HEADER HYDROLASE/HYDROLASE INHIBITOR 24-SEP-13 4MVN
TITLE CRYSTAL STRUCTURE OF THE STAPHYLOCOCCAL SERINE PROTEASE SPLA IN
TITLE 2 COMPLEX WITH A SPECIFIC PHOSPHONATE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE SPLA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.4.21.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 93061;
SOURCE 4 STRAIN: NCTC 8325;
SOURCE 5 GENE: SPLA, SAOUHSC_01942;
SOURCE 6 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1423
KEYWDS CHYMOTRYPSIN-LIKE FOLD, SERINE ENDOPEPTIDASE, EXTRACELLULAR
KEYWDS 2 STAPHYLOCOCCAL PROTEASES, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZDZALIK,E.BURCHACKA,J.S.NIEMCZYK,K.PUSTELNY,G.M.POPOWICZ,B.WLADYKA,
AUTHOR 2 A.DUBIN,J.POTEMPA,M.SIENCZYK,G.DUBIN,J.OLEKSYSZYN
REVDAT 3 08-NOV-23 4MVN 1 REMARK LINK
REVDAT 2 05-MAR-14 4MVN 1 JRNL
REVDAT 1 22-JAN-14 4MVN 0
JRNL AUTH E.BURCHACKA,M.ZDZALIK,J.S.NIEMCZYK,K.PUSTELNY,G.POPOWICZ,
JRNL AUTH 2 B.WLADYKA,A.DUBIN,J.POTEMPA,M.SIENCZYK,G.DUBIN,J.OLEKSYSZYN
JRNL TITL DEVELOPMENT AND BINDING CHARACTERISTICS OF PHOSPHONATE
JRNL TITL 2 INHIBITORS OF SPLA PROTEASE FROM STAPHYLOCOCCUS AUREUS.
JRNL REF PROTEIN SCI. V. 23 179 2014
JRNL REFN ISSN 0961-8368
JRNL PMID 24375505
JRNL DOI 10.1002/PRO.2403
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 81518
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 + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4355
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6038
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 303
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 873
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.05000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.105
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.912
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6351 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8619 ; 2.129 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 828 ; 6.910 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 283 ;38.936 ;25.760
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1009 ;12.683 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;24.239 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 944 ; 0.167 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4907 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3971 ; 1.449 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6420 ; 2.291 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2380 ; 3.315 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2180 ; 4.951 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4MVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85873
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2W7S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 0.2M CALCIUM CHLORIDE, 25%
