HEADER HYDROLASE (ACID PROTEINASE) 23-JAN-95 1PSN
TITLE THE CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX WITH
TITLE 2 PEPSTATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPSIN 3A;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.23.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HYDROLASE (ACID PROTEINASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FUJINAGA,M.M.CHERNAIA,N.TARASOVA,S.C.MOSIMANN,M.N.G.JAMES
REVDAT 2 24-FEB-09 1PSN 1 VERSN
REVDAT 1 20-APR-95 1PSN 0
JRNL AUTH M.FUJINAGA,M.M.CHERNAIA,N.I.TARASOVA,S.C.MOSIMANN,
JRNL AUTH 2 M.N.JAMES
JRNL TITL CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX
JRNL TITL 2 WITH PEPSTATIN.
JRNL REF PROTEIN SCI. V. 4 960 1995
JRNL REFN ISSN 0961-8368
JRNL PMID 7663352
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.R.SIELECKI,A.A.FEDOROV,A.BOODHOO,N.S.ANDREEVA,
REMARK 1 AUTH 2 M.N.G.JAMES
REMARK 1 TITL MOLECULAR AND CRYSTAL STRUCTURES OF MONOCLINIC
REMARK 1 TITL 2 PORCINE PEPSIN REFINED AT 1.8 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 214 143 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMOS
REMARK 3 AUTHORS : FUJINAGA,GROS,VAN GUNSTEREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 21303
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) : 0.188
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 : 2438
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 136
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.00
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.39
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.81
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES WITH ZERO OCCUPANCIES AND
REMARK 3 NEGATIVE B-FACTORS ARE DISORDERED AND THEIR POSITIONS ARE NOT
REMARK 3 CONSIDERED TO HAVE BEEN DETERMINED.
REMARK 4
REMARK 4 1PSN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SAN DIEGO MULTIWIRE DETECTION
REMARK 200 SYSTEM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAN DIEGO SOFTWARE
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33057
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.0
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 35.98500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 20.57500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.79500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 20.57500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.98500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.79500
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 VAL A 1
REMARK 475 SER A 241
REMARK 475 ASP A 242
REMARK 475 GLY A 243
REMARK 475 GLU A 294
REMARK 475 SER A 295
REMARK 475 GLY A 296
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 125 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
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 ASP A 159 16.41 57.02
REMARK 500 ASN A 240 -162.67 -100.71
REMARK 500 GLU A 279 61.23 61.28
REMARK 500 SER A 295 42.83 -103.86
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 PHE A 27 0.08 SIDE_CHAIN
REMARK 500 TYR A 154 0.10 SIDE_CHAIN
REMARK 500 TYR A 175 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 301 12.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 399 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH A 403 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 419 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH A 440 DISTANCE = 6.13 ANGSTROMS
DBREF 1PSN A 1 326 UNP P00790 PEPA_HUMAN 63 388
SEQRES 1 A 326 VAL ASP GLU GLN PRO LEU GLU ASN TYR LEU ASP MET GLU
SEQRES 2 A 326 TYR PHE GLY THR ILE GLY ILE GLY THR PRO ALA GLN ASP
SEQRES 3 A 326 PHE THR VAL VAL PHE ASP THR GLY SER SER ASN LEU TRP
