HEADER HYDROLASE 20-MAR-12 4E8D
TITLE CRYSTAL STRUCTURE OF STREPTOCOCCAL BETA-GALACTOSIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSYL HYDROLASE, FAMILY 35;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-GALACTOSIDASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 GENE: SP_0060;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P21
KEYWDS TIM BARREL, BETA-PROPELLER, GLYCOHYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.CHENG,L.WANG,X.H.BAI,Y.L.JIANG,Q.LI,G.YU,C.Z.ZHOU,Y.X.CHEN
REVDAT 4 08-NOV-23 4E8D 1 REMARK
REVDAT 3 07-AUG-13 4E8D 1 JRNL
REVDAT 2 13-JUN-12 4E8D 1 JRNL
REVDAT 1 30-MAY-12 4E8D 0
JRNL AUTH W.CHENG,L.WANG,Y.L.JIANG,X.H.BAI,J.CHU,Q.LI,G.YU,Q.L.LIANG,
JRNL AUTH 2 C.Z.ZHOU,Y.X.CHEN
JRNL TITL STRUCTURAL INSIGHTS INTO THE SUBSTRATE SPECIFICITY OF
JRNL TITL 2 STREPTOCOCCUS PNEUMONIAE BETA (1,3)-GALACTOSIDASE BGAC
JRNL REF J.BIOL.CHEM. V. 287 22910 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22593580
JRNL DOI 10.1074/JBC.M112.367128
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 103282
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5411
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7718
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 397
REMARK 3 BIN FREE R VALUE : 0.2210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9697
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 871
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.36000
REMARK 3 B22 (A**2) : 1.63000
REMARK 3 B33 (A**2) : -0.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.134
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.188
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10036 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13572 ; 0.929 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1182 ; 5.361 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 512 ;35.038 ;24.141
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1687 ;11.460 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;17.164 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1384 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7762 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 5883 ; 0.410 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9467 ; 0.823 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4153 ; 1.358 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4105 ; 2.314 ; 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 : 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
