HEADER HYDROLASE 23-JUN-12 4AZ6
TITLE DIFFERENTIAL INHIBITION OF THE TANDEM GH20 CATALYTIC MODULES IN THE
TITLE 2 PNEUMOCOCCAL EXO-BETA-D-N-ACETYLGLUCOSAMINIDASE, STRH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-N-ACETYLHEXOSAMINIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC MODULE, RESIDUES 181-613;
COMPND 5 SYNONYM: GLYCOSIDE HYDROLASE 20;
COMPND 6 EC: 3.2.1.52;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.PLUVINAGE,K.A.STUBBS,D.J.VOCADLO,A.B.BORASTON
REVDAT 4 20-DEC-23 4AZ6 1 REMARK SHEET
REVDAT 3 13-NOV-13 4AZ6 1 JRNL
REVDAT 2 30-OCT-13 4AZ6 1 JRNL
REVDAT 1 10-JUL-13 4AZ6 0
JRNL AUTH B.PLUVINAGE,K.A.STUBBS,D.J.VOCADLO,A.B.BORASTON
JRNL TITL INHIBITION OF THE FAMILY 20 GLYCOSIDE HYDROLASE CATALYTIC
JRNL TITL 2 MODULES IN THE STREPTOCOCCUS PNEUMONIAE
JRNL TITL 3 EXO-BETA-D-N-ACETYLGLUCOSAMINIDASE, STRH.
JRNL REF ORG.BIOMOL.CHEM. V. 11 7907 2013
JRNL REFN ISSN 1477-0520
JRNL PMID 24132305
JRNL DOI 10.1039/C3OB41579A
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 88573
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) : 0.116
REMARK 3 R VALUE (WORKING SET) : 0.115
REMARK 3 FREE R VALUE : 0.140
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4692
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) : 1.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3779
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3402
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 652
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : -0.21000
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): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.045
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.022
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.168
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3915 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2636 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5333 ; 1.360 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6432 ; 0.894 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 512 ; 5.785 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 188 ;35.538 ;25.585
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 677 ;11.421 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;14.983 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 557 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4583 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 784 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 6550 ; 3.096 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 110 ;35.563 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6987 ; 8.460 ; 5.000
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 RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4AZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1290053030.
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 : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93267
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.360
REMARK 200 RESOLUTION RANGE LOW (A) : 28.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
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: PDB ENTRY 2YL6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 39.15000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.30000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.15000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.80000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.30000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.15000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.80000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.30000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.15000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.80000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.30000
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 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 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 A2393 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2394 LIES ON A SPECIAL POSITION.
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 HIS A 180 CG ND1 CD2 CE1 NE2
