HEADER HYDROLASE 17-MAR-14 4CUA
TITLE UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
TITLE 2 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE, BGAA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 1463-1645;
COMPND 5 EC: 3.2.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 STRAIN: NCH18;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.SINGH,B.PLUVINAGE,M.A.HIGGINS,A.B.DALIA,M.FLYNN,A.R.LLOYD,
AUTHOR 2 J.N.WEISER,K.A.STUBBS,A.B.BORASTON,S.J.KING
REVDAT 2 24-SEP-14 4CUA 1 JRNL
REVDAT 1 20-AUG-14 4CUA 0
JRNL AUTH A.K.SINGH,B.PLUVINAGE,M.A.HIGGINS,A.B.DALIA,S.A.WOODIGA,
JRNL AUTH 2 M.FLYNN,A.R.LLOYD,J.N.WEISER,K.A.STUBBS,A.B.BORASTON,
JRNL AUTH 3 S.J.KING
JRNL TITL UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
JRNL TITL 2 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE, BGAA.
JRNL REF PLOS PATHOG. V. 10 04364 2014
JRNL REFN ISSN 1553-7366
JRNL PMID 25210925
JRNL DOI 10.1371/JOURNAL.PPAT.1004364
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.92
REMARK 3 NUMBER OF REFLECTIONS : 56805
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) : 0.16224
REMARK 3 R VALUE (WORKING SET) : 0.16085
REMARK 3 FREE R VALUE : 0.18893
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 3022
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) : 1.542
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.582
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4094
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.198
REMARK 3 BIN FREE R VALUE SET COUNT : 224
REMARK 3 BIN FREE R VALUE : 0.260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2874
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 702
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.427
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01
REMARK 3 B22 (A**2) : 0.01
REMARK 3 B33 (A**2) : -0.01
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.254
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3025 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2737 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4132 ; 1.873 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6316 ; 0.871 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 394 ; 7.177 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;34.432 ;25.338
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 443 ;10.197 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;12.423 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 435 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3637 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 722 ; 0.001 ; 0.020
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): 1522 ; 1.296 ; 1.325
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1521 ; 1.281 ; 1.324
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1934 ; 1.932 ; 1.982
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1503 ; 2.065 ; 1.517
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 4CUA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAR-14.
REMARK 100 THE PDBE ID CODE IS EBI-60050.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97874
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59949
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.54
REMARK 200 RESOLUTION RANGE LOW (A) : 36.33
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.6
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 16.5
REMARK 200 R MERGE FOR SHELL (I) : 0.40
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SHELX CDE
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 79.84500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.14500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.14500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 119.76750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.14500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.14500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.92250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.14500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.14500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 119.76750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.14500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.14500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.92250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.84500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A2273 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2299 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2300 LIES ON A SPECIAL POSITION.
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 GLN A 1463