REMARK 4
REMARK 4 4E8D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071297.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-10
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108735
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.07000
REMARK 200 R SYM FOR SHELL (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.30
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: 3D3A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.65000
REMARK 290 SMTRY3 2 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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1
REMARK 465 GLY A 592
REMARK 465 GLU A 593
REMARK 465 ASN A 594
REMARK 465 LEU A 595
REMARK 465 MET B 1
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 ARG A 7 -128.87 -122.56
REMARK 500 PRO A 91 41.07 -94.36
REMARK 500 CYS A 96 -99.87 63.22
REMARK 500 GLU A 154 -158.21 54.36
REMARK 500 ASN A 155 111.01 -162.29
REMARK 500 TYR A 160 -43.69 -145.61
REMARK 500 PRO A 189 46.85 -87.06
REMARK 500 SER A 212 -179.96 -173.51
REMARK 500 GLN A 424 -111.71 48.34
REMARK 500 LYS A 436 122.46 -39.82
REMARK 500 ASP A 475 -118.54 55.60
REMARK 500 ASN A 481 85.37 69.74
REMARK 500 TRP A 544 119.77 -162.69
REMARK 500 ARG B 7 -132.96 -115.90
REMARK 500 PRO B 91 37.71 -93.54
REMARK 500 CYS B 96 -99.37 64.14
REMARK 500 GLU B 154 -155.80 56.05
REMARK 500 ASN B 155 113.95 -163.37
REMARK 500 TYR B 160 -43.72 -141.90
REMARK 500 GLU B 162 25.56 -140.26
REMARK 500 PRO B 189 48.63 -89.20
REMARK 500 SER B 212 -178.30 -172.61
REMARK 500 LYS B 248 -9.73 81.00
REMARK 500 ASP B 405 61.16 64.31
REMARK 500 GLN B 424 -110.41 47.64
REMARK 500 ASP B 475 -114.38 53.92
REMARK 500 ASN B 481 81.48 73.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 609
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E8C RELATED DB: PDB
DBREF 4E8D A 1 595 UNP Q97T90 Q97T90_STRPN 1 595
DBREF 4E8D B 1 595 UNP Q97T90 Q97T90_STRPN 1 595
SEQRES 1 A 595 MET THR ARG PHE GLU ILE ARG ASP ASP PHE TYR LEU ASP
SEQRES 2 A 595 GLY LYS SER PHE LYS ILE LEU SER GLY ALA ILE HIS TYR
SEQRES 3 A 595 PHE ARG VAL PRO PRO GLU ASP TRP TYR HIS SER LEU TYR
SEQRES 4 A 595 ASN LEU LYS ALA LEU GLY PHE ASN THR VAL GLU THR TYR
SEQRES 5 A 595 VAL ALA TRP ASN LEU HIS GLU PRO CYS GLU GLY GLU PHE
SEQRES 6 A 595 HIS PHE GLU GLY ASP LEU ASP LEU GLU LYS PHE LEU GLN
SEQRES 7 A 595 ILE ALA GLN ASP LEU GLY LEU TYR ALA ILE VAL ARG PRO
SEQRES 8 A 595 SER PRO PHE ILE CYS ALA GLU TRP GLU PHE GLY GLY LEU
SEQRES 9 A 595 PRO ALA TRP LEU LEU THR LYS ASN MET ARG ILE ARG SER