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 LYS A 389 CE NZ
REMARK 480 GLU A 503 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 A 2513 O HOH A 2514 1.94
REMARK 500 O HOH A 2140 O HOH A 2144 2.01
REMARK 500 O HOH A 2317 O HOH A 2557 2.03
REMARK 500 O HOH A 2139 O HOH A 2140 2.08
REMARK 500 O HOH A 2140 O HOH A 2141 2.09
REMARK 500 O HOH A 2140 O HOH A 2142 2.09
REMARK 500 O HOH A 2317 O HOH A 2558 2.12
REMARK 500 OE1 GLU A 206 O HOH A 2042 2.13
REMARK 500 O HOH A 2054 O HOH A 2618 2.13
REMARK 500 O HOH A 2221 O HOH A 2224 2.13
REMARK 500 O HOH A 2136 O HOH A 2140 2.14
REMARK 500 OD2 ASP A 259 O HOH A 2140 2.14
REMARK 500 O HOH A 2317 O HOH A 2319 2.15
REMARK 500 OD1 ASP A 259 O HOH A 2122 2.16
REMARK 500 O HOH A 2618 O HOH A 2619 2.17
REMARK 500 OD2 ASP A 400 O HOH A 2384 2.19
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 CE LYS A 561 O HOH A 2397 4565 1.90
REMARK 500 O HOH A 2223 O HOH A 2317 4565 1.98
REMARK 500 O HOH A 2161 O HOH A 2317 2565 2.09
REMARK 500 O HOH A 2227 O HOH A 2470 8455 2.16
REMARK 500 O HOH A 2112 O HOH A 2464 8455 2.19
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 A 503 CD GLU A 503 OE1 -0.161
REMARK 500 GLU A 503 CD GLU A 503 OE2 0.114
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 225 92.22 -166.22
REMARK 500 ASP A 226 -73.26 69.99
REMARK 500 TYR A 261 117.07 -160.17
REMARK 500 LYS A 350 -10.65 68.99
REMARK 500 LYS A 350 -13.66 70.35
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 A2322 DISTANCE = 6.00 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAN A 1614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P15 A 1618
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YL5 RELATED DB: PDB
REMARK 900 INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR
REMARK 900 INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
REMARK 900 RELATED ID: 2YL6 RELATED DB: PDB
REMARK 900 INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR
REMARK 900 INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
REMARK 900 RELATED ID: 2YL8 RELATED DB: PDB
REMARK 900 INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR
REMARK 900 INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
REMARK 900 RELATED ID: 2YL9 RELATED DB: PDB
REMARK 900 INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR
REMARK 900 INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
REMARK 900 RELATED ID: 2YLA RELATED DB: PDB
REMARK 900 INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR
REMARK 900 INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
REMARK 900 RELATED ID: 2YLL RELATED DB: PDB
REMARK 900 INHIBITION OF THE PNEUMOCOCCAL VIRULENCE FACTOR STRH AND MOLECULAR
REMARK 900 INSIGHTS INTO N-GLYCAN RECOGNITION AND HYDROLYSIS
REMARK 900 RELATED ID: 4AZ5 RELATED DB: PDB
REMARK 900 DIFFERENTIAL INHIBITION OF THE TANDEM GH20 CATALYTIC MODULES IN THE
REMARK 900 PNEUMOCOCCAL EXO-BETA-D-N- ACETYLGLUCOSAMINIDASE, STRH
REMARK 900 RELATED ID: 4AZ7 RELATED DB: PDB
REMARK 900 DIFFERENTIAL INHIBITION OF THE TANDEM GH20 CATALYTIC MODULES IN THE
REMARK 900 PNEUMOCOCCAL EXO-BETA-D-N- ACETYLGLUCOSAMINIDASE, STRH
DBREF 4AZ6 A 181 613 UNP P49610 STRH_STRPN 181 613
SEQADV 4AZ6 SER A 179 UNP P49610 EXPRESSION TAG
SEQADV 4AZ6 HIS A 180 UNP P49610 EXPRESSION TAG
SEQRES 1 A 435 SER HIS ASN GLU LYS LEU ALA LYS LYS LYS ILE VAL SER
SEQRES 2 A 435 ILE ASP ALA GLY ARG LYS TYR PHE SER PRO GLU GLN LEU
SEQRES 3 A 435 LYS GLU ILE ILE ASP LYS ALA LYS HIS TYR GLY TYR THR
SEQRES 4 A 435 ASP LEU HIS LEU LEU VAL GLY ASN ASP GLY LEU ARG PHE
SEQRES 5 A 435 MET LEU ASP ASP MET SER ILE THR ALA ASN GLY LYS THR
SEQRES 6 A 435 TYR ALA SER ASP ASP VAL LYS ARG ALA ILE GLU LYS GLY
SEQRES 7 A 435 THR ASN ASP TYR TYR ASN ASP PRO ASN GLY ASN HIS LEU
SEQRES 8 A 435 THR GLU SER GLN MET THR ASP LEU ILE ASN TYR ALA LYS
SEQRES 9 A 435 ASP LYS GLY ILE GLY LEU ILE PRO THR VAL ASN SER PRO
SEQRES 10 A 435 GLY HIS MET ASP ALA ILE LEU ASN ALA MET LYS GLU LEU
SEQRES 11 A 435 GLY ILE GLN ASN PRO ASN PHE SER TYR PHE GLY LYS LYS
SEQRES 12 A 435 SER ALA ARG THR VAL ASP LEU ASP ASN GLU GLN ALA VAL