REMARK 280 PEG 4000, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 297K, VAPOR
REMARK 280 DIFFUSION, SITTING DROP
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 36.56550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.89350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.81300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.89350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.56550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.81300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 177
REMARK 465 LYS B 60
REMARK 465 LYS C 58
REMARK 465 GLY C 59
REMARK 465 LYS C 60
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 LYS A 2 CD CE NZ
REMARK 470 LYS A 42 CD CE NZ
REMARK 470 LYS A 48 CD CE NZ
REMARK 470 LYS A 58 CE NZ
REMARK 470 LYS A 60 CD CE NZ
REMARK 470 GLU A 72 OE1 OE2
REMARK 470 LYS A 96 NZ
REMARK 470 LYS A 108 CE NZ
REMARK 470 LYS A 110 CE NZ
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 ASP A 176 CA C O CB CG OD1 OD2
REMARK 470 LYS A 200 CD CE NZ
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LYS B 31 CD CE NZ
REMARK 470 LYS B 42 CE NZ
REMARK 470 ASP B 45 CG OD1 OD2
REMARK 470 LYS B 48 CD CE NZ
REMARK 470 LYS B 58 CD CE NZ
REMARK 470 GLY B 59 C O
REMARK 470 GLU B 90 CG CD OE1 OE2
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 LYS B 108 CD CE NZ
REMARK 470 LYS B 110 CD CE NZ
REMARK 470 LYS B 120 CE NZ
REMARK 470 LYS B 125 CB CG CD CE NZ
REMARK 470 LYS B 127 CD CE NZ
REMARK 470 LYS B 162 NZ
REMARK 470 LYS B 175 NZ
REMARK 470 ASP B 176 OD1 OD2
REMARK 470 LYS B 200 CG CD CE NZ
REMARK 470 LYS C 2 NZ
REMARK 470 LYS C 5 CG CD CE NZ
REMARK 470 LYS C 12 CD CE NZ
REMARK 470 LYS C 31 NZ
REMARK 470 SER C 57 CB OG
REMARK 470 GLY C 61 N CA
REMARK 470 LYS C 96 CE NZ
REMARK 470 LYS C 102 CD CE NZ
REMARK 470 LYS C 110 CD CE NZ
REMARK 470 LYS C 162 NZ
REMARK 470 LYS C 175 CD CE NZ
REMARK 470 LYS C 200 CD CE NZ
REMARK 470 LYS D 12 CE NZ
REMARK 470 LYS D 42 CE NZ
REMARK 470 LYS D 58 NZ
REMARK 470 LYS D 60 CD CE NZ
REMARK 470 LYS D 102 CD CE NZ
REMARK 470 LYS D 125 CD CE NZ
REMARK 470 GLU D 192 CD OE1 OE2
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 C 475 O HOH C 495 2.13
REMARK 500 O HOH D 572 O HOH D 588 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 107 C ALA A 107 O 0.140
REMARK 500 PHE A 145 CZ PHE A 145 CE2 0.124
REMARK 500 TYR C 73 CE2 TYR C 73 CD2 0.107
REMARK 500 VAL C 84 CB VAL C 84 CG2 0.134
REMARK 500 GLY D 62 N GLY D 62 CA 0.093
REMARK 500 TYR D 170 CE2 TYR D 170 CD2 0.092
REMARK 500
REMARK 500 REMARK: NULL
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 GLY D 61 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 GLY D 62 C - N - CA ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG D 112 NE - CZ - NH2 ANGL. DEV. = -3.5 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 ASN A 32 20.72 49.72