SEQRES 10 A 595 SER ASP PRO ALA TYR ILE GLU ALA VAL GLY ARG TYR TYR
SEQRES 11 A 595 ASP GLN LEU LEU PRO ARG LEU VAL PRO ARG LEU LEU ASP
SEQRES 12 A 595 ASN GLY GLY ASN ILE LEU MET MET GLN VAL GLU ASN GLU
SEQRES 13 A 595 TYR GLY SER TYR GLY GLU ASP LYS ALA TYR LEU ARG ALA
SEQRES 14 A 595 ILE ARG GLN LEU MET GLU GLU CYS GLY VAL THR CYS PRO
SEQRES 15 A 595 LEU PHE THR SER ASP GLY PRO TRP ARG ALA THR LEU LYS
SEQRES 16 A 595 ALA GLY THR LEU ILE GLU GLU ASP LEU PHE VAL THR GLY
SEQRES 17 A 595 ASN PHE GLY SER LYS ALA PRO TYR ASN PHE SER GLN MET
SEQRES 18 A 595 GLN GLU PHE PHE ASP GLU HIS GLY LYS LYS TRP PRO LEU
SEQRES 19 A 595 MET CYS MET GLU PHE TRP ASP GLY TRP PHE ASN ARG TRP
SEQRES 20 A 595 LYS GLU PRO ILE ILE THR ARG ASP PRO LYS GLU LEU ALA
SEQRES 21 A 595 ASP ALA VAL ARG GLU VAL LEU GLU GLN GLY SER ILE ASN
SEQRES 22 A 595 LEU TYR MET PHE HIS GLY GLY THR ASN PHE GLY PHE MET
SEQRES 23 A 595 ASN GLY CYS SER ALA ARG GLY THR LEU ASP LEU PRO GLN
SEQRES 24 A 595 VAL THR SER TYR ASP TYR ASP ALA LEU LEU ASP GLU GLU
SEQRES 25 A 595 GLY ASN PRO THR ALA LYS TYR LEU ALA VAL LYS LYS MET
SEQRES 26 A 595 MET ALA THR HIS PHE SER GLU TYR PRO GLN LEU GLU PRO
SEQRES 27 A 595 LEU TYR LYS GLU SER MET GLU LEU ASP ALA ILE PRO LEU
SEQRES 28 A 595 VAL GLU LYS VAL SER LEU PHE GLU THR LEU ASP SER LEU
SEQRES 29 A 595 SER SER PRO VAL GLU SER LEU TYR PRO GLN LYS MET GLU
SEQRES 30 A 595 GLU LEU GLY GLN SER TYR GLY TYR LEU LEU TYR ARG THR
SEQRES 31 A 595 GLU THR ASN TRP ASP ALA GLU GLU GLU ARG LEU ARG ILE
SEQRES 32 A 595 ILE ASP GLY ARG ASP ARG ALA GLN LEU TYR VAL ASP GLY
SEQRES 33 A 595 GLN TRP VAL LYS THR GLN TYR GLN THR GLU ILE GLY GLU
SEQRES 34 A 595 ASP ILE PHE TYR GLN GLY LYS LYS LYS GLY LEU SER ARG
SEQRES 35 A 595 LEU ASP ILE LEU ILE GLU ASN MET GLY ARG VAL ASN TYR
SEQRES 36 A 595 GLY HIS LYS PHE LEU ALA ASP THR GLN ARG LYS GLY ILE
SEQRES 37 A 595 ARG THR GLY VAL CYS LYS ASP LEU HIS PHE LEU LEU ASN
SEQRES 38 A 595 TRP LYS HIS TYR PRO LEU PRO LEU ASP ASN PRO GLU LYS
SEQRES 39 A 595 ILE ASP PHE SER LYS GLY TRP THR GLN GLY GLN PRO ALA
SEQRES 40 A 595 PHE TYR ALA TYR ASP PHE THR VAL GLU GLU PRO LYS ASP
SEQRES 41 A 595 THR TYR LEU ASP LEU SER GLU PHE GLY LYS GLY VAL ALA
SEQRES 42 A 595 PHE VAL ASN GLY GLN ASN LEU GLY ARG PHE TRP ASN VAL
SEQRES 43 A 595 GLY PRO THR LEU SER LEU TYR ILE PRO HIS SER TYR LEU
SEQRES 44 A 595 LYS GLU GLY ALA ASN ARG ILE ILE ILE PHE GLU THR GLU
SEQRES 45 A 595 GLY GLN TYR LYS GLU GLU ILE HIS LEU THR ARG LYS PRO
