HEADER HYDROLASE 13-JUN-08 2VW2
TITLE CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS
TITLE 2 PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NANB SIALIDASE, NEURAMINIDASE B;
COMPND 5 EC: 3.2.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 STRAIN: TIGR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE, SIALIDASE, GLYCOSIDASE, DRUG DESIGN,
KEYWDS 2 NEURAMINIDASE, VIRULENCE FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR G.XU,J.A.POTTER,R.J.M.RUSSELL,M.R.OGGIONI,P.W.ANDREW,
AUTHOR 2 G.L.TAYLOR
REVDAT 3 24-FEB-09 2VW2 1 VERSN
REVDAT 2 18-NOV-08 2VW2 1 SOURCE JRNL REMARK
REVDAT 1 24-JUN-08 2VW2 0
JRNL AUTH G.XU,J.A.POTTER,R.J.M.RUSSELL,M.R.OGGIONI,
JRNL AUTH 2 P.W.ANDREW,G.L.TAYLOR
JRNL TITL CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
JRNL TITL 2 STREPTOCOCCUS PNEUMONIAE
JRNL REF J.MOL.BIOL. V. 384 436 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18835278
JRNL DOI 10.1016/J.JMB.2008.09.032
REMARK 2
REMARK 2 RESOLUTION. 1.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 67.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 71846
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3758
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) : 3421
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 194
REMARK 3 BIN FREE R VALUE : 0.4240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5189
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 797
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.50000
REMARK 3 B22 (A**2) : -0.84000
REMARK 3 B33 (A**2) : 1.34000
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): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.719
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5329 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7204 ; 1.099 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 657 ; 6.364 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;36.022 ;25.020
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 922 ;12.310 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;11.128 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 785 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4020 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2492 ; 0.183 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3618 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 727 ; 0.122 ; 0.200
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): 31 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.107 ; 0.200
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): 3370 ; 0.463 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5266 ; 0.796 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2263 ; 1.106 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1938 ; 1.742 ; 4.500
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2VW2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-08.
REMARK 100 THE PDBE ID CODE IS EBI-36565.
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 : 9.5
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 MICROMAX-007 HF
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 : CCD (SATURN 944)
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75667
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.70
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 3
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.90
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) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3
REMARK 200 R MERGE FOR SHELL (I) : 0.36
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1SLI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.15M NACL, 0.1M
REMARK 280 CHES PH 9.5
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 38.32100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.34200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.32100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.34200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: PQS
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 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 MET A 1
REMARK 465 ASN A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 TYR A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 LEU A 10
REMARK 465 GLY A 11
REMARK 465 ILE A 12
REMARK 465 SER A 13
REMARK 465 VAL A 14
REMARK 465 VAL A 15
REMARK 465 GLY A 16
REMARK 465 ILE A 17
REMARK 465 SER A 18
REMARK 465 LEU A 19
REMARK 465 LEU A 20
REMARK 465 MET A 21
REMARK 465 GLY A 22
REMARK 465 VAL A 23
REMARK 465 PRO A 24
REMARK 465 THR A 25
REMARK 465 LEU A 26
REMARK 465 ILE A 27
REMARK 465 HIS A 28
REMARK 465 ALA A 29
REMARK 465 ASN A 30
REMARK 465 GLU A 31
REMARK 465 LEU A 32
REMARK 465 ASN A 33
REMARK 465 TYR A 34
