HEADER CARBOHYDRATE-BINDING PROTEIN 15-AUG-06 2J1T
TITLE STRUCTURE OF A STREPTOCOCCUS PNEUMONIAE FUCOSE BINDING MODULE IN
TITLE 2 COMPLEX WITH THE LEWIS Y ANTIGEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUCOLECTIN-RELATED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FUCOSE BINDING MODULE, RESIDUES 601-745;
COMPND 5 SYNONYM: FUCOSE BINDING MODULE;
COMPND 6 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
KEYWDS CARBOHYDRATE-BINDING PROTEIN, CARBOHYDRATE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.BORASTON,D.WANG,R.D.BURKE
REVDAT 5 29-JUL-20 2J1T 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 24-FEB-09 2J1T 1 VERSN
REVDAT 3 15-NOV-06 2J1T 1 JRNL
REVDAT 2 27-SEP-06 2J1T 1 JRNL
REVDAT 1 06-SEP-06 2J1T 0
JRNL AUTH A.B.BORASTON,D.WANG,R.D.BURKE
JRNL TITL BLOOD GROUP ANTIGEN RECOGNITION BY A STREPTOCOCCUS
JRNL TITL 2 PNEUMONIAE VIRULENCE FACTOR
JRNL REF J.BIOL.CHEM. V. 281 35263 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16987809
JRNL DOI 10.1074/JBC.M607620200
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 32433
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1687
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2152
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 447
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : 0.11000
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): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.839
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2248 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1966 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3051 ; 1.685 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4585 ; 0.901 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 276 ; 6.385 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 349 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2491 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 437 ; 0.012 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 430 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2416 ; 0.258 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1332 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 277 ; 0.175 ; 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): 9 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.308 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 40 ; 0.207 ; 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): 1359 ; 1.374 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2196 ; 2.008 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 889 ; 2.979 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 852 ; 4.442 ; 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 : BABINET MODEL WITH 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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2J1T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 113.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34122
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 28.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 21.85350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.44450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.97150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.44450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.85350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.97150
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
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 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 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 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 ALA A 5