SEQRES 46 A 595 THR LEU LYS HIS ILE LYS GLY GLU ASN LEU
SEQRES 1 B 595 MET THR ARG PHE GLU ILE ARG ASP ASP PHE TYR LEU ASP
SEQRES 2 B 595 GLY LYS SER PHE LYS ILE LEU SER GLY ALA ILE HIS TYR
SEQRES 3 B 595 PHE ARG VAL PRO PRO GLU ASP TRP TYR HIS SER LEU TYR
SEQRES 4 B 595 ASN LEU LYS ALA LEU GLY PHE ASN THR VAL GLU THR TYR
SEQRES 5 B 595 VAL ALA TRP ASN LEU HIS GLU PRO CYS GLU GLY GLU PHE
SEQRES 6 B 595 HIS PHE GLU GLY ASP LEU ASP LEU GLU LYS PHE LEU GLN
SEQRES 7 B 595 ILE ALA GLN ASP LEU GLY LEU TYR ALA ILE VAL ARG PRO
SEQRES 8 B 595 SER PRO PHE ILE CYS ALA GLU TRP GLU PHE GLY GLY LEU
SEQRES 9 B 595 PRO ALA TRP LEU LEU THR LYS ASN MET ARG ILE ARG SER
SEQRES 10 B 595 SER ASP PRO ALA TYR ILE GLU ALA VAL GLY ARG TYR TYR
SEQRES 11 B 595 ASP GLN LEU LEU PRO ARG LEU VAL PRO ARG LEU LEU ASP
SEQRES 12 B 595 ASN GLY GLY ASN ILE LEU MET MET GLN VAL GLU ASN GLU
SEQRES 13 B 595 TYR GLY SER TYR GLY GLU ASP LYS ALA TYR LEU ARG ALA
SEQRES 14 B 595 ILE ARG GLN LEU MET GLU GLU CYS GLY VAL THR CYS PRO
SEQRES 15 B 595 LEU PHE THR SER ASP GLY PRO TRP ARG ALA THR LEU LYS
SEQRES 16 B 595 ALA GLY THR LEU ILE GLU GLU ASP LEU PHE VAL THR GLY
SEQRES 17 B 595 ASN PHE GLY SER LYS ALA PRO TYR ASN PHE SER GLN MET
SEQRES 18 B 595 GLN GLU PHE PHE ASP GLU HIS GLY LYS LYS TRP PRO LEU
SEQRES 19 B 595 MET CYS MET GLU PHE TRP ASP GLY TRP PHE ASN ARG TRP
SEQRES 20 B 595 LYS GLU PRO ILE ILE THR ARG ASP PRO LYS GLU LEU ALA
SEQRES 21 B 595 ASP ALA VAL ARG GLU VAL LEU GLU GLN GLY SER ILE ASN
SEQRES 22 B 595 LEU TYR MET PHE HIS GLY GLY THR ASN PHE GLY PHE MET
SEQRES 23 B 595 ASN GLY CYS SER ALA ARG GLY THR LEU ASP LEU PRO GLN
SEQRES 24 B 595 VAL THR SER TYR ASP TYR ASP ALA LEU LEU ASP GLU GLU
SEQRES 25 B 595 GLY ASN PRO THR ALA LYS TYR LEU ALA VAL LYS LYS MET
SEQRES 26 B 595 MET ALA THR HIS PHE SER GLU TYR PRO GLN LEU GLU PRO
SEQRES 27 B 595 LEU TYR LYS GLU SER MET GLU LEU ASP ALA ILE PRO LEU
SEQRES 28 B 595 VAL GLU LYS VAL SER LEU PHE GLU THR LEU ASP SER LEU
SEQRES 29 B 595 SER SER PRO VAL GLU SER LEU TYR PRO GLN LYS MET GLU
SEQRES 30 B 595 GLU LEU GLY GLN SER TYR GLY TYR LEU LEU TYR ARG THR
SEQRES 31 B 595 GLU THR ASN TRP ASP ALA GLU GLU GLU ARG LEU ARG ILE
SEQRES 32 B 595 ILE ASP GLY ARG ASP ARG ALA GLN LEU TYR VAL ASP GLY
SEQRES 33 B 595 GLN TRP VAL LYS THR GLN TYR GLN THR GLU ILE GLY GLU
SEQRES 34 B 595 ASP ILE PHE TYR GLN GLY LYS LYS LYS GLY LEU SER ARG
SEQRES 35 B 595 LEU ASP ILE LEU ILE GLU ASN MET GLY ARG VAL ASN TYR
SEQRES 36 B 595 GLY HIS LYS PHE LEU ALA ASP THR GLN ARG LYS GLY ILE
