HEADER HYDROLASE 19-FEB-13 4JAW
TITLE CRYSTAL STRUCTURE OF LACTO-N-BIOSIDASE FROM BIFIDOBACTERIUM BIFIDUM
TITLE 2 COMPLEXED WITH LNB-THIAZOLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTO-N-BIOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUE 41-663;
COMPND 5 EC: 3.2.1.140;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BIFIDOBACTERIUM BIFIDUM;
SOURCE 3 ORGANISM_TAXID: 398514;
SOURCE 4 STRAIN: JCM1254;
SOURCE 5 GENE: LNBB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28B
KEYWDS ALPHA/BETA-DOMAIN, TIM BARREL, BETA-TREFOIL, HYDROLASE, MEMBRANE-
KEYWDS 2 ANCHORED EXTRACELLULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ITO,T.KATAYAMA,K.A.STUBBS,S.FUSHINOBU
REVDAT 4 08-NOV-23 4JAW 1 HETSYN
REVDAT 3 29-JUL-20 4JAW 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 10-JUL-13 4JAW 1 JRNL
REVDAT 1 20-MAR-13 4JAW 0
JRNL AUTH T.ITO,T.KATAYAMA,M.HATTIE,H.SAKURAMA,J.WADA,R.SUZUKI,
JRNL AUTH 2 H.ASHIDA,T.WAKAGI,K.YAMAMOTO,K.A.STUBBS,S.FUSHINOBU
JRNL TITL CRYSTAL STRUCTURES OF A GLYCOSIDE HYDROLASE FAMILY 20
JRNL TITL 2 LACTO-N-BIOSIDASE FROM BIFIDOBACTERIUM BIFIDUM
JRNL REF J.BIOL.CHEM. V. 288 11795 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23479733
JRNL DOI 10.1074/JBC.M112.420109
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.WADA,T.ANDO,M.KIYOHARA,H.ASHIDA,M.KITAOKA,M.YAMAGUCHI,
REMARK 1 AUTH 2 H.KUMAGAI,T.KATAYAMA,K.YAMAMOTO
REMARK 1 TITL BIFIDOBACTERIUM BIFIDUM LACTO-N-BIOSIDASE, A CRITICAL ENZYME
REMARK 1 TITL 2 FOR THE DEGRADATION OF HUMAN MILK OLIGOSACCHARIDES WITH A
REMARK 1 TITL 3 TYPE 1 STRUCTURE.
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 74 3996 2008
REMARK 1 REFN ISSN 0099-2240
REMARK 1 PMID 18469123
REMARK 1 DOI 10.1128/AEM.00149-08
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 141665
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7499
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) : 9905
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 522
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9932
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 403
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.879
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10236 ; 0.027 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13898 ; 2.365 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1263 ; 7.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 472 ;33.270 ;24.873
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1719 ;13.646 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;20.064 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1520 ; 0.275 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7762 ; 0.015 ; 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): 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): 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4JAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111), NUMERICAL LINK TYPE
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150089
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9700
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) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.6.0117
REMARK 200 STARTING MODEL: PDB ENTRY 4H04
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE
REMARK 280 TETRAHYDRATE, 0.1M SODIUM CITRATE, 2.0M AMMONIUM SULFATE, PH 5.6,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
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 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 58.26200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.77850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.26200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.77850
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, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 A 950 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 939 LIES ON A SPECIAL POSITION.