REMARK 500 LYS A 110 -5.48 87.31
REMARK 500 LYS B 2 78.91 -119.88
REMARK 500 HIS B 54 46.39 39.02
REMARK 500 LYS B 110 -6.53 84.29
REMARK 500 ASP C 45 -112.18 56.73
REMARK 500 LYS C 110 -8.62 85.57
REMARK 500 ASN D 32 19.67 56.07
REMARK 500 LYS D 110 -7.33 83.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 174 LYS A 175 -136.43
REMARK 500 LYS D 60 GLY D 61 -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE INHIBITOR FULL CHEMICAL FORMULA CBZ-PHE(P)(OC6H5-4-SO2CH3)2 IS
REMARK 600 HYDROLYSED BY THE PROTEASE (THAT IS THE REACTION MECHANISM) AND
REMARK 600 ONLY THE PART CBZ-PHE(P) (LIGAND I1S) OF IT INTERACTS WITH THE
REMARK 600 PROTEIN.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I1S A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I1S B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I1S C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I1S D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UFA RELATED DB: PDB
REMARK 900 RELATED ID: 3W7S RELATED DB: PDB
REMARK 900 APO-PROTEIN
REMARK 900 RELATED ID: 2W7U RELATED DB: PDB
REMARK 900 APO-PROTEIN
DBREF 4MVN A 1 200 UNP Q2FXC2 SPLA_STAA8 36 235
DBREF 4MVN B 1 200 UNP Q2FXC2 SPLA_STAA8 36 235
DBREF 4MVN C 1 200 UNP Q2FXC2 SPLA_STAA8 36 235
DBREF 4MVN D 1 200 UNP Q2FXC2 SPLA_STAA8 36 235
SEQRES 1 A 200 GLU LYS ASN VAL LYS GLU ILE THR ASP ALA THR LYS GLU
SEQRES 2 A 200 PRO TYR ASN SER VAL VAL ALA PHE VAL GLY GLY THR GLY
SEQRES 3 A 200 VAL VAL VAL GLY LYS ASN THR ILE VAL THR ASN LYS HIS
SEQRES 4 A 200 ILE ALA LYS SER ASN ASP ILE PHE LYS ASN ARG VAL SER
SEQRES 5 A 200 ALA HIS HIS SER SER LYS GLY LYS GLY GLY GLY ASN TYR
SEQRES 6 A 200 ASP VAL LYS ASP ILE VAL GLU TYR PRO GLY LYS GLU ASP
SEQRES 7 A 200 LEU ALA ILE VAL HIS VAL HIS GLU THR SER THR GLU GLY
SEQRES 8 A 200 LEU ASN PHE ASN LYS ASN VAL SER TYR THR LYS PHE ALA
SEQRES 9 A 200 ASP GLY ALA LYS VAL LYS ASP ARG ILE SER VAL ILE GLY
SEQRES 10 A 200 TYR PRO LYS GLY ALA GLN THR LYS TYR LYS MET PHE GLU
SEQRES 11 A 200 SER THR GLY THR ILE ASN HIS ILE SER GLY THR PHE MET
SEQRES 12 A 200 GLU PHE ASP ALA TYR ALA GLN PRO GLY ASN SER GLY SER
SEQRES 13 A 200 PRO VAL LEU ASN SER LYS HIS GLU LEU ILE GLY ILE LEU
SEQRES 14 A 200 TYR ALA GLY SER GLY LYS ASP GLU SER GLU LYS ASN PHE
SEQRES 15 A 200 GLY VAL TYR PHE THR PRO GLN LEU LYS GLU PHE ILE GLN
SEQRES 16 A 200 ASN ASN ILE GLU LYS
SEQRES 1 B 200 GLU LYS ASN VAL LYS GLU ILE THR ASP ALA THR LYS GLU
SEQRES 2 B 200 PRO TYR ASN SER VAL VAL ALA PHE VAL GLY GLY THR GLY
SEQRES 3 B 200 VAL VAL VAL GLY LYS ASN THR ILE VAL THR ASN LYS HIS
SEQRES 4 B 200 ILE ALA LYS SER ASN ASP ILE PHE LYS ASN ARG VAL SER
SEQRES 5 B 200 ALA HIS HIS SER SER LYS GLY LYS GLY GLY GLY ASN TYR
SEQRES 6 B 200 ASP VAL LYS ASP ILE VAL GLU TYR PRO GLY LYS GLU ASP
SEQRES 7 B 200 LEU ALA ILE VAL HIS VAL HIS GLU THR SER THR GLU GLY