SEQRES 37 B 595 ARG THR GLY VAL CYS LYS ASP LEU HIS PHE LEU LEU ASN
SEQRES 38 B 595 TRP LYS HIS TYR PRO LEU PRO LEU ASP ASN PRO GLU LYS
SEQRES 39 B 595 ILE ASP PHE SER LYS GLY TRP THR GLN GLY GLN PRO ALA
SEQRES 40 B 595 PHE TYR ALA TYR ASP PHE THR VAL GLU GLU PRO LYS ASP
SEQRES 41 B 595 THR TYR LEU ASP LEU SER GLU PHE GLY LYS GLY VAL ALA
SEQRES 42 B 595 PHE VAL ASN GLY GLN ASN LEU GLY ARG PHE TRP ASN VAL
SEQRES 43 B 595 GLY PRO THR LEU SER LEU TYR ILE PRO HIS SER TYR LEU
SEQRES 44 B 595 LYS GLU GLY ALA ASN ARG ILE ILE ILE PHE GLU THR GLU
SEQRES 45 B 595 GLY GLN TYR LYS GLU GLU ILE HIS LEU THR ARG LYS PRO
SEQRES 46 B 595 THR LEU LYS HIS ILE LYS GLY GLU ASN LEU
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET GOL B 601 6
HET GOL B 602 6
HET GOL B 603 6
HET GOL B 604 6
HET GOL B 605 6
HET GOL B 606 6
HET GOL B 607 6
HET GOL B 608 6
HET GOL B 609 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 13(C3 H8 O3)
FORMUL 16 HOH *871(H2 O)
HELIX 1 1 TYR A 26 VAL A 29 5 4
HELIX 2 2 PRO A 30 GLU A 32 5 3
HELIX 3 3 ASP A 33 LEU A 44 1 12
HELIX 4 4 ALA A 54 GLU A 59 1 6
HELIX 5 5 GLU A 68 LEU A 71 5 4
HELIX 6 6 ASP A 72 LEU A 83 1 12
HELIX 7 7 TRP A 99 LEU A 104 5 6
HELIX 8 8 PRO A 105 LYS A 111 5 7
HELIX 9 9 ASP A 119 LEU A 134 1 16
HELIX 10 10 PRO A 135 GLY A 145 5 11
HELIX 11 11 GLU A 156 TYR A 160 5 5
HELIX 12 12 ASP A 163 CYS A 177 1 15
HELIX 13 13 TRP A 190 THR A 198 1 9
HELIX 14 14 LEU A 199 ASP A 203 5 5
HELIX 15 15 LYS A 213 HIS A 228 1 16
HELIX 16 16 ASP A 255 GLY A 270 1 16
HELIX 17 17 THR A 316 PHE A 330 1 15
HELIX 18 18 LEU A 357 SER A 365 1 9
HELIX 19 19 MET A 376 GLY A 380 5 5
HELIX 20 20 THR A 425 ILE A 427 5 3
HELIX 21 21 TYR A 455 PHE A 459 5 5
HELIX 22 22 ALA A 461 ARG A 465 5 5
HELIX 23 23 ASN A 491 ILE A 495 5 5
HELIX 24 24 PRO A 555 LEU A 559 5 5
HELIX 25 25 TYR B 26 VAL B 29 5 4
HELIX 26 26 PRO B 30 GLU B 32 5 3
HELIX 27 27 ASP B 33 LEU B 44 1 12
HELIX 28 28 ALA B 54 GLU B 59 1 6
HELIX 29 29 GLU B 68 LEU B 71 5 4
HELIX 30 30 ASP B 72 LEU B 83 1 12
HELIX 31 31 TRP B 99 LEU B 104 5 6
HELIX 32 32 PRO B 105 LYS B 111 5 7
HELIX 33 33 ASP B 119 VAL B 138 1 20
HELIX 34 34 PRO B 139 GLY B 145 5 7
HELIX 35 35 GLU B 156 TYR B 160 5 5
HELIX 36 36 ASP B 163 CYS B 177 1 15
HELIX 37 37 TRP B 190 THR B 198 1 9
HELIX 38 38 LEU B 199 ASP B 203 5 5
HELIX 39 39 LYS B 213 HIS B 228 1 16
HELIX 40 40 ASP B 255 GLY B 270 1 16
HELIX 41 41 THR B 316 PHE B 330 1 15
HELIX 42 42 THR B 360 SER B 365 1 6
HELIX 43 43 MET B 376 GLY B 380 5 5
HELIX 44 44 THR B 425 ILE B 427 5 3
