HEADER HYDROLASE 16-JUN-99 1QRX
TITLE CRYSTAL STRUCTURE OF WILD-TYPE ALPHA-LYTIC PROTEASE AT 1.6 A, PH 5.14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-LYTIC PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MATURE PROTEASE DOMAIN, RESIDUES 1-198;
COMPND 5 EC: 3.4.21.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LYSOBACTER ENZYMOGENES;
SOURCE 3 ORGANISM_TAXID: 69;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PALP12
KEYWDS PROTEIN FOLDING, PRO REGION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.I.DERMAN,T.MAU,D.A.AGARD
REVDAT 4 13-JUL-11 1QRX 1 VERSN
REVDAT 3 24-FEB-09 1QRX 1 VERSN
REVDAT 2 23-SEP-03 1QRX 1 DBREF
REVDAT 1 18-JUN-99 1QRX 0
JRNL AUTH A.I.DERMAN,T.MAU,D.A.AGARD
JRNL TITL A GENETIC SCREEN THAT TARGETS SPECIFICALLY THE FOLDING
JRNL TITL 2 TRANSITION STATE OF ALPHA-LYTIC PROTEASE
JRNL REF TO BE PUBLISHED 1999
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
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) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 26057
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) : 0.165
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2581
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 : 1391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 257
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.57
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QRX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB009192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 97
REMARK 200 PH : 5.14
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
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 RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26626
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.880
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.37500
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 (%): 50.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, TRIS-SULFATE, PH
REMARK 280 5.14, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.97333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.48667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.48667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.97333
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 355 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 456 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 205 O HOH A 206 2.18
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 ALA A 14 -90.33 -126.54
REMARK 500 ASN A 41 -5.16 81.19
REMARK 500 PRO A 60 -151.82 -85.10
REMARK 500 SER A 84 -168.58 -100.76
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 248 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 283 DISTANCE = 5.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QQ4 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE R102H/G134S MUTANT AT THE SAME PH
REMARK 900 (5.14).
REMARK 900 RELATED ID: 1TAL RELATED DB: PDB
REMARK 900 THE TRUCTURE OF SAME MOLECULE DETERMINED AT PH 8. IN
REMARK 900 ADDITION, THE TRIS MOLECULE (TAM) IN 1TAL SHOULD HAVE BEEN
REMARK 900 MODELED AS A GLYCEROL MOLECULE, AS IT IS DONE IN THIS ENTRY.
DBREF 1QRX A 1 198 UNP P00778 PRLA_LYSEN 200 397
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 MET 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
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 A 204 5
HET GOL A 201 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *257(H2 O)
HELIX 1 1 ALA A 34 GLY A 38 5 5
HELIX 2 2 PRO A 173 ARG A 177 5 5
HELIX 3 3 LEU A 184 GLY A 192 1 9
SHEET 1 A 3 ASN A 2 GLY A 5 0
SHEET 2 A 3 THR A 74 ASN A 81 1 O THR A 74 N ILE A 3
SHEET 3 A 3 SER A 84 THR A 87 -1 N SER A 84 O ASN A 81
SHEET 1 B 8 SER A 15 SER A 18 0
SHEET 2 B 8 GLU A 8 ILE A 11 -1 O TYR A 9 N CYS A 17
SHEET 3 B 8 THR A 43 ILE A 46 -1 O ARG A 45 N SER A 10
SHEET 4 B 8 ALA A 49 VAL A 58 -1 O ALA A 49 N ILE A 46
SHEET 5 B 8 ARG A 64 LEU A 69 -1 O ARG A 64 N VAL A 58
SHEET 6 B 8 THR A 28 THR A 33 -1 O LYS A 29 N LEU A 69
SHEET 7 B 8 PHE A 21 ARG A 25 -1 O PHE A 21 N VAL A 32
SHEET 8 B 8 SER A 194 LEU A 195 -1 N SER A 194 O THR A 24
SHEET 1 C 7 ALA A 99 GLY A 104 0
SHEET 2 C 7 GLY A 108 TYR A 123 -1 N GLY A 108 O GLY A 104
SHEET 3 C 7 ALA A 99 GLY A 104 -1 O VAL A 100 N GLY A 112
SHEET 4 C 7 SER A 146 ILE A 148 -1 O SER A 146 N SER A 103
SHEET 5 C 7 ALA A 154 GLY A 161 -1 N GLN A 155 O TRP A 147
SHEET 6 C 7 SER A 179 ARG A 183 -1 N LEU A 180 O GLY A 160
SHEET 7 C 7 GLY A 126 GLY A 134 -1 O THR A 132 N PHE A 181
SSBOND 1 CYS A 17 CYS A 37 1555 1555 2.10
SSBOND 2 CYS A 101 CYS A 111 1555 1555 2.10
SSBOND 3 CYS A 137 CYS A 170 1555 1555 2.09
CISPEP 1 PHE A 59 PRO A 60 0 5.53
SITE 1 AC1 11 ARG A 25 ARG A 78 GLN A 190 TYR A 191
SITE 2 AC1 11 HOH A 230 HOH A 231 HOH A 232 HOH A 380
SITE 3 AC1 11 HOH A 381 HOH A 382 HOH A 429
SITE 1 AC2 10 ALA A 1 ASN A 2 ARG A 183 PRO A 186
SITE 2 AC2 10 HOH A 207 HOH A 273 HOH A 342 HOH A 343
SITE 3 AC2 10 HOH A 398 HOH A 399
SITE 1 AC3 9 HIS A 36 ARG A 89 ARG A 140 GLY A 141
SITE 2 AC3 9 SER A 143 GOL A 201 HOH A 361 HOH A 362
SITE 3 AC3 9 HOH A 363
SITE 1 AC4 7 HIS A 36 ARG A 89 TYR A 123 GLU A 125
SITE 2 AC4 7 SER A 159 GLY A 160 SO4 A 204
CRYST1 65.627 65.627 79.460 90.00 90.00 120.00 P 32 2 1 6
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 0.015238 0.008797 0.000000 0.00000
SCALE2 0.000000 0.017595 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012585 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