REMARK 465 THR A 1464
REMARK 465 GLU A 1465
REMARK 465 GLN A 1644
REMARK 465 VAL A 1645
REMARK 465 GLN B 1463
REMARK 465 THR B 1464
REMARK 465 GLU B 1465
REMARK 465 GLN B 1644
REMARK 465 VAL B 1645
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 A1643 CG CD CE NZ
REMARK 470 LYS B1565 CG CD CE NZ
REMARK 470 LYS B1614 CG CD CE NZ
REMARK 470 LYS B1643 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN B 1506 CD OE1 NE2
REMARK 480 LYS B 1597 CE NZ
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 OD1B ASN A 1573 O HOH A 2269 2.01
REMARK 500 OD2A ASP A 1581 O HOH A 2283 2.01
REMARK 500 O HOH A 2040 O HOH A 2200 2.09
REMARK 500 O HOH A 2206 O HOH A 2207 2.19
REMARK 500 O HOH A 2312 O HOH A 2331 2.12
REMARK 500 O HOH A 2337 O HOH A 2338 2.17
REMARK 500 O HOH B 2036 O HOH B 2191 2.19
REMARK 500 O HOH B 2062 O HOH B 2294 2.19
REMARK 500 O HOH B 2083 O HOH B 2084 2.18
REMARK 500 O HOH B 2154 O HOH B 2163 1.92
REMARK 500 O HOH B 2165 O HOH A 2358 2.19
REMARK 500 O HOH B 2241 O HOH B 2242 1.97
REMARK 500 O HOH B 2263 O HOH B 2264 2.14
REMARK 500 O HOH B 2279 O HOH B 2294 2.00
REMARK 500 O HOH B 2304 O HOH B 2305 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 ND2B ASN A 1573 ND2B ASN A 1573 8555 2.01
REMARK 500 NE2 GLN A 1601 OE2B GLU B 1547 6555 2.15
REMARK 500 O HOH A 2269 O HOH A 2269 8555 1.93
REMARK 500 O HOH B 2036 O HOH B 2302 8665 2.15
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 GLU B1478 CD GLU B1478 OE2 -0.077
REMARK 500 LYS B1597 CD LYS B1597 CE -0.351
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 ASP A1472 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A1536 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B1486 CB - CG - OD1 ANGL. DEV. = 5.9 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 A1504 -158.78 -143.03
REMARK 500 LYS B1499 -0.44 71.93
REMARK 500 ASN B1504 -156.28 -142.56
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 A2089 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A2092 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH A2369 DISTANCE = 9.12 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2644 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1637 OE1
REMARK 620 2 ASN A1495 O 91.4
REMARK 620 3 ASP A1498 OD1 83.7 82.5
REMARK 620 4 LEU A1500 O 87.8 173.6 91.1
REMARK 620 5 ASN A1509 OD1 173.1 95.4 96.4 85.4
REMARK 620 6 THR A1636 O 88.4 82.2 162.6 104.1 93.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2644 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B1509 OD1
REMARK 620 2 THR B1636 O 93.6
REMARK 620 3 LEU B1500 O 83.3 102.2
REMARK 620 4 ASP B1498 OD1 96.6 162.4 93.2
REMARK 620 5 ASN B1495 O 94.0 83.0 174.2 82.0
REMARK 620 6 GLU B1637 OE1 172.6 88.7 89.3 83.1 93.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2644
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2644
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A2645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A2646
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A2647
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A2648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A2649
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2646
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2647
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2648
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A2650
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2649
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CU6 RELATED DB: PDB
REMARK 900 UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
REMARK 900 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE,
REMARK 900 BGAA
REMARK 900 RELATED ID: 4CU7 RELATED DB: PDB
REMARK 900 UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
REMARK 900 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE,
REMARK 900 BGAA
REMARK 900 RELATED ID: 4CU8 RELATED DB: PDB
REMARK 900 UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
REMARK 900 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE,
REMARK 900 BGAA
REMARK 900 RELATED ID: 4CU9 RELATED DB: PDB
REMARK 900 UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
REMARK 900 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE,
REMARK 900 BGAA
REMARK 900 RELATED ID: 4CUB RELATED DB: PDB
REMARK 900 UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
REMARK 900 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE,
REMARK 900 BGAA
REMARK 900 RELATED ID: 4CUC RELATED DB: PDB
REMARK 900 UNRAVELLING THE MULTIPLE FUNCTIONS OF THE ARCHITECTURALLY
REMARK 900 INTRICATE STREPTOCOCCUS PNEUMONIAE BETA-GALACTOSIDASE,
REMARK 900 BGAA.