REMARK 465 SER A 6
REMARK 465 THR A 7
REMARK 465 PRO A 8
REMARK 465 ASP A 9
REMARK 465 LYS A 10
REMARK 465 PHE A 11
REMARK 465 ASN A 12
REMARK 465 ASP A 13
REMARK 465 GLU A 150
REMARK 465 SER A 151
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 ALA B 5
REMARK 465 SER B 6
REMARK 465 THR B 7
REMARK 465 PRO B 8
REMARK 465 ASP B 9
REMARK 465 LYS B 10
REMARK 465 PHE B 11
REMARK 465 ASN B 12
REMARK 465 ASP B 13
REMARK 465 GLY B 14
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 SER B 151 CA C O CB OG
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 OD1 ASN B 110 O HOH B 2175 2.17
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 VAL A 104 CB VAL A 104 CG2 -0.133
REMARK 500 GLU B 150 CD GLU B 150 OE1 0.066
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 A 93 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 98 CB - CG - OD1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ASP B 120 CB - CG - OD2 ANGL. DEV. = 7.9 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 HIS A 54 119.89 -165.58
REMARK 500 LYS A 68 -29.55 81.77
REMARK 500 GLU A 123 13.27 81.78
REMARK 500 GLU A 144 144.05 -170.30
REMARK 500 LYS B 68 -20.19 82.00
REMARK 500 GLU B 144 146.81 -177.00
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 A2023 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B2016 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B2018 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH B2028 DISTANCE = 7.14 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 A1154 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 37 O
REMARK 620 2 ASP A 40 OD1 77.9
REMARK 620 3 ASN A 42 O 164.2 91.3
REMARK 620 4 SER A 51 O 73.5 121.0 122.2
REMARK 620 5 SER A 51 OG 130.9 104.2 62.8 63.5
REMARK 620 6 SER A 51 OG 101.1 66.2 84.7 70.2 43.4
REMARK 620 7 ALA A 143 O 97.4 160.5 89.0 74.5 93.2 133.2
REMARK 620 8 GLU A 144 OE1 87.1 76.3 79.0 149.1 141.8 138.6 84.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 37 O
REMARK 620 2 ASP B 40 OD1 76.7
REMARK 620 3 ASN B 42 O 160.7 87.7
REMARK 620 4 SER B 51 O 76.7 124.7 122.1
REMARK 620 5 SER B 51 OG 113.4 79.1 73.8 68.7
REMARK 620 6 ALA B 143 O 98.5 159.2 92.1 72.4 120.8
REMARK 620 7 GLU B 144 OE1 82.0 74.6 83.0 145.7 145.4 84.7
REMARK 620 N 1 2 3 4 5 6
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2J1R RELATED DB: PDB
REMARK 900 STRUCTURE OF A STREPTOCOCCUS PNEUMONIAE FUCOSE BINDING MODULE
REMARK 900 RELATED ID: 2J1S RELATED DB: PDB
REMARK 900 STRUCTURE OF A STREPTOCOCCUS PNEUMONIAE FUCOSE BINDING MODULE IN
REMARK 900 COMPLEX WITH FUCOSE
REMARK 900 RELATED ID: 2J1U RELATED DB: PDB
REMARK 900 STRUCTURE OF A STREPTOCOCCUS PNEUMONIAE FUCOSE BINDING MODULE IN
REMARK 900 COMPLEX WITH THE BLOOD GROUP A-TETRASACCHARIDE
REMARK 900 RELATED ID: 2J1V RELATED DB: PDB
REMARK 900 STRUCTURE OF A STREPTOCOCCUS PNEUMONIAE FUCOSE BINDING MODULE IN
REMARK 900 COMPLEX WITH THE BLOOD GROUP H-TRISACCHARIDE
REMARK 900 RELATED ID: 2J22 RELATED DB: PDB
REMARK 900 STRUCTURE OF A STREPTOCOCCUS PNEUMONIAE FUCOSE BINDING MODULE, SPX-3
DBREF 2J1T A 1 6 PDB 2J1T 2J1T 1 6
DBREF 2J1T A 7 151 UNP Q97N96 Q97N96_STRPN 601 745
DBREF 2J1T B 1 6 PDB 2J1T 2J1T 1 6
DBREF 2J1T B 7 151 UNP Q97N96 Q97N96_STRPN 601 745
SEQRES 1 A 151 GLY SER HIS MET ALA SER THR PRO ASP LYS PHE ASN ASP
SEQRES 2 A 151 GLY ASN LEU ASN ILE ALA TYR ALA LYS PRO THR THR GLN
SEQRES 3 A 151 SER SER VAL ASP TYR ASN GLY ASP PRO ASN ARG ALA VAL
SEQRES 4 A 151 ASP GLY ASN ARG ASN GLY ASN PHE ASN SER GLY SER VAL
SEQRES 5 A 151 THR HIS THR ARG ALA ASP ASN PRO SER TRP TRP GLU VAL
SEQRES 6 A 151 ASP LEU LYS LYS MET ASP LYS VAL GLY LEU VAL LYS ILE