SEQRES 8 B 200 LEU ASN PHE ASN LYS ASN VAL SER TYR THR LYS PHE ALA
SEQRES 9 B 200 ASP GLY ALA LYS VAL LYS ASP ARG ILE SER VAL ILE GLY
SEQRES 10 B 200 TYR PRO LYS GLY ALA GLN THR LYS TYR LYS MET PHE GLU
SEQRES 11 B 200 SER THR GLY THR ILE ASN HIS ILE SER GLY THR PHE MET
SEQRES 12 B 200 GLU PHE ASP ALA TYR ALA GLN PRO GLY ASN SER GLY SER
SEQRES 13 B 200 PRO VAL LEU ASN SER LYS HIS GLU LEU ILE GLY ILE LEU
SEQRES 14 B 200 TYR ALA GLY SER GLY LYS ASP GLU SER GLU LYS ASN PHE
SEQRES 15 B 200 GLY VAL TYR PHE THR PRO GLN LEU LYS GLU PHE ILE GLN
SEQRES 16 B 200 ASN ASN ILE GLU LYS
SEQRES 1 C 200 GLU LYS ASN VAL LYS GLU ILE THR ASP ALA THR LYS GLU
SEQRES 2 C 200 PRO TYR ASN SER VAL VAL ALA PHE VAL GLY GLY THR GLY
SEQRES 3 C 200 VAL VAL VAL GLY LYS ASN THR ILE VAL THR ASN LYS HIS
SEQRES 4 C 200 ILE ALA LYS SER ASN ASP ILE PHE LYS ASN ARG VAL SER
SEQRES 5 C 200 ALA HIS HIS SER SER LYS GLY LYS GLY GLY GLY ASN TYR
SEQRES 6 C 200 ASP VAL LYS ASP ILE VAL GLU TYR PRO GLY LYS GLU ASP
SEQRES 7 C 200 LEU ALA ILE VAL HIS VAL HIS GLU THR SER THR GLU GLY
SEQRES 8 C 200 LEU ASN PHE ASN LYS ASN VAL SER TYR THR LYS PHE ALA
SEQRES 9 C 200 ASP GLY ALA LYS VAL LYS ASP ARG ILE SER VAL ILE GLY
SEQRES 10 C 200 TYR PRO LYS GLY ALA GLN THR LYS TYR LYS MET PHE GLU
SEQRES 11 C 200 SER THR GLY THR ILE ASN HIS ILE SER GLY THR PHE MET
SEQRES 12 C 200 GLU PHE ASP ALA TYR ALA GLN PRO GLY ASN SER GLY SER
SEQRES 13 C 200 PRO VAL LEU ASN SER LYS HIS GLU LEU ILE GLY ILE LEU
SEQRES 14 C 200 TYR ALA GLY SER GLY LYS ASP GLU SER GLU LYS ASN PHE
SEQRES 15 C 200 GLY VAL TYR PHE THR PRO GLN LEU LYS GLU PHE ILE GLN
SEQRES 16 C 200 ASN ASN ILE GLU LYS
SEQRES 1 D 200 GLU LYS ASN VAL LYS GLU ILE THR ASP ALA THR LYS GLU
SEQRES 2 D 200 PRO TYR ASN SER VAL VAL ALA PHE VAL GLY GLY THR GLY
SEQRES 3 D 200 VAL VAL VAL GLY LYS ASN THR ILE VAL THR ASN LYS HIS
SEQRES 4 D 200 ILE ALA LYS SER ASN ASP ILE PHE LYS ASN ARG VAL SER
SEQRES 5 D 200 ALA HIS HIS SER SER LYS GLY LYS GLY GLY GLY ASN TYR
SEQRES 6 D 200 ASP VAL LYS ASP ILE VAL GLU TYR PRO GLY LYS GLU ASP
SEQRES 7 D 200 LEU ALA ILE VAL HIS VAL HIS GLU THR SER THR GLU GLY
SEQRES 8 D 200 LEU ASN PHE ASN LYS ASN VAL SER TYR THR LYS PHE ALA
SEQRES 9 D 200 ASP GLY ALA LYS VAL LYS ASP ARG ILE SER VAL ILE GLY
SEQRES 10 D 200 TYR PRO LYS GLY ALA GLN THR LYS TYR LYS MET PHE GLU
SEQRES 11 D 200 SER THR GLY THR ILE ASN HIS ILE SER GLY THR PHE MET
SEQRES 12 D 200 GLU PHE ASP ALA TYR ALA GLN PRO GLY ASN SER GLY SER
SEQRES 13 D 200 PRO VAL LEU ASN SER LYS HIS GLU LEU ILE GLY ILE LEU
SEQRES 14 D 200 TYR ALA GLY SER GLY LYS ASP GLU SER GLU LYS ASN PHE
SEQRES 15 D 200 GLY VAL TYR PHE THR PRO GLN LEU LYS GLU PHE ILE GLN
SEQRES 16 D 200 ASN ASN ILE GLU LYS
HET I1S A 301 22
HET I1S B 301 22
HET I1S C 301 44
HET I1S D 301 22
HETNAM I1S [(1S)-1-{[(BENZYLOXY)CARBONYL]AMINO}-2-
HETNAM 2 I1S PHENYLETHYL]PHOSPHONIC ACID
FORMUL 5 I1S 4(C16 H18 N O5 P)
FORMUL 9 HOH *873(H2 O)
HELIX 1 1 PRO A 14 ASN A 16 5 3
HELIX 2 2 ASN A 37 LYS A 48 1 12
HELIX 3 3 ASN A 93 VAL A 98 1 6
HELIX 4 4 LYS A 120 THR A 124 5 5
HELIX 5 5 THR A 187 ASN A 197 1 11
HELIX 6 6 PRO B 14 ASN B 16 5 3
HELIX 7 7 ASN B 37 LYS B 42 1 6
HELIX 8 8 ASN B 93 VAL B 98 1 6
HELIX 9 9 LYS B 120 LYS B 125 1 6
HELIX 10 10 THR B 187 ASN B 197 1 11
HELIX 11 11 PRO C 14 ASN C 16 5 3
HELIX 12 12 ASN C 37 LYS C 42 1 6
HELIX 13 13 ASN C 93 VAL C 98 1 6
HELIX 14 14 LYS C 120 LYS C 125 1 6
HELIX 15 15 THR C 187 ASN C 197 1 11
HELIX 16 16 PRO D 14 ASN D 16 5 3
HELIX 17 17 ASN D 37 PHE D 47 1 11
HELIX 18 18 ASN D 93 VAL D 98 1 6
HELIX 19 19 LYS D 120 LYS D 125 1 6
HELIX 20 20 THR D 187 ASN D 197 1 11
SHEET 1 A 8 VAL A 4 ILE A 7 0
SHEET 2 A 8 MET A 128 SER A 139 -1 O GLU A 130 N LYS A 5
SHEET 3 A 8 PHE A 142 PHE A 145 -1 O GLU A 144 N ASN A 136
SHEET 4 A 8 ASN A 181 TYR A 185 -1 O GLY A 183 N MET A 143
SHEET 5 A 8 LEU A 165 GLY A 172 -1 N ALA A 171 O PHE A 182
SHEET 6 A 8 PRO A 157 LEU A 159 -1 N VAL A 158 O ILE A 166
SHEET 7 A 8 ARG A 112 GLY A 117 -1 N SER A 114 O LEU A 159
SHEET 8 A 8 MET A 128 SER A 139 -1 O GLY A 133 N ILE A 113
SHEET 1 B 7 ASN A 64 TYR A 65 0
SHEET 2 B 7 VAL A 51 ALA A 53 -1 N VAL A 51 O TYR A 65
SHEET 3 B 7 VAL A 18 PHE A 21 -1 N ALA A 20 O SER A 52
SHEET 4 B 7 GLY A 24 GLY A 30 -1 O GLY A 24 N PHE A 21
SHEET 5 B 7 THR A 33 THR A 36 -1 O VAL A 35 N VAL A 27
SHEET 6 B 7 ALA A 80 VAL A 84 -1 O VAL A 82 N ILE A 34
SHEET 7 B 7 VAL A 67 GLU A 72 -1 N VAL A 71 O ILE A 81
SHEET 1 C 8 ASN B 3 ILE B 7 0
SHEET 2 C 8 MET B 128 SER B 139 -1 O GLU B 130 N LYS B 5
SHEET 3 C 8 PHE B 142 PHE B 145 -1 O GLU B 144 N ASN B 136
SHEET 4 C 8 ASN B 181 TYR B 185 -1 O ASN B 181 N PHE B 145
SHEET 5 C 8 LEU B 165 GLY B 172 -1 N ALA B 171 O PHE B 182
SHEET 6 C 8 PRO B 157 LEU B 159 -1 N VAL B 158 O ILE B 166
SHEET 7 C 8 ARG B 112 GLY B 117 -1 N SER B 114 O LEU B 159
SHEET 8 C 8 MET B 128 SER B 139 -1 O SER B 131 N VAL B 115
SHEET 1 D 7 VAL B 18 PHE B 21 0
SHEET 2 D 7 GLY B 24 GLY B 30 -1 O GLY B 26 N VAL B 19
SHEET 3 D 7 THR B 33 THR B 36 -1 O THR B 33 N VAL B 29
SHEET 4 D 7 ALA B 80 VAL B 84 -1 O VAL B 82 N ILE B 34
SHEET 5 D 7 ASN B 64 GLU B 72 -1 N VAL B 71 O ILE B 81
SHEET 6 D 7 ARG B 50 ALA B 53 -1 N VAL B 51 O TYR B 65
SHEET 7 D 7 VAL B 18 PHE B 21 -1 N ALA B 20 O SER B 52
SHEET 1 E 8 VAL C 4 ILE C 7 0
SHEET 2 E 8 MET C 128 SER C 139 -1 O MET C 128 N ILE C 7
SHEET 3 E 8 PHE C 142 PHE C 145 -1 O PHE C 142 N SER C 139
SHEET 4 E 8 ASN C 181 TYR C 185 -1 O GLY C 183 N MET C 143
SHEET 5 E 8 LEU C 165 ALA C 171 -1 N TYR C 170 O PHE C 182
SHEET 6 E 8 PRO C 157 LEU C 159 -1 N VAL C 158 O ILE C 166
SHEET 7 E 8 ARG C 112 GLY C 117 -1 N SER C 114 O LEU C 159