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 20
REMARK 465 GLY A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 HIS A 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 HIS A 27
REMARK 465 HIS A 28
REMARK 465 HIS A 29
REMARK 465 ASP A 663
REMARK 465 MET B 20
REMARK 465 GLY B 21
REMARK 465 SER B 22
REMARK 465 SER B 23
REMARK 465 HIS B 24
REMARK 465 HIS B 25
REMARK 465 HIS B 26
REMARK 465 HIS B 27
REMARK 465 HIS B 28
REMARK 465 HIS B 29
REMARK 465 SER B 662
REMARK 465 ASP B 663
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 HIS A 39 CG HIS A 39 CD2 0.060
REMARK 500 ARG A 52 CZ ARG A 52 NH1 0.091
REMARK 500 TRP A 62 CG TRP A 62 CD1 0.086
REMARK 500 TRP A 62 CE2 TRP A 62 CD2 0.099
REMARK 500 TRP A 267 CE2 TRP A 267 CD2 0.077
REMARK 500 TRP A 465 CE2 TRP A 465 CD2 0.074
REMARK 500 HIS B 39 CG HIS B 39 CD2 0.068
REMARK 500 TRP B 62 CE2 TRP B 62 CD2 0.111
REMARK 500 ARG B 162 CZ ARG B 162 NH1 0.089
REMARK 500 HIS B 263 CG HIS B 263 CD2 0.066
REMARK 500 TRP B 267 CE2 TRP B 267 CD2 0.084
REMARK 500 TRP B 420 CE2 TRP B 420 CD2 0.079
REMARK 500 ARG B 497 CZ ARG B 497 NH2 0.120
REMARK 500 TRP B 544 CG TRP B 544 CD1 0.086
REMARK 500 HIS B 573 CG HIS B 573 CD2 0.073
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 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 147 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 239 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 239 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 289 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 LYS A 297 CD - CE - NZ ANGL. DEV. = -14.8 DEGREES
REMARK 500 ASP A 304 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TYR A 322 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 371 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 433 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 433 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 448 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 448 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 486 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 497 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ASP A 597 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 613 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU A 626 CB - CG - CD1 ANGL. DEV. = -11.3 DEGREES
REMARK 500 SER B 38 N - CA - CB ANGL. DEV. = 9.8 DEGREES
REMARK 500 LYS B 112 CD - CE - NZ ANGL. DEV. = 16.9 DEGREES
REMARK 500 ASP B 147 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 200 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 200 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP B 239 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 239 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 LYS B 246 CD - CE - NZ ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG B 371 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU B 434 CB - CG - CD1 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG B 497 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 587 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 613 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 613 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 647 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU B 660 CB - CG - CD1 ANGL. DEV. = 11.3 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 ALA A 188 62.98 -100.30
REMARK 500 GLN A 190 -63.01 72.25
REMARK 500 ALA A 230 48.49 -82.62
REMARK 500 THR A 326 -153.23 -157.07
REMARK 500 LYS A 381 -62.24 -136.21
REMARK 500 ASN A 438 33.05 70.03
REMARK 500 ASP A 467 -138.87 44.46
REMARK 500 TRP A 493 -61.46 -92.13
REMARK 500 GLN B 190 -65.11 77.54
REMARK 500 THR B 326 -149.02 -159.62
REMARK 500 LYS B 381 -60.50 -135.10
REMARK 500 ASP B 467 -141.46 43.55
REMARK 500 ASP B 617 -38.78 136.06
REMARK 500 GLN B 628 15.82 59.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 106 GLY B 107 -146.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H04 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH LACTO-N-BIOSE
DBREF 4JAW A 41 663 UNP B3TLD6 B3TLD6_BIFBI 41 663
DBREF 4JAW B 41 663 UNP B3TLD6 B3TLD6_BIFBI 41 663