SEQRES 7 A 151 TYR ASN ARG THR ASP ALA GLU THR GLN ARG LEU SER ASN
SEQRES 8 A 151 PHE ASP VAL ILE LEU TYR ASP ASN ASN ARG ASN GLU VAL
SEQRES 9 A 151 ALA LYS LYS HIS VAL ASN ASN LEU SER GLY GLU SER VAL
SEQRES 10 A 151 SER LEU ASP PHE LYS GLU LYS GLY ALA ARG TYR ILE LYS
SEQRES 11 A 151 VAL LYS LEU LEU THR SER GLY VAL PRO LEU SER LEU ALA
SEQRES 12 A 151 GLU VAL GLU VAL PHE ARG GLU SER
SEQRES 1 B 151 GLY SER HIS MET ALA SER THR PRO ASP LYS PHE ASN ASP
SEQRES 2 B 151 GLY ASN LEU ASN ILE ALA TYR ALA LYS PRO THR THR GLN
SEQRES 3 B 151 SER SER VAL ASP TYR ASN GLY ASP PRO ASN ARG ALA VAL
SEQRES 4 B 151 ASP GLY ASN ARG ASN GLY ASN PHE ASN SER GLY SER VAL
SEQRES 5 B 151 THR HIS THR ARG ALA ASP ASN PRO SER TRP TRP GLU VAL
SEQRES 6 B 151 ASP LEU LYS LYS MET ASP LYS VAL GLY LEU VAL LYS ILE
SEQRES 7 B 151 TYR ASN ARG THR ASP ALA GLU THR GLN ARG LEU SER ASN
SEQRES 8 B 151 PHE ASP VAL ILE LEU TYR ASP ASN ASN ARG ASN GLU VAL
SEQRES 9 B 151 ALA LYS LYS HIS VAL ASN ASN LEU SER GLY GLU SER VAL
SEQRES 10 B 151 SER LEU ASP PHE LYS GLU LYS GLY ALA ARG TYR ILE LYS
SEQRES 11 B 151 VAL LYS LEU LEU THR SER GLY VAL PRO LEU SER LEU ALA
SEQRES 12 B 151 GLU VAL GLU VAL PHE ARG GLU SER
HET NAG C 1 15
HET GAL C 2 11
HET FUC C 3 10
HET FUC C 4 10
HET CA A1154 1
HET CA B1152 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM CA CALCIUM ION
FORMUL 3 NAG C8 H15 N O6
FORMUL 3 GAL C6 H12 O6
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *447(H2 O)
HELIX 1 1 ASP A 34 ASP A 40 5 7
HELIX 2 2 ASN A 46 GLY A 50 5 5
HELIX 3 3 GLU A 85 LEU A 89 5 5
HELIX 4 4 ASP B 34 ASP B 40 5 7
HELIX 5 5 ASN B 46 GLY B 50 5 5
HELIX 6 6 GLU B 85 LEU B 89 5 5
SHEET 1 AA 5 THR A 24 GLN A 26 0
SHEET 2 AA 5 TRP A 62 ASN A 80 -1 O GLU A 64 N THR A 25
SHEET 3 AA 5 SER A 116 LEU A 133 -1 O VAL A 117 N ILE A 78
SHEET 4 AA 5 PHE A 92 TYR A 97 -1 O ASP A 93 N LYS A 132
SHEET 5 AA 5 GLU A 103 VAL A 109 -1 N VAL A 104 O LEU A 96
SHEET 1 AB 3 THR A 24 GLN A 26 0
SHEET 2 AB 3 TRP A 62 ASN A 80 -1 O GLU A 64 N THR A 25
SHEET 3 AB 3 LEU A 142 VAL A 147 -1 N ALA A 143 O TYR A 79
SHEET 1 BA 5 THR B 24 GLN B 26 0
SHEET 2 BA 5 TRP B 62 ASN B 80 -1 O GLU B 64 N THR B 25
SHEET 3 BA 5 SER B 116 LEU B 133 -1 O VAL B 117 N ILE B 78
SHEET 4 BA 5 PHE B 92 TYR B 97 -1 O ASP B 93 N LYS B 132
SHEET 5 BA 5 GLU B 103 VAL B 109 -1 N VAL B 104 O LEU B 96
SHEET 1 BB 3 THR B 24 GLN B 26 0
SHEET 2 BB 3 TRP B 62 ASN B 80 -1 O GLU B 64 N THR B 25
SHEET 3 BB 3 LEU B 142 VAL B 147 -1 N ALA B 143 O TYR B 79
LINK O4 NAG C 1 C1 GAL C 2 1555 1555 1.41
LINK O3 NAG C 1 C1 FUC C 4 1555 1555 1.61
LINK O2 GAL C 2 C1 FUC C 3 1555 1555 1.42
LINK O ARG A 37 CA CA A1154 1555 1555 2.29
LINK OD1 ASP A 40 CA CA A1154 1555 1555 2.41
LINK O ASN A 42 CA CA A1154 1555 1555 2.36
LINK O SER A 51 CA CA A1154 1555 1555 2.49
LINK OG ASER A 51 CA CA A1154 1555 1555 2.65
LINK OG BSER A 51 CA CA A1154 1555 1555 2.46
LINK O ALA A 143 CA CA A1154 1555 1555 2.22
LINK OE1 GLU A 144 CA CA A1154 1555 1555 2.34
LINK O ARG B 37 CA CA B1152 1555 1555 2.40
LINK OD1 ASP B 40 CA CA B1152 1555 1555 2.45
LINK O ASN B 42 CA CA B1152 1555 1555 2.31
LINK O SER B 51 CA CA B1152 1555 1555 2.50
LINK OG SER B 51 CA CA B1152 1555 1555 2.32
LINK O ALA B 143 CA CA B1152 1555 1555 2.27
LINK OE1 GLU B 144 CA CA B1152 1555 1555 2.39
CISPEP 1 ASN A 59 PRO A 60 0 -8.39
CISPEP 2 ASN B 59 PRO B 60 0 -5.72
CRYST1 43.707 59.943 98.889 90.00 90.00 90.00 P 21 21 21 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 0.022880 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016683 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010112 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