SHEET 8 E 8 MET C 128 SER C 139 -1 O GLY C 133 N ILE C 113
SHEET 1 F 7 VAL C 18 PHE C 21 0
SHEET 2 F 7 GLY C 24 GLY C 30 -1 O GLY C 24 N PHE C 21
SHEET 3 F 7 THR C 33 THR C 36 -1 O THR C 33 N GLY C 30
SHEET 4 F 7 ALA C 80 VAL C 84 -1 O VAL C 82 N ILE C 34
SHEET 5 F 7 GLY C 63 GLU C 72 -1 N LYS C 68 O HIS C 83
SHEET 6 F 7 ARG C 50 ALA C 53 -1 N VAL C 51 O TYR C 65
SHEET 7 F 7 VAL C 18 PHE C 21 -1 N ALA C 20 O SER C 52
SHEET 1 G 8 VAL D 4 ILE D 7 0
SHEET 2 G 8 MET D 128 SER D 139 -1 O MET D 128 N ILE D 7
SHEET 3 G 8 PHE D 142 PHE D 145 -1 O PHE D 142 N SER D 139
SHEET 4 G 8 ASN D 181 TYR D 185 -1 O GLY D 183 N MET D 143
SHEET 5 G 8 LEU D 165 ALA D 171 -1 N ALA D 171 O PHE D 182
SHEET 6 G 8 PRO D 157 LEU D 159 -1 N VAL D 158 O ILE D 166
SHEET 7 G 8 ARG D 112 GLY D 117 -1 N SER D 114 O LEU D 159
SHEET 8 G 8 MET D 128 SER D 139 -1 O GLY D 133 N ILE D 113
SHEET 1 H 7 ASN D 64 TYR D 65 0
SHEET 2 H 7 VAL D 51 ALA D 53 -1 N VAL D 51 O TYR D 65
SHEET 3 H 7 VAL D 18 PHE D 21 -1 N ALA D 20 O SER D 52
SHEET 4 H 7 GLY D 24 GLY D 30 -1 O GLY D 24 N PHE D 21
SHEET 5 H 7 THR D 33 THR D 36 -1 O VAL D 35 N VAL D 27
SHEET 6 H 7 ALA D 80 VAL D 84 -1 O VAL D 82 N ILE D 34
SHEET 7 H 7 VAL D 67 GLU D 72 -1 N LYS D 68 O HIS D 83
LINK OG SER A 154 P13 I1S A 301 1555 1555 1.72
LINK OG SER B 154 P13 I1S B 301 1555 1555 1.69
LINK OG SER C 154 P13AI1S C 301 1555 1555 1.68
LINK OG SER C 154 P13BI1S C 301 1555 1555 1.70
LINK OG SER D 154 P13 I1S D 301 1555 1555 1.66
CISPEP 1 GLU A 13 PRO A 14 0 3.52
CISPEP 2 GLU B 13 PRO B 14 0 -1.53
CISPEP 3 GLU C 13 PRO C 14 0 -3.24
CISPEP 4 GLU D 13 PRO D 14 0 2.69
SITE 1 AC1 16 HIS A 39 ALA A 149 GLN A 150 PRO A 151
SITE 2 AC1 16 SER A 154 TYR A 170 ALA A 171 GLY A 172
SITE 3 AC1 16 SER A 173 GLY A 174 ASN A 181 HOH A 443
SITE 4 AC1 16 HOH A 516 HOH A 553 HOH A 598 LYS C 76
SITE 1 AC2 17 HIS B 39 ALA B 149 GLN B 150 PRO B 151
SITE 2 AC2 17 SER B 154 TYR B 170 ALA B 171 GLY B 172
SITE 3 AC2 17 GLY B 174 LYS B 175 HOH B 402 HOH B 411
SITE 4 AC2 17 HOH B 432 HOH B 473 LYS D 76 GLU D 77
SITE 5 AC2 17 HOH D 440
SITE 1 AC3 19 LYS A 76 GLU A 77 HOH A 456 HOH A 596
SITE 2 AC3 19 HIS C 39 ALA C 149 GLN C 150 PRO C 151
SITE 3 AC3 19 SER C 154 TYR C 170 ALA C 171 GLY C 172
SITE 4 AC3 19 GLY C 174 LYS C 175 SER C 178 HOH C 403
SITE 5 AC3 19 HOH C 456 HOH C 464 HOH C 498
SITE 1 AC4 14 LYS B 76 GLN D 150 PRO D 151 SER D 154
SITE 2 AC4 14 TYR D 170 ALA D 171 GLY D 172 GLY D 174
SITE 3 AC4 14 LYS D 175 HOH D 406 HOH D 411 HOH D 469
SITE 4 AC4 14 HOH D 506 HOH D 550
CRYST1 73.131 81.626 133.787 90.00 90.00 90.00 P 21 21 21 16
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 0.013674 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012251 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007475 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