SEQADV 4JAW MET A 20 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW GLY A 21 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER A 22 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER A 23 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 24 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 25 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 26 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 27 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 28 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 29 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER A 30 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER A 31 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW GLY A 32 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW LEU A 33 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW VAL A 34 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW PRO A 35 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW ARG A 36 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW GLY A 37 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER A 38 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS A 39 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW MET A 40 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW MET B 20 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW GLY B 21 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER B 22 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER B 23 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 24 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 25 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 26 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 27 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 28 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 29 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER B 30 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER B 31 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW GLY B 32 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW LEU B 33 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW VAL B 34 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW PRO B 35 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW ARG B 36 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW GLY B 37 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW SER B 38 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW HIS B 39 UNP B3TLD6 EXPRESSION TAG
SEQADV 4JAW MET B 40 UNP B3TLD6 EXPRESSION TAG
SEQRES 1 A 644 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 644 LEU VAL PRO ARG GLY SER HIS MET GLY TYR SER ALA THR
SEQRES 3 A 644 ALA PRO VAL ASN LEU THR ARG PRO ALA THR VAL PRO SER
SEQRES 4 A 644 MET ASP GLY TRP THR ASP GLY THR GLY ALA TRP THR LEU
SEQRES 5 A 644 GLY GLU GLY THR ARG VAL VAL SER SER ASP ALA LEU ALA
SEQRES 6 A 644 ALA ARG ALA GLN SER LEU ALA SER GLU LEU THR LYS PHE
SEQRES 7 A 644 THR ASP VAL ASP ILE LYS ALA ALA THR GLY SER ALA THR
SEQRES 8 A 644 GLY LYS ASP ILE SER LEU THR LEU ASP ALA SER LYS LYS
SEQRES 9 A 644 ALA GLU LEU GLY ASP GLU GLY PHE LYS LEU ASN ILE GLY
SEQRES 10 A 644 SER LYS GLY LEU GLU VAL ILE GLY ALA THR ASP ILE GLY
SEQRES 11 A 644 VAL PHE TYR GLY THR ARG SER VAL SER GLN MET LEU ARG
SEQRES 12 A 644 GLN GLY GLN LEU THR LEU PRO ALA GLY THR VAL ALA THR
SEQRES 13 A 644 LYS PRO LYS TYR LYS GLU ARG GLY ALA THR LEU CYS ALA
SEQRES 14 A 644 CYS GLN ILE ASN ILE SER THR ASP TRP ILE ASP ARG PHE
SEQRES 15 A 644 LEU SER ASP MET ALA ASP LEU ARG LEU ASN TYR VAL LEU
SEQRES 16 A 644 LEU GLU MET LYS LEU LYS PRO GLU GLU ASP ASN THR LYS
SEQRES 17 A 644 LYS ALA ALA THR TRP SER TYR TYR THR ARG ASP ASP VAL
SEQRES 18 A 644 LYS LYS PHE VAL LYS LYS ALA ASN ASN TYR GLY ILE ASP
SEQRES 19 A 644 VAL ILE PRO GLU ILE ASN SER PRO GLY HIS MET ASN VAL
SEQRES 20 A 644 TRP LEU GLU ASN TYR PRO GLU TYR GLN LEU ALA ASP ASN
SEQRES 21 A 644 SER GLY ARG LYS ASP PRO ASN LYS LEU ASP ILE SER ASN
SEQRES 22 A 644 PRO GLU ALA VAL LYS PHE TYR LYS THR LEU ILE ASP GLU
SEQRES 23 A 644 TYR ASP GLY VAL PHE THR THR LYS TYR TRP HIS MET GLY
SEQRES 24 A 644 ALA ASP GLU TYR MET ILE GLY THR SER PHE ASP ASN TYR
SEQRES 25 A 644 SER LYS LEU LYS THR PHE ALA GLU LYS GLN TYR GLY ALA
SEQRES 26 A 644 GLY ALA THR PRO ASN ASP ALA PHE THR GLY PHE ILE ASN
SEQRES 27 A 644 ASP ILE ASP LYS TYR VAL LYS ALA LYS GLY LYS GLN LEU