DBREF 4CUA A 1463 1645 UNP Q8DQP4 Q8DQP4_STRR6 1463 1645
DBREF 4CUA B 1463 1645 UNP Q8DQP4 Q8DQP4_STRR6 1463 1645
SEQRES 1 A 183 GLN THR GLU GLN GLY ALA ASN ILE SER ASP GLN TRP THR
SEQRES 2 A 183 GLY SER GLU LEU PRO LEU ALA PHE ALA SER ASP SER ASN
SEQRES 3 A 183 PRO SER ASP PRO VAL SER ASN VAL ASN ASP LYS LEU ILE
SEQRES 4 A 183 SER TYR ASN ASN GLN PRO ALA ASN ARG TRP THR ASN TRP
SEQRES 5 A 183 ASN ARG SER ASN PRO GLU ALA SER VAL GLY VAL LEU PHE
SEQRES 6 A 183 GLY ASP SER GLY ILE LEU SER LYS ARG SER VAL ASP ASN
SEQRES 7 A 183 LEU SER VAL GLY PHE HIS GLU ASP HIS GLY VAL GLY ALA
SEQRES 8 A 183 PRO LYS SER TYR VAL ILE GLU TYR TYR VAL GLY LYS THR
SEQRES 9 A 183 VAL PRO THR ALA PRO LYS ASN PRO SER PHE VAL GLY ASN
SEQRES 10 A 183 GLU ASP HIS VAL PHE ASN ASP SER ALA ASN TRP LYS PRO
SEQRES 11 A 183 VAL THR ASN LEU LYS ALA PRO ALA GLN LEU LYS ALA GLY
SEQRES 12 A 183 GLU MSE ASN HIS PHE SER PHE ASP LYS VAL GLU THR TYR
SEQRES 13 A 183 ALA ILE ARG ILE ARG MSE VAL LYS ALA ASP ASN LYS ARG
SEQRES 14 A 183 GLY THR SER ILE THR GLU VAL GLN ILE PHE ALA LYS GLN
SEQRES 15 A 183 VAL
SEQRES 1 B 183 GLN THR GLU GLN GLY ALA ASN ILE SER ASP GLN TRP THR
SEQRES 2 B 183 GLY SER GLU LEU PRO LEU ALA PHE ALA SER ASP SER ASN
SEQRES 3 B 183 PRO SER ASP PRO VAL SER ASN VAL ASN ASP LYS LEU ILE
SEQRES 4 B 183 SER TYR ASN ASN GLN PRO ALA ASN ARG TRP THR ASN TRP
SEQRES 5 B 183 ASN ARG SER ASN PRO GLU ALA SER VAL GLY VAL LEU PHE
SEQRES 6 B 183 GLY ASP SER GLY ILE LEU SER LYS ARG SER VAL ASP ASN
SEQRES 7 B 183 LEU SER VAL GLY PHE HIS GLU ASP HIS GLY VAL GLY ALA
SEQRES 8 B 183 PRO LYS SER TYR VAL ILE GLU TYR TYR VAL GLY LYS THR
SEQRES 9 B 183 VAL PRO THR ALA PRO LYS ASN PRO SER PHE VAL GLY ASN
SEQRES 10 B 183 GLU ASP HIS VAL PHE ASN ASP SER ALA ASN TRP LYS PRO
SEQRES 11 B 183 VAL THR ASN LEU LYS ALA PRO ALA GLN LEU LYS ALA GLY
SEQRES 12 B 183 GLU MSE ASN HIS PHE SER PHE ASP LYS VAL GLU THR TYR
SEQRES 13 B 183 ALA ILE ARG ILE ARG MSE VAL LYS ALA ASP ASN LYS ARG
SEQRES 14 B 183 GLY THR SER ILE THR GLU VAL GLN ILE PHE ALA LYS GLN
SEQRES 15 B 183 VAL
MODRES 4CUA MSE A 1607 MET SELENOMETHIONINE
MODRES 4CUA MSE A 1624 MET SELENOMETHIONINE
MODRES 4CUA MSE B 1607 MET SELENOMETHIONINE
MODRES 4CUA MSE B 1624 MET SELENOMETHIONINE
HET MSE A1607 8
HET MSE A1624 8
HET MSE B1607 8
HET MSE B1624 8
HET CA B2644 1
HET CA A2644 1
HET EDO A2645 4
HET EDO B2645 4
HET EDO A2646 4
HET EDO A2647 4
HET EDO A2648 4
HET EDO A2649 4
HET EDO B2646 4
HET EDO B2647 4
HET EDO B2648 4
HET EDO A2650 4
HET EDO B2649 4
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MSE 4(C5 H11 N O2 SE)
FORMUL 4 EDO 11(C2 H6 O2)
FORMUL 5 CA 2(CA 2+)
FORMUL 6 HOH *702(H2 O)
HELIX 1 1 PRO A 1492 ASP A 1498 5 7
HELIX 2 2 ASN A 1573 GLU A 1580 5 8
HELIX 3 3 HIS A 1582 ASP A 1586 5 5
HELIX 4 4 ASP A 1586 ALA A 1588 5 3
HELIX 5 5 PRO B 1492 ASP B 1498 5 7
HELIX 6 6 ASN B 1573 GLU B 1580 5 8
HELIX 7 7 HIS B 1582 ASP B 1586 5 5
HELIX 8 8 ASP B 1586 ALA B 1588 5 3
SHEET 1 AA 5 LEU A1481 ALA A1484 0
SHEET 2 AA 5 GLU A1520 LEU A1526 -1 O GLY A1524 N PHE A1483
SHEET 3 AA 5 ALA A1619 VAL A1625 -1 O ILE A1620 N VAL A1525
SHEET 4 AA 5 SER A1556 TYR A1562 -1 O SER A1556 N VAL A1625
SHEET 5 AA 5 TRP A1590 PRO A1592 -1 O LYS A1591 N TYR A1561
SHEET 1 AB 4 TRP A1511 THR A1512 0
SHEET 2 AB 4 SER A1634 GLN A1639 -1 O ILE A1635 N TRP A1511
SHEET 3 AB 4 ARG A1536 PHE A1545 -1 O SER A1542 N GLN A1639
SHEET 4 AB 4 MSE A1607 THR A1617 -1 O ASN A1608 N VAL A1543
SHEET 1 AC 2 GLY A1528 ASP A1529 0
SHEET 2 AC 2 ILE A1532 LEU A1533 -1 O ILE A1532 N ASP A1529
SHEET 1 BA 2 ALA B1468 ASN B1469 0
SHEET 2 BA 2 PHE B1641 ALA B1642 -1 O ALA B1642 N ALA B1468
SHEET 1 BB 5 LEU B1481 ALA B1484 0
SHEET 2 BB 5 GLU B1520 LEU B1526 -1 O GLY B1524 N PHE B1483
SHEET 3 BB 5 ALA B1619 LYS B1626 -1 O ILE B1620 N VAL B1525
SHEET 4 BB 5 PRO B1554 TYR B1562 -1 N LYS B1555 O VAL B1625
SHEET 5 BB 5 TRP B1590 PRO B1592 -1 O LYS B1591 N TYR B1561
SHEET 1 BC 2 TRP B1511 THR B1512 0
SHEET 2 BC 2 GLY B1632 GLN B1639 -1 O ILE B1635 N TRP B1511
SHEET 1 BD 2 VAL B1551 GLY B1552 0
SHEET 2 BD 2 GLY B1632 GLN B1639 -1 O GLY B1632 N GLY B1552
SHEET 1 BE 4 MSE B1607 THR B1617 0
SHEET 2 BE 4 ARG B1536 PHE B1545 -1 O ARG B1536 N THR B1617
SHEET 3 BE 4 GLY B1632 GLN B1639 -1 N THR B1636 O GLY B1544
SHEET 4 BE 4 VAL B1551 GLY B1552 -1 O GLY B1552 N SER B1634
SHEET 1 BF 4 MSE B1607 THR B1617 0
SHEET 2 BF 4 ARG B1536 PHE B1545 -1 O ARG B1536 N THR B1617
SHEET 3 BF 4 GLY B1632 GLN B1639 -1 N THR B1636 O GLY B1544
SHEET 4 BF 4 TRP B1511 THR B1512 -1 O TRP B1511 N ILE B1635
SHEET 1 BG 2 GLY B1528 ASP B1529 0
SHEET 2 BG 2 ILE B1532 LEU B1533 -1 O ILE B1532 N ASP B1529
LINK C GLU A1606 N MSE A1607 1555 1555 1.33
LINK C MSE A1607 N ASN A1608 1555 1555 1.32
LINK C ARG A1623 N MSE A1624 1555 1555 1.33
LINK C MSE A1624 N VAL A1625 1555 1555 1.32
LINK CA CA A2644 OE1 GLU A1637 1555 1555 2.29
LINK CA CA A2644 O ASN A1495 1555 1555 2.27
LINK CA CA A2644 OD1 ASP A1498 1555 1555 2.39
LINK CA CA A2644 O THR A1636 1555 1555 2.35
LINK CA CA A2644 OD1 ASN A1509 1555 1555 2.28
LINK CA CA A2644 O LEU A1500 1555 1555 2.29
LINK C GLU B1606 N MSE B1607 1555 1555 1.33
LINK C MSE B1607 N ASN B1608 1555 1555 1.32
LINK C ARG B1623 N MSE B1624 1555 1555 1.34
LINK C MSE B1624 N VAL B1625 1555 1555 1.33
LINK CA CA B2644 O THR B1636 1555 1555 2.35
LINK CA CA B2644 O LEU B1500 1555 1555 2.27
LINK CA CA B2644 OD1 ASP B1498 1555 1555 2.43
LINK CA CA B2644 O ASN B1495 1555 1555 2.24
LINK CA CA B2644 OE1 GLU B1637 1555 1555 2.24
LINK CA CA B2644 OD1 ASN B1509 1555 1555 2.34
CISPEP 1 LEU A 1479 PRO A 1480 0 5.10
CISPEP 2 GLN A 1506 PRO A 1507 0 5.95
CISPEP 3 LEU B 1479 PRO B 1480 0 4.43
CISPEP 4 GLN B 1506 PRO B 1507 0 3.65
SITE 1 AC1 6 ASN B1495 ASP B1498 LEU B1500 ASN B1509
SITE 2 AC1 6 THR B1636 GLU B1637
SITE 1 AC2 6 ASN A1495 ASP A1498 LEU A1500 ASN A1509
SITE 2 AC2 6 THR A1636 GLU A1637
SITE 1 AC3 6 ASP A1491 ARG A1510 THR A1512 ASP A1548
SITE 2 AC3 6 HOH A2172 HOH A2363
SITE 1 AC4 5 ASP B1491 ARG B1510 THR B1512 ASP B1548
SITE 2 AC4 5 HOH B2329
SITE 1 AC5 8 PHE A1483 SER A1485 SER A1522 VAL A1577
SITE 2 AC5 8 GLY A1578 PHE A1584 ASN A1585 ARG A1621
SITE 1 AC6 8 SER A1490 ASP A1491 PRO A1492 ASN A1495
SITE 2 AC6 8 ALA A1508 ASN A1509 ARG A1510 HOH A2364
SITE 1 AC7 9 GLN A1473 SER A1477 GLU A1478 PRO A1480
SITE 2 AC7 9 HOH A2110 HOH A2119 HOH A2121 HOH A2365
SITE 3 AC7 9 HOH A2366
SITE 1 AC8 7 THR A1566 VAL A1567 THR A1569 HIS A1582
SITE 2 AC8 7 VAL A1583 HOH A2287 HOH A2367
SITE 1 AC9 7 SER B1490 ASP B1491 PRO B1492 ASN B1495
SITE 2 AC9 7 ALA B1508 ASN B1509 ARG B1510
SITE 1 BC1 8 SER B1485 GLU B1520 ALA B1521 SER B1522
SITE 2 BC1 8 ARG B1621 ARG B1623 HOH B2170 HOH B2309
SITE 1 BC2 5 MSE A1607 HIS A1609 HOH A2329 ASN B1573
SITE 2 BC2 5 ASN B1579
SITE 1 BC3 4 ARG A1536 SER A1537 HOH A2209 HOH A2368
SITE 1 BC4 3 SER B1556 TYR B1557 HOH B2331
CRYST1 70.290 70.290 159.690 90.00 90.00 90.00 P 43 21 2 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 0.014227 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006262 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