SEQRES 4 A 326 VAL PRO SER VAL TYR CYS SER SER LEU ALA CYS THR ASN
SEQRES 5 A 326 HIS ASN ARG PHE ASN PRO GLU ASP SER SER THR TYR GLN
SEQRES 6 A 326 SER THR SER GLU THR VAL SER ILE THR TYR GLY THR GLY
SEQRES 7 A 326 SER MET THR GLY ILE LEU GLY TYR ASP THR VAL GLN VAL
SEQRES 8 A 326 GLY GLY ILE SER ASP THR ASN GLN ILE PHE GLY LEU SER
SEQRES 9 A 326 GLU THR GLU PRO GLY SER PHE LEU TYR TYR ALA PRO PHE
SEQRES 10 A 326 ASP GLY ILE LEU GLY LEU ALA TYR PRO SER ILE SER SER
SEQRES 11 A 326 SER GLY ALA THR PRO VAL PHE ASP ASN ILE TRP ASN GLN
SEQRES 12 A 326 GLY LEU VAL SER GLN ASP LEU PHE SER VAL TYR LEU SER
SEQRES 13 A 326 ALA ASP ASP GLN SER GLY SER VAL VAL ILE PHE GLY GLY
SEQRES 14 A 326 ILE ASP SER SER TYR TYR THR GLY SER LEU ASN TRP VAL
SEQRES 15 A 326 PRO VAL THR VAL GLU GLY TYR TRP GLN ILE THR VAL ASP
SEQRES 16 A 326 SER ILE THR MET ASN GLY GLU ALA ILE ALA CYS ALA GLU
SEQRES 17 A 326 GLY CYS GLN ALA ILE VAL ASP THR GLY THR SER LEU LEU
SEQRES 18 A 326 THR GLY PRO THR SER PRO ILE ALA ASN ILE GLN SER ASP
SEQRES 19 A 326 ILE GLY ALA SER GLU ASN SER ASP GLY ASP MET VAL VAL
SEQRES 20 A 326 SER CYS SER ALA ILE SER SER LEU PRO ASP ILE VAL PHE
SEQRES 21 A 326 THR ILE ASN GLY VAL GLN TYR PRO VAL PRO PRO SER ALA
SEQRES 22 A 326 TYR ILE LEU GLN SER GLU GLY SER CYS ILE SER GLY PHE
SEQRES 23 A 326 GLN GLY MET ASN LEU PRO THR GLU SER GLY GLU LEU TRP
SEQRES 24 A 326 ILE LEU GLY ASP VAL PHE ILE ARG GLN TYR PHE THR VAL
SEQRES 25 A 326 PHE ASP ARG ALA ASN ASN GLN VAL GLY LEU ALA PRO VAL
SEQRES 26 A 326 ALA
FORMUL 2 HOH *136(H2 O)
HELIX 1 1 LEU A 48 ASN A 52 1 5
HELIX 2 2 PRO A 58 ASP A 60 5 3
HELIX 3 3 PHE A 111 TYR A 114 1 4
HELIX 4 4 PRO A 126 ILE A 128 5 3
HELIX 5 5 SER A 130 GLY A 132 5 3
HELIX 6 6 VAL A 136 ASN A 142 1 7
HELIX 7 7 SER A 172 TYR A 174 5 3
HELIX 8 8 THR A 225 ASP A 234 1 10
HELIX 9 9 CYS A 249 SER A 254 5 6
HELIX 10 10 PRO A 271 TYR A 274 1 4
HELIX 11 11 ASP A 303 ILE A 306 1 4
SHEET 1 A 6 ASP A 2 PRO A 5 0
SHEET 2 A 6 VAL A 164 PHE A 167 -1 N PHE A 167 O ASP A 2
SHEET 3 A 6 LEU A 150 TYR A 154 -1 N TYR A 154 O VAL A 164
SHEET 4 A 6 TYR A 309 ASP A 314 -1 N PHE A 313 O PHE A 151
SHEET 5 A 6 GLN A 319 PRO A 324 -1 N ALA A 323 O PHE A 310
SHEET 6 A 6 ASN A 180 PRO A 183 -1 N VAL A 182 O VAL A 320
SHEET 1 B 4 GLU A 7 TYR A 9 0
SHEET 2 B 4 GLU A 13 ILE A 20 -1 N PHE A 15 O GLU A 7
SHEET 3 B 4 GLN A 25 ASP A 32 -1 N VAL A 29 O GLY A 16
SHEET 4 B 4 GLY A 119 GLY A 122 1 N GLY A 119 O VAL A 30
SHEET 1 C 3 THR A 70 THR A 74 0
SHEET 2 C 3 SER A 79 ASP A 87 -1 N GLY A 82 O VAL A 71
SHEET 3 C 3 GLN A 99 THR A 106 -1 N THR A 106 O THR A 81
SHEET 1 D 2 VAL A 89 VAL A 91 0
SHEET 2 D 2 ILE A 94 ASP A 96 -1 N ASP A 96 O VAL A 89
SHEET 1 E 3 GLN A 191 VAL A 194 0
SHEET 2 E 3 CYS A 210 VAL A 214 -1 N ALA A 212 O ILE A 192
SHEET 3 E 3 LEU A 298 LEU A 301 1 N TRP A 299 O GLN A 211
SHEET 1 F 4 VAL A 265 VAL A 269 0
SHEET 2 F 4 ILE A 258 ILE A 262 -1 N ILE A 262 O VAL A 265
SHEET 3 F 4 SER A 196 MET A 199 -1 N THR A 198 O VAL A 259
SHEET 4 F 4 GLU A 202 ALA A 205 -1 N ALA A 205 O ILE A 197
SHEET 1 G 2 LEU A 221 GLY A 223 0
SHEET 2 G 2 PHE A 286 GLY A 288 1 N GLN A 287 O LEU A 221
SHEET 1 H 2 ILE A 275 SER A 278 0
SHEET 2 H 2 SER A 281 SER A 284 -1 N ILE A 283 O LEU A 276
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.03
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.04
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.04
CISPEP 1 THR A 22 PRO A 23 0 -4.09
CRYST1 71.970 151.590 41.150 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 0.013895 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006597 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END