SEQRES 28 A 644 ARG ILE TRP ASN ASP GLY ILE VAL ASN THR LYS ASN VAL
SEQRES 29 A 644 SER LEU ASN LYS ASP ILE VAL ILE GLU TYR TRP TYR GLY
SEQRES 30 A 644 ALA GLY ARG LYS PRO GLN GLU LEU VAL GLN ASP GLY TYR
SEQRES 31 A 644 THR LEU MET ASN ALA THR GLN ALA LEU TYR TRP SER ARG
SEQRES 32 A 644 SER ALA GLN VAL TYR LYS VAL ASN ALA ALA ARG LEU TYR
SEQRES 33 A 644 ASN ASN ASN TRP ASN VAL GLY THR PHE ASP GLY GLY ARG
SEQRES 34 A 644 GLN ILE ASP LYS ASN TYR ASP LYS LEU THR GLY ALA LYS
SEQRES 35 A 644 VAL SER ILE TRP PRO ASP SER SER TYR PHE GLN THR GLU
SEQRES 36 A 644 ASN GLU VAL GLU LYS GLU ILE PHE ASP GLY MET ARG PHE
SEQRES 37 A 644 ILE SER GLN MET THR TRP SER ASP SER ARG PRO TRP ALA
SEQRES 38 A 644 THR TRP ASN ASP MET LYS ALA ASP ILE ASP LYS ILE GLY
SEQRES 39 A 644 TYR PRO LEU ASP ILE ARG GLU TYR ASP TYR THR PRO VAL
SEQRES 40 A 644 ASP ALA GLY ILE TYR ASP ILE PRO GLN LEU LYS SER ILE
SEQRES 41 A 644 SER LYS GLY PRO TRP GLU LEU ILE THR THR PRO ASP GLY
SEQRES 42 A 644 TYR TYR GLN MET LYS ASP THR VAL SER GLY LYS CYS LEU
SEQRES 43 A 644 ALA LEU PHE THR GLY SER LYS HIS LEU ASP VAL VAL THR
SEQRES 44 A 644 GLN VAL GLY ALA ARG PRO GLU LEU ARG ASN CYS ALA ASP
SEQRES 45 A 644 VAL SER VAL GLY GLN ASP GLN ARG ASN THR ALA ASN GLU
SEQRES 46 A 644 ARG ASN THR GLN LYS TRP GLN ILE ARG ALA ASP LYS ASP
SEQRES 47 A 644 GLY LYS TYR THR ILE SER PRO ALA LEU THR GLN GLN ARG
SEQRES 48 A 644 LEU ALA ILE ALA THR GLY ASN GLU GLN ASN ILE ASP LEU
SEQRES 49 A 644 GLU THR HIS ARG PRO ALA ALA GLY THR VAL ALA GLN PHE
SEQRES 50 A 644 PRO ALA ASP LEU VAL SER ASP
SEQRES 1 B 644 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 644 LEU VAL PRO ARG GLY SER HIS MET GLY TYR SER ALA THR
SEQRES 3 B 644 ALA PRO VAL ASN LEU THR ARG PRO ALA THR VAL PRO SER
SEQRES 4 B 644 MET ASP GLY TRP THR ASP GLY THR GLY ALA TRP THR LEU
SEQRES 5 B 644 GLY GLU GLY THR ARG VAL VAL SER SER ASP ALA LEU ALA
SEQRES 6 B 644 ALA ARG ALA GLN SER LEU ALA SER GLU LEU THR LYS PHE
SEQRES 7 B 644 THR ASP VAL ASP ILE LYS ALA ALA THR GLY SER ALA THR
SEQRES 8 B 644 GLY LYS ASP ILE SER LEU THR LEU ASP ALA SER LYS LYS
SEQRES 9 B 644 ALA GLU LEU GLY ASP GLU GLY PHE LYS LEU ASN ILE GLY
SEQRES 10 B 644 SER LYS GLY LEU GLU VAL ILE GLY ALA THR ASP ILE GLY
SEQRES 11 B 644 VAL PHE TYR GLY THR ARG SER VAL SER GLN MET LEU ARG
SEQRES 12 B 644 GLN GLY GLN LEU THR LEU PRO ALA GLY THR VAL ALA THR
SEQRES 13 B 644 LYS PRO LYS TYR LYS GLU ARG GLY ALA THR LEU CYS ALA
SEQRES 14 B 644 CYS GLN ILE ASN ILE SER THR ASP TRP ILE ASP ARG PHE
SEQRES 15 B 644 LEU SER ASP MET ALA ASP LEU ARG LEU ASN TYR VAL LEU
SEQRES 16 B 644 LEU GLU MET LYS LEU LYS PRO GLU GLU ASP ASN THR LYS
SEQRES 17 B 644 LYS ALA ALA THR TRP SER TYR TYR THR ARG ASP ASP VAL
SEQRES 18 B 644 LYS LYS PHE VAL LYS LYS ALA ASN ASN TYR GLY ILE ASP
SEQRES 19 B 644 VAL ILE PRO GLU ILE ASN SER PRO GLY HIS MET ASN VAL
SEQRES 20 B 644 TRP LEU GLU ASN TYR PRO GLU TYR GLN LEU ALA ASP ASN
SEQRES 21 B 644 SER GLY ARG LYS ASP PRO ASN LYS LEU ASP ILE SER ASN
SEQRES 22 B 644 PRO GLU ALA VAL LYS PHE TYR LYS THR LEU ILE ASP GLU
SEQRES 23 B 644 TYR ASP GLY VAL PHE THR THR LYS TYR TRP HIS MET GLY
SEQRES 24 B 644 ALA ASP GLU TYR MET ILE GLY THR SER PHE ASP ASN TYR
SEQRES 25 B 644 SER LYS LEU LYS THR PHE ALA GLU LYS GLN TYR GLY ALA
SEQRES 26 B 644 GLY ALA THR PRO ASN ASP ALA PHE THR GLY PHE ILE ASN
SEQRES 27 B 644 ASP ILE ASP LYS TYR VAL LYS ALA LYS GLY LYS GLN LEU
SEQRES 28 B 644 ARG ILE TRP ASN ASP GLY ILE VAL ASN THR LYS ASN VAL
SEQRES 29 B 644 SER LEU ASN LYS ASP ILE VAL ILE GLU TYR TRP TYR GLY
SEQRES 30 B 644 ALA GLY ARG LYS PRO GLN GLU LEU VAL GLN ASP GLY TYR
SEQRES 31 B 644 THR LEU MET ASN ALA THR GLN ALA LEU TYR TRP SER ARG
SEQRES 32 B 644 SER ALA GLN VAL TYR LYS VAL ASN ALA ALA ARG LEU TYR
SEQRES 33 B 644 ASN ASN ASN TRP ASN VAL GLY THR PHE ASP GLY GLY ARG
SEQRES 34 B 644 GLN ILE ASP LYS ASN TYR ASP LYS LEU THR GLY ALA LYS
SEQRES 35 B 644 VAL SER ILE TRP PRO ASP SER SER TYR PHE GLN THR GLU
SEQRES 36 B 644 ASN GLU VAL GLU LYS GLU ILE PHE ASP GLY MET ARG PHE
SEQRES 37 B 644 ILE SER GLN MET THR TRP SER ASP SER ARG PRO TRP ALA
SEQRES 38 B 644 THR TRP ASN ASP MET LYS ALA ASP ILE ASP LYS ILE GLY
SEQRES 39 B 644 TYR PRO LEU ASP ILE ARG GLU TYR ASP TYR THR PRO VAL
SEQRES 40 B 644 ASP ALA GLY ILE TYR ASP ILE PRO GLN LEU LYS SER ILE
SEQRES 41 B 644 SER LYS GLY PRO TRