HEADER SUGAR-BINDING PROTEIN 25-JUL-07 2V72
TITLE THE STRUCTURE OF THE FAMILY 32 CBM FROM C. PERFRINGENS NANJ
TITLE 2 IN COMPLEX WITH GALACTOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXO-ALPHA-SIALIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 42-180;
COMPND 5 SYNONYM: CBM32;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;
SOURCE 3 ORGANISM_TAXID: 1502;
SOURCE 4 ATCC: 13124;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET 28A
KEYWDS GALACTOSE, BACTERIAL PATHOGEN, CARBOHYDRATE-BINDING MODULE,
KEYWDS 2 SUGAR-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.BORASTON,E.FICKO-BLEAN,M.HEALEY
REVDAT 3 24-FEB-09 2V72 1 VERSN
REVDAT 2 16-OCT-07 2V72 1 JRNL
REVDAT 1 21-AUG-07 2V72 0
JRNL AUTH A.B.BORASTON,E.FICKO-BLEAN,M.HEALEY
JRNL TITL CARBOHYDRATE RECOGNITION BY A LARGE SIALIDASE
JRNL TITL 2 TOXIN FROM CLOSTRIDIUM PERFRINGENS.
JRNL REF BIOCHEMISTRY V. 46 11352 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17850114
JRNL DOI 10.1021/BI701317G
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 5668
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) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.325
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 636
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 422
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1022
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.62000
REMARK 3 B22 (A**2) : -2.29000
REMARK 3 B33 (A**2) : -0.34000
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): 0.532
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.338
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.243
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.813
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1051 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1432 ; 1.253 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 136 ; 5.947 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ;47.857 ;26.889
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 168 ;16.242 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;17.018 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 170 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 785 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 479 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 710 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 61 ; 0.139 ; 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): 27 ; 0.153 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.229 ; 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): 700 ; 0.408 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1092 ; 0.698 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 404 ; 0.904 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 340 ; 1.400 ; 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 : BABINET MODEL WITH 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.
REMARK 4
REMARK 4 2V72 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-07.
REMARK 100 THE PDBE ID CODE IS EBI-33278.
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
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 : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6309
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.25
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 4.34
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.21
REMARK 200 R MERGE FOR SHELL (I) : 0.26
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.10
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
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 21.13250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.50150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.93000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.50150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.13250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.93000
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 GLY A -4
REMARK 465 MET A -3
REMARK 465 ALA A -2
REMARK 465 SER A -1
REMARK 465 ALA A 0
REMARK 465 ILE A 1
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 ILE A 2 CB CG1 CG2 CD1
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 ASP A 22 69.60 -118.67
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 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 A1139 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 29 OD1
REMARK 620 2 THR A 34 O 138.7
REMARK 620 3 ALA A 132 O 141.4 74.8
REMARK 620 4 GLU A 133 OE2 71.7 149.6 77.5
REMARK 620 5 ASN A 31 O 97.2 87.4 104.0 87.3
REMARK 620 6 SER A 26 O 80.0 86.0 85.8 104.2 166.4
REMARK 620 7 THR A 34 OG1 71.5 68.9 143.2 139.2 80.4 86.1
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1139
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A1140
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V73 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE FAMILY 40 CBM FROM
REMARK 900 C. PERFRINGENS NANJ IN COMPLEX WITH A
REMARK 900 SIALIC ACID CONTAINING MOLECULE
DBREF 2V72 A -4 -1 PDB 2V72 2V72 -4 -1
DBREF 2V72 A 0 138 UNP Q8XMY5 Q8XMY5_CLOPE 42 180
SEQRES 1 A 143 GLY MET ALA SER ALA ILE ILE GLU THR ALA ILE PRO GLN
SEQRES 2 A 143 SER GLU MET THR ALA SER ALA THR SER GLU GLU GLY GLN
SEQRES 3 A 143 ASP PRO ALA SER SER ALA ILE ASP GLY ASN ILE ASN THR
SEQRES 4 A 143 MET TRP HIS THR LYS TRP ASN GLY SER ASP ALA LEU PRO
SEQRES 5 A 143 GLN SER LEU SER VAL ASN LEU GLY LYS ALA ARG LYS VAL
SEQRES 6 A 143 SER SER ILE ALA ILE THR PRO ARG THR SER GLY ASN ASN
SEQRES 7 A 143 GLY PHE ILE THR LYS TYR GLU ILE HIS ALA ILE ASN ASN
SEQRES 8 A 143 GLY VAL GLU THR LEU VAL ALA GLU GLY THR TRP GLU GLU
SEQRES 9 A 143 ASN ASN LEU VAL LYS THR VAL THR PHE ASP SER PRO ILE
SEQRES 10 A 143 ASP ALA GLU GLU ILE LYS ILE THR ALA ILE GLN GLY VAL
SEQRES 11 A 143 GLY GLY PHE ALA SER ILE ALA GLU LEU ASN VAL TYR GLU
HET CA A1139 1
HET GAL A1140 12
HETNAM GAL BETA-D-GALACTOSE
HETNAM CA CALCIUM ION
FORMUL 2 GAL C6 H12 O6
FORMUL 3 CA CA 2+
FORMUL 4 HOH *42(H2 O1)
HELIX 1 1 PRO A 7 MET A 11 5 5
HELIX 2 2 PRO A 23 ILE A 28 5 6
HELIX 3 3 GLY A 126 PHE A 128 5 3
SHEET 1 AA 5 THR A 12 ALA A 15 0
SHEET 2 AA 5 GLN A 48 THR A 66 -1 O SER A 51 N SER A 14
SHEET 3 AA 5 LYS A 104 GLY A 124 -1 O LYS A 104 N ILE A 65
SHEET 4 AA 5 ILE A 76 ASN A 85 -1 N THR A 77 O GLN A 123
SHEET 5 AA 5 VAL A 88 THR A 96 -1 O VAL A 88 N ASN A 85
SHEET 1 AB 3 THR A 12 ALA A 15 0
SHEET 2 AB 3 GLN A 48 THR A 66 -1 O SER A 51 N SER A 14
SHEET 3 AB 3 GLU A 133 TYR A 137 -1 O GLU A 133 N THR A 66
SHEET 1 AC 2 TRP A 36 HIS A 37 0
SHEET 2 AC 2 SER A 130 ILE A 131 -1 O ILE A 131 N TRP A 36
LINK CA CA A1139 OD1 ASP A 29 1555 1555 2.31
LINK CA CA A1139 O THR A 34 1555 1555 2.35
LINK CA CA A1139 O ALA A 132 1555 1555 2.32
LINK CA CA A1139 OE2 GLU A 133 1555 1555 2.41
LINK CA CA A1139 O ASN A 31 1555 1555 2.29
LINK CA CA A1139 O SER A 26 1555 1555 2.31
LINK CA CA A1139 OG1 THR A 34 1555 1555 2.57
CISPEP 1 LEU A 46 PRO A 47 0 -1.08
CISPEP 2 ASN A 86 GLY A 87 0 -22.10
SITE 1 AC1 6 SER A 26 ASP A 29 ASN A 31 THR A 34
SITE 2 AC1 6 ALA A 132 GLU A 133
SITE 1 AC2 5 HIS A 37 TRP A 40 ARG A 68 ASN A 73
SITE 2 AC2 5 HOH A2042
CRYST1 42.265 45.860 69.003 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 0.023660 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021805 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014492 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