REMARK 465 GLY A 35
REMARK 465 GLN A 36
REMARK 465 LEU A 37
REMARK 465 SER A 38
REMARK 465 LYS A 697
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 C1 GOL A 1699 - O HOH A 2797 1.95
REMARK 500 O1 GOL A 1699 - O HOH A 2797 2.02
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 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 SER A 47 59.46 37.07
REMARK 500 ASN A 51 60.00 -115.94
REMARK 500 ALA A 78 89.71 -158.57
REMARK 500 ALA A 190 171.65 176.27
REMARK 500 GLN A 240 16.01 59.05
REMARK 500 ILE A 246 63.38 64.70
REMARK 500 SER A 273 -171.23 -173.23
REMARK 500 ASP A 327 90.78 63.58
REMARK 500 ASP A 633 10.20 -143.21
REMARK 500 TYR A 651 112.89 -161.59
REMARK 500 ALA A 652 -120.89 -116.39
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 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1699
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VW0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900 STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2VW1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900 STREPTOCOCCUS PNEUMONIAE
DBREF 2VW2 A 1 697 UNP Q54727 NANB_STRPN 1 697
SEQRES 1 A 697 MET ASN LYS ARG GLY LEU TYR SER LYS LEU GLY ILE SER
SEQRES 2 A 697 VAL VAL GLY ILE SER LEU LEU MET GLY VAL PRO THR LEU
SEQRES 3 A 697 ILE HIS ALA ASN GLU LEU ASN TYR GLY GLN LEU SER ILE
SEQRES 4 A 697 SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN ASN
SEQRES 5 A 697 LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS LEU
SEQRES 6 A 697 SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS ALA
SEQRES 7 A 697 ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU SER
SEQRES 8 A 697 ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER ILE
SEQRES 9 A 697 PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE ARG
SEQRES 10 A 697 ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG PRO
SEQRES 11 A 697 ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL GLU
SEQRES 12 A 697 ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS THR
SEQRES 13 A 697 TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER GLU
SEQRES 14 A 697 THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN GLY
SEQRES 15 A 697 ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU GLY
SEQRES 16 A 697 LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU ILE
SEQRES 17 A 697 SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL SER
SEQRES 18 A 697 THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE GLN
SEQRES 19 A 697 SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE PRO
SEQRES 20 A 697 THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER SER
SEQRES 21 A 697 ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS SER
SEQRES 22 A 697 LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN GLY
SEQRES 23 A 697 LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE ASN
SEQRES 24 A 697 ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP ASN
SEQRES 25 A 697 LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER PHE
SEQRES 26 A 697 ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY LYS
SEQRES 27 A 697 THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE GLY
SEQRES 28 A 697 ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS GLU
SEQRES 29 A 697 ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN GLY
SEQRES 30 A 697 ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY VAL
SEQRES 31 A 697 VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR THR
SEQRES 32 A 697 ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS SER
SEQRES 33 A 697 LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER GLY
SEQRES 34 A 697 SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO MET
SEQRES 35 A 697 ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR PRO
SEQRES 36 A 697 THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG GLY
SEQRES 37 A 697 GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE LEU
SEQRES 38 A 697 GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY GLN
SEQRES 39 A 697 GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE ALA
SEQRES 40 A 697 THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER ASP
SEQRES 41 A 697 ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER ILE
SEQRES 42 A 697 PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL GLU
SEQRES 43 A 697 LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR THR
SEQRES 44 A 697 THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER GLY
SEQRES 45 A 697 GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE GLN
SEQRES 46 A 697 GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS TYR
SEQRES 47 A 697 SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU SER
