 2 SER A 15 SER A 18 -1 N CYS A 17 O TYR A 9
SHEET 1 B 5 PHE A 21 ARG A 25 0
SHEET 2 B 5 THR A 28 THR A 33 -1 N VAL A 32 O PHE A 21
SHEET 3 B 5 ARG A 64 LEU A 69 -1 N VAL A 67 O PHE A 31
SHEET 4 B 5 ALA A 49 VAL A 58 -1 N VAL A 58 O ARG A 64
SHEET 5 B 5 THR A 43 ILE A 46 -1 N ILE A 46 O ALA A 49
SHEET 1 C 2 ARG A 78 ASN A 81 0
SHEET 2 C 2 SER A 84 THR A 87 -1 N VAL A 86 O VAL A 79
SHEET 1 D 6 GLY A 108 THR A 113 0
SHEET 2 D 6 ALA A 99 GLY A 104 -1 N GLY A 104 O GLY A 108
SHEET 3 D 6 SER A 146 THR A 149 -1 N ILE A 148 O CYS A 101
SHEET 4 D 6 ALA A 154 GLY A 161 -1 N GLY A 156 O TRP A 147
SHEET 5 D 6 SER A 179 ARG A 183 -1 N GLU A 182 O VAL A 157
SHEET 6 D 6 THR A 132 GLY A 134 -1 N GLY A 134 O SER A 179
SHEET 1 E 2 ALA A 121 TYR A 123 0
SHEET 2 E 2 GLY A 126 VAL A 128 -1 N VAL A 128 O ALA A 121
SHEET 1 F 3 SER C 51 ARG C 55 0
SHEET 2 F 3 PHE C 61 THR C 67 -1 N VAL C 64 O TRP C 52
SHEET 3 F 3 GLU C 80 ASN C 83 1 N GLU C 80 O ALA C 65
SHEET 1 G 3 VAL C 154 SER C 159 0
SHEET 2 G 3 ALA C 127 ASP C 133 1 N VAL C 128 O ARG C 155
SHEET 3 G 3 VAL C 116 ASP C 122 -1 N ASP C 122 O ALA C 127
SHEET 1 H 2 GLU B 8 ILE B 11 0
SHEET 2 H 2 SER B 15 SER B 18 -1 N CYS B 17 O TYR B 9
SHEET 1 I 5 PHE B 21 ARG B 25 0
SHEET 2 I 5 THR B 28 THR B 33 -1 N VAL B 32 O PHE B 21
SHEET 3 I 5 ARG B 64 LEU B 69 -1 N VAL B 67 O PHE B 31
SHEET 4 I 5 ALA B 49 VAL B 58 -1 N VAL B 58 O ARG B 64
SHEET 5 I 5 THR B 43 ILE B 46 -1 N ILE B 46 O ALA B 49
SHEET 1 J 2 ARG B 78 ASN B 81 0
SHEET 2 J 2 SER B 84 THR B 87 -1 N VAL B 86 O VAL B 79
SHEET 1 K 6 GLY B 108 THR B 113 0
SHEET 2 K 6 ALA B 99 GLY B 104 -1 N GLY B 104 O GLY B 108
SHEET 3 K 6 SER B 146 ILE B 148 -1 N ILE B 148 O CYS B 101
SHEET 4 K 6 ALA B 154 GLY B 161 -1 N GLY B 156 O TRP B 147
SHEET 5 K 6 SER B 179 ARG B 183 -1 N GLU B 182 O VAL B 157
SHEET 6 K 6 THR B 132 GLY B 134 -1 N GLY B 134 O SER B 179
SHEET 1 L 2 ALA B 121 TYR B 123 0
SHEET 2 L 2 GLY B 126 VAL B 128 -1 N VAL B 128 O ALA B 121
SHEET 1 M 3 SER D 51 ARG D 55 0
SHEET 2 M 3 PHE D 61 THR D 67 -1 N VAL D 64 O TRP D 52
SHEET 3 M 3 VAL D 79 ASN D 83 1 N GLU D 80 O LEU D 63
SHEET 1 N 3 VAL D 154 SER D 159 0
SHEET 2 N 3 ALA D 127 ASP D 133 1 N VAL D 128 O ARG D 155
SHEET 3 N 3 VAL D 116 ASP D 122 -1 N ASP D 122 O ALA D 127
SSBOND 1 CYS A 17 CYS A 37 1555 1555 2.03
SSBOND 2 CYS A 101 CYS A 111 1555 1555 2.03
SSBOND 3 CYS A 137 CYS A 170 1555 1555 2.03
SSBOND 4 CYS B 17 CYS B 37 1555 1555 2.02
SSBOND 5 CYS B 101 CYS B 111 1555 1555 2.03
SSBOND 6 CYS B 137 CYS B 170 1555 1555 2.03
CISPEP 1 PHE A 59 PRO A 60 0 -0.11
CISPEP 2 PHE B 59 PRO B 60 0 0.00
CRYST1 53.800 61.900 72.600 109.40 99.20 102.40 P 1 2
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 0.018587 0.004087 0.004934 0.00000
SCALE2 0.000000 0.016541 0.006798 0.00000
SCALE3 0.000000 0.000000 0.015086 0.00000
MTRIX1 1 0.778697 0.440619 0.446638 -20.37255 1
MTRIX2 1 0.429057 -0.893387 0.133302 26.29845 1
MTRIX3 1 0.457756 0.087831 -0.884729 54.59003 1
(ATOM LINES ARE NOT SHOWN.)
END