SEQRES 13 A 435 ALA PHE THR LYS ALA LEU ILE ASP LYS TYR ALA ALA TYR
SEQRES 14 A 435 PHE ALA LYS LYS THR GLU ILE PHE ASN ILE GLY LEU ASP
SEQRES 15 A 435 GLU TYR ALA ASN ASP ALA THR ASP ALA LYS GLY TRP SER
SEQRES 16 A 435 VAL LEU GLN ALA ASP LYS TYR TYR PRO ASN GLU GLY TYR
SEQRES 17 A 435 PRO VAL LYS GLY TYR GLU LYS PHE ILE ALA TYR ALA ASN
SEQRES 18 A 435 ASP LEU ALA ARG ILE VAL LYS SER HIS GLY LEU LYS PRO
SEQRES 19 A 435 MET ALA PHE ASN ASP GLY ILE TYR TYR ASN SER ASP THR
SEQRES 20 A 435 SER PHE GLY SER PHE ASP LYS ASP ILE ILE VAL SER MET
SEQRES 21 A 435 TRP THR GLY GLY TRP GLY GLY TYR ASP VAL ALA SER SER
SEQRES 22 A 435 LYS LEU LEU ALA GLU LYS GLY HIS GLN ILE LEU ASN THR
SEQRES 23 A 435 ASN ASP ALA TRP TYR TYR VAL LEU GLY ARG ASN ALA ASP
SEQRES 24 A 435 GLY GLN GLY TRP TYR ASN LEU ASP GLN GLY LEU ASN GLY
SEQRES 25 A 435 ILE LYS ASN THR PRO ILE THR SER VAL PRO LYS THR GLU
SEQRES 26 A 435 GLY ALA ASP ILE PRO ILE ILE GLY GLY MET VAL ALA ALA
SEQRES 27 A 435 TRP ALA ASP THR PRO SER ALA ARG TYR SER PRO SER ARG
SEQRES 28 A 435 LEU PHE LYS LEU MET ARG HIS PHE ALA ASN ALA ASN ALA
SEQRES 29 A 435 GLU TYR PHE ALA ALA ASP TYR GLU SER ALA GLU GLN ALA
SEQRES 30 A 435 LEU ASN GLU VAL PRO LYS ASP LEU ASN ARG TYR THR ALA
SEQRES 31 A 435 GLU SER VAL THR ALA VAL LYS GLU ALA GLU LYS ALA ILE
SEQRES 32 A 435 ARG SER LEU ASP SER ASN LEU SER ARG ALA GLN GLN ASP
SEQRES 33 A 435 THR ILE ASP GLN ALA ILE ALA LYS LEU GLN GLU THR VAL
SEQRES 34 A 435 ASN ASN LEU THR LEU THR
HET OAN A1614 25
HET EDO A1615 4
HET EDO A1616 4
HET EDO A1617 4
HET P15 A1618 20
HETNAM OAN O-(2-ACETAMIDO-2-DEOXY D-GLUCOPYRANOSYLIDENE) AMINO-N-
HETNAM 2 OAN PHENYLCARBAMATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETSYN OAN PUGNAC
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 OAN C15 H19 N3 O7
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 P15 C13 H28 O7
FORMUL 7 HOH *652(H2 O)
HELIX 1 1 SER A 179 ALA A 185 1 7
HELIX 2 2 SER A 200 GLY A 215 1 16
HELIX 3 3 ALA A 245 TYR A 261 1 17
HELIX 4 4 GLU A 271 LYS A 284 1 14
HELIX 5 5 MET A 298 GLY A 309 1 12
HELIX 6 6 ASN A 330 ALA A 349 1 20
HELIX 7 7 LYS A 370 TYR A 381 1 12
HELIX 8 8 LYS A 389 HIS A 408 1 20
HELIX 9 9 TYR A 420 ASP A 424 5 5
HELIX 10 10 SER A 450 LYS A 457 1 8
HELIX 11 11 ASN A 465 TYR A 469 5 5
HELIX 12 12 ASN A 483 THR A 494 1 12
HELIX 13 13 SER A 526 ASN A 541 1 16
HELIX 14 14 TYR A 549 GLU A 558 1 10
HELIX 15 15 THR A 567 SER A 583 1 17
HELIX 16 16 GLN A 592 ASN A 609 1 18
SHEET 1 AA10 LYS A 187 ASP A 193 0
SHEET 2 AA10 GLY A 511 TRP A 517 1 O GLY A 512 N ILE A 189
SHEET 3 AA10 TYR A 470 VAL A 471 1 O TYR A 470 N TRP A 517
SHEET 4 AA10 ASP A 218 GLY A 224 0
SHEET 5 AA10 GLY A 287 SER A 294 0
SHEET 6 AA10 ILE A 354 GLY A 358 0
SHEET 7 AA10 LYS A 411 PHE A 415 0
SHEET 8 AA10 ILE A 435 MET A 438 0
SHEET 9 AA10 ILE A 461 ASN A 463 0
SHEET 10 AA10 LYS A 187 ASP A 193 1 O LYS A 187 N GLY A 512
SHEET 1 AB 2 PHE A 230 MET A 231 0
SHEET 2 AB 2 LEU A 269 THR A 270 1 O LEU A 269 N MET A 231
SHEET 1 AC 2 ILE A 237 ALA A 239 0
SHEET 2 AC 2 LYS A 242 TYR A 244 -1 O LYS A 242 N ALA A 239
SHEET 1 AD 2 ASN A 314 TYR A 317 0
SHEET 2 AD 2 LYS A 320 VAL A 326 -1 O LYS A 320 N TYR A 317
CISPEP 1 SER A 294 PRO A 295 0 -7.99
SITE 1 AC1 17 ARG A 196 ARG A 251 HIS A 297 ASP A 360
SITE 2 AC1 17 GLU A 361 TRP A 439 TRP A 443 TYR A 469
SITE 3 AC1 17 TRP A 481 TYR A 482 TRP A 517 ASP A 519
SITE 4 AC1 17 EDO A1615 EDO A1616 HOH A2059 HOH A2463
SITE 5 AC1 17 HOH A2648
SITE 1 AC2 7 HIS A 297 ARG A 324 GLU A 361 ASN A 364
SITE 2 AC2 7 OAN A1614 HOH A2019 HOH A2649
SITE 1 AC3 8 THR A 440 GLY A 442 TRP A 443 ASP A 466
SITE 2 AC3 8 OAN A1614 HOH A2454 HOH A2650 HOH A2651
SITE 1 AC4 4 GLN A 592 THR A 595 HOH A2003 HOH A2609
SITE 1 AC5 9 TYR A 317 LYS A 370 SER A 373 TYR A 381
SITE 2 AC5 9 GLU A 384 TYR A 386 HOH A2245 HOH A2349
SITE 3 AC5 9 HOH A2652
CRYST1 78.300 109.600 112.600 90.00 90.00 90.00 I 2 2 2 8
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 0.012771 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009124 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008881 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