HELIX 45 45 ALA B 461 ARG B 465 5 5
HELIX 46 46 ASN B 491 ILE B 495 5 5
HELIX 47 47 PRO B 555 LEU B 559 5 5
SHEET 1 A 3 PHE A 4 ILE A 6 0
SHEET 2 A 3 PHE A 10 LEU A 12 -1 O TYR A 11 N GLU A 5
SHEET 3 A 3 LYS A 15 SER A 16 -1 O LYS A 15 N LEU A 12
SHEET 1 B 9 LEU A 20 ILE A 24 0
SHEET 2 B 9 THR A 48 TYR A 52 1 O GLU A 50 N GLY A 22
SHEET 3 B 9 TYR A 86 ARG A 90 1 O ARG A 90 N THR A 51
SHEET 4 B 9 ILE A 148 GLN A 152 1 O LEU A 149 N ALA A 87
SHEET 5 B 9 LEU A 183 ASP A 187 1 O PHE A 184 N MET A 151
SHEET 6 B 9 PHE A 205 PHE A 210 1 O PHE A 205 N THR A 185
SHEET 7 B 9 MET A 235 TRP A 240 1 O MET A 235 N GLY A 208
SHEET 8 B 9 SER A 271 HIS A 278 1 O ASN A 273 N PHE A 239
SHEET 9 B 9 LEU A 20 ILE A 24 1 N ALA A 23 O LEU A 274
SHEET 1 C 2 CYS A 289 ARG A 292 0
SHEET 2 C 2 LEU A 295 PRO A 298 -1 O LEU A 297 N SER A 290
SHEET 1 D 8 GLN A 538 TRP A 544 0
SHEET 2 D 8 LYS A 530 VAL A 535 -1 N ALA A 533 O LEU A 540
SHEET 3 D 8 GLY A 562 GLU A 570 -1 O ILE A 567 N PHE A 534
SHEET 4 D 8 ALA A 507 VAL A 515 -1 N VAL A 515 O GLY A 562
SHEET 5 D 8 LEU A 346 SER A 356 -1 N VAL A 352 O ALA A 510
SHEET 6 D 8 GLU A 578 THR A 582 -1 O LEU A 581 N LEU A 346
SHEET 7 D 8 THR A 521 ASP A 524 -1 N TYR A 522 O THR A 582
SHEET 8 D 8 SER A 551 ILE A 554 -1 O ILE A 554 N THR A 521
SHEET 1 E 6 VAL A 368 SER A 370 0
SHEET 2 E 6 TRP A 482 LEU A 487 -1 O TRP A 482 N SER A 370
SHEET 3 E 6 TYR A 385 ASN A 393 -1 N LEU A 387 O TYR A 485
SHEET 4 E 6 LEU A 440 GLU A 448 -1 O SER A 441 N THR A 392
SHEET 5 E 6 ARG A 409 VAL A 414 -1 N TYR A 413 O ASP A 444
SHEET 6 E 6 GLN A 417 TYR A 423 -1 O VAL A 419 N LEU A 412
SHEET 1 F 4 ILE A 431 TYR A 433 0
SHEET 2 F 4 GLU A 399 ARG A 407 -1 N LEU A 401 O ILE A 431
SHEET 3 F 4 GLY A 467 LYS A 474 -1 O ARG A 469 N ASP A 405
SHEET 4 F 4 HIS A 477 PHE A 478 -1 O HIS A 477 N LYS A 474
SHEET 1 G 3 PHE B 4 ILE B 6 0
SHEET 2 G 3 PHE B 10 LEU B 12 -1 O TYR B 11 N GLU B 5
SHEET 3 G 3 LYS B 15 SER B 16 -1 O LYS B 15 N LEU B 12
SHEET 1 H 9 LEU B 20 ILE B 24 0
SHEET 2 H 9 THR B 48 TYR B 52 1 O GLU B 50 N GLY B 22
SHEET 3 H 9 TYR B 86 ARG B 90 1 O ARG B 90 N THR B 51
SHEET 4 H 9 ILE B 148 GLN B 152 1 O LEU B 149 N ALA B 87
SHEET 5 H 9 LEU B 183 ASP B 187 1 O PHE B 184 N MET B 151
SHEET 6 H 9 PHE B 205 PHE B 210 1 O ASN B 209 N ASP B 187
SHEET 7 H 9 MET B 235 TRP B 240 1 O MET B 235 N GLY B 208
SHEET 8 H 9 SER B 271 HIS B 278 1 O ASN B 273 N PHE B 239
SHEET 9 H 9 LEU B 20 ILE B 24 1 N ALA B 23 O LEU B 274
SHEET 1 I 2 CYS B 289 ARG B 292 0