SEQRES 48 A 697 THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN LEU
SEQRES 49 A 697 VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE ASP
SEQRES 50 A 697 TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER TYR GLY
SEQRES 51 A 697 TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS HIS
SEQRES 52 A 697 ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER ARG
SEQRES 53 A 697 ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE ASP
SEQRES 54 A 697 LEU GLU ILE ASN ASP LEU THR LYS
HET NHE A1000 13
HET NHE A1001 13
HET GOL A1699 6
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETNAM GOL GLYCEROL
FORMUL 2 NHE 2(C8 H17 N O3 S)
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *797(H2 O1)
HELIX 1 1 ILE A 57 LEU A 62 1 6
HELIX 2 2 ASP A 63 LEU A 65 5 3
HELIX 3 3 SER A 216 SER A 221 1 6
HELIX 4 4 GLU A 691 THR A 696 1 6
SHEET 1 AA 6 PHE A 43 ASN A 51 0
SHEET 2 AA 6 LYS A 202 PHE A 211 -1 O GLY A 203 N LEU A 50
SHEET 3 AA 6 GLN A 70 LYS A 77 -1 O THR A 71 N PHE A 211
SHEET 4 AA 6 ASN A 144 ASP A 151 -1 O ASN A 144 N PHE A 76
SHEET 5 AA 6 THR A 156 VAL A 161 -1 O THR A 156 N ASP A 151
SHEET 6 AA 6 ILE A 164 THR A 170 -1 O ILE A 164 N VAL A 161
SHEET 1 AB 6 ILE A 55 ASP A 56 0
SHEET 2 AB 6 LYS A 185 LEU A 188 -1 O LEU A 188 N ILE A 55
SHEET 3 AB 6 LEU A 84 SER A 91 -1 O GLY A 89 N THR A 187
SHEET 4 AB 6 TYR A 101 ARG A 107 -1 O PHE A 102 N LEU A 90
SHEET 5 AB 6 ILE A 112 ASP A 118 -1 O GLY A 113 N PHE A 105
SHEET 6 AB 6 ILE A 123 ARG A 129 -1 O ILE A 123 N ASP A 118
SHEET 1 AC 2 LYS A 136 HIS A 137 0
SHEET 2 AC 2 GLN A 140 ALA A 141 -1 O GLN A 140 N HIS A 137
SHEET 1 AD 2 VAL A 191 ARG A 193 0
SHEET 2 AD 2 LYS A 196 HIS A 198 -1 O LYS A 196 N ARG A 193
SHEET 1 AE 3 TYR A 243 ARG A 245 0
SHEET 2 AE 3 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 AE 3 TYR A 250 THR A 251 -1 O TYR A 250 N LEU A 258
SHEET 1 AF 4 TYR A 243 ARG A 245 0
SHEET 2 AF 4 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 AF 4 ILE A 275 SER A 282 -1 O ASN A 276 N ALA A 263
SHEET 4 AF 4 ILE A 293 MET A 296 -1 O ILE A 293 N THR A 279
SHEET 1 AG 5 LYS A 475 LEU A 476 0
SHEET 2 AG 5 TYR A 458 SER A 464 -1 O MET A 461 N LYS A 475
SHEET 3 AG 5 THR A 339 MET A 346 -1 O THR A 339 N SER A 464
SHEET 4 AG 5 SER A 324 GLU A 332 -1 O SER A 324 N MET A 346
SHEET 5 AG 5 GLY A 493 GLN A 494 1 O GLY A 493 N ILE A 330
SHEET 1 AH 7 PHE A 362 ILE A 365 0
SHEET 2 AH 7 HIS A 368 LYS A 375 -1 O HIS A 368 N ILE A 365
SHEET 3 AH 7 TYR A 383 VAL A 385 -1 O TYR A 383 N LEU A 373
SHEET 4 AH 7 VAL A 390 ASN A 393 -1 O TYR A 392 N THR A 384
SHEET 5 AH 7 LYS A 398 ILE A 404 -1 O LYS A 398 N ASN A 393
SHEET 6 AH 7 VAL A 410 GLU A 412 -1 O LEU A 411 N THR A 403
SHEET 7 AH 7 LYS A 415 SER A 416 -1 O LYS A 415 N GLU A 412
SHEET 1 AI 3 PHE A 362 ILE A 365 0
SHEET 2 AI 3 HIS A 368 LYS A 375 -1 O HIS A 368 N ILE A 365
SHEET 3 AI 3 PHE A 451 LYS A 452 -1 O LYS A 452 N LYS A 374
SHEET 1 AJ 2 THR A 418 ASP A 425 0
SHEET 2 AJ 2 ARG A 432 PRO A 441 -1 O ARG A 432 N ASP A 425
SHEET 1 AK 3 TYR A 489 LEU A 490 0
SHEET 2 AK 3 LEU A 504 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 AK 3 LEU A 496 ALA A 497 -1 O LEU A 496 N ILE A 505
SHEET 1 AL 4 TYR A 489 LEU A 490 0
SHEET 2 AL 4 LEU A 504 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 AL 4 GLU A 513 SER A 519 -1 O GLU A 513 N THR A 510
SHEET 4 AL 4 LYS A 527 SER A 532 -1 O LYS A 527 N ILE A 518
SHEET 1 AM 4 ALA A 542 ARG A 548 0
SHEET 2 AM 4 VAL A 551 PHE A 556 -1 O VAL A 551 N LEU A 547
SHEET 3 AM 4 ALA A 564 SER A 568 -1 O ALA A 564 N PHE A 556
SHEET 4 AM 4 SER A 579 TYR A 580 -1 O SER A 579 N TYR A 565
SHEET 1 AN 4 SER A 594 LYS A 597 0
SHEET 2 AN 4 ALA A 607 PRO A 613 -1 O ILE A 609 N ILE A 596
SHEET 3 AN 4 GLY A 622 VAL A 629 -1 O GLN A 623 N THR A 612
SHEET 4 AN 4 ILE A 636 ASP A 643 -1 O ASP A 637 N LEU A 628
SHEET 1 AO 3 SER A 654 GLU A 658 0
SHEET 2 AO 3 ILE A 664 GLU A 669 -1 O GLY A 665 N THR A 657
SHEET 3 AO 3 VAL A 685 LEU A 690 -1 O GLN A 686 N PHE A 668
CISPEP 1 SER A 271 LYS A 272 0 2.69
SITE 1 AC1 13 ARG A 245 ASP A 270 ILE A 326 ASP A 327
SITE 2 AC1 13 ASN A 352 TYR A 489 TYR A 509 ARG A 557
SITE 3 AC1 13 ARG A 619 TYR A 653 TRP A 674 HOH A2413
SITE 4 AC1 13 HOH A2792
SITE 1 AC2 9 ASN A 312 LYS A 334 ALA A 497 LYS A 499
SITE 2 AC2 9 GLU A 658 GOL A1699 HOH A2793 HOH A2794
SITE 3 AC2 9 HOH A2796
SITE 1 AC3 7 TYR A 250 THR A 251 GLN A 494 THR A 657
SITE 2 AC3 7 NHE A1001 HOH A2583 HOH A2797
CRYST1 76.642 82.684 116.700 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013048 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012094 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008569 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