SHEET 2 I 2 LEU B 295 PRO B 298 -1 O LEU B 297 N SER B 290
SHEET 1 J 8 GLN B 538 TRP B 544 0
SHEET 2 J 8 LYS B 530 VAL B 535 -1 N ALA B 533 O LEU B 540
SHEET 3 J 8 GLY B 562 GLU B 570 -1 O PHE B 569 N VAL B 532
SHEET 4 J 8 ALA B 507 VAL B 515 -1 N VAL B 515 O GLY B 562
SHEET 5 J 8 LEU B 346 SER B 356 -1 N VAL B 352 O ALA B 510
SHEET 6 J 8 GLU B 578 THR B 582 -1 O LEU B 581 N LEU B 346
SHEET 7 J 8 THR B 521 ASP B 524 -1 N TYR B 522 O THR B 582
SHEET 8 J 8 SER B 551 ILE B 554 -1 O ILE B 554 N THR B 521
SHEET 1 K 6 VAL B 368 SER B 370 0
SHEET 2 K 6 TRP B 482 LEU B 487 -1 O HIS B 484 N VAL B 368
SHEET 3 K 6 TYR B 385 THR B 392 -1 N TYR B 385 O LEU B 487
SHEET 4 K 6 SER B 441 GLU B 448 -1 O SER B 441 N THR B 392
SHEET 5 K 6 ARG B 409 VAL B 414 -1 N TYR B 413 O ASP B 444
SHEET 6 K 6 GLN B 417 TYR B 423 -1 O GLN B 422 N ALA B 410
SHEET 1 L 4 ILE B 431 TYR B 433 0
SHEET 2 L 4 GLU B 399 ARG B 407 -1 N LEU B 401 O ILE B 431
SHEET 3 L 4 GLY B 467 LYS B 474 -1 O ARG B 469 N ASP B 405
SHEET 4 L 4 HIS B 477 PHE B 478 -1 O HIS B 477 N LYS B 474
CISPEP 1 TYR A 275 MET A 276 0 -1.36
CISPEP 2 ARG A 407 ASP A 408 0 3.03
CISPEP 3 GLY A 547 PRO A 548 0 9.06
CISPEP 4 TYR B 275 MET B 276 0 0.89
CISPEP 5 ARG B 407 ASP B 408 0 3.57
CISPEP 6 GLY B 547 PRO B 548 0 9.27
SITE 1 AC1 5 LYS A 341 GLU A 342 LYS A 519 ASP A 520
SITE 2 AC1 5 HIS A 556
SITE 1 AC2 5 GLN A 81 GLY A 84 LEU A 85 TYR A 86
SITE 2 AC2 5 ASN A 147
SITE 1 AC3 6 ASP A 304 GLU A 311 PRO A 585 HOH A 857
SITE 2 AC3 6 HOH A 878 HOH A 988
SITE 1 AC4 7 ARG A 191 GLN A 220 GLU A 223 PHE A 224
SITE 2 AC4 7 GLU A 227 LYS A 438 HOH A1012
SITE 1 AC5 8 ASP B 490 PRO B 492 PHE B 534 GLY B 537
SITE 2 AC5 8 GLN B 538 ASN B 539 GOL B 604 HOH B 861
SITE 1 AC6 6 GLU B 32 ASP B 70 GLN B 538 SER B 557
SITE 2 AC6 6 TYR B 558 HOH B1031
SITE 1 AC7 5 LYS B 213 PRO B 215 GLU B 265 HOH B 735
SITE 2 AC7 5 HOH B 919
SITE 1 AC8 6 GLY B 284 PHE B 285 PRO B 488 ASN B 539
SITE 2 AC8 6 GOL B 601 HOH B 927
SITE 1 AC9 7 ARG B 191 LEU B 194 GLN B 220 GLU B 223
SITE 2 AC9 7 PHE B 224 GLU B 227 LYS B 438
SITE 1 BC1 2 VAL B 368 GLU B 369
SITE 1 BC2 4 ARG B 171 GLU B 175 HOH B 863 HOH B 944
SITE 1 BC3 6 LYS B 341 GLU B 342 LYS B 519 ASP B 520
SITE 2 BC3 6 HIS B 556 HOH B 995
SITE 1 BC4 1 HOH B 954
CRYST1 79.971 79.300 99.387 90.00 106.94 90.00 P 1 21 1 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 0.012505 0.000000 0.003809 0.00000
SCALE2 0.000000 0.012610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010518 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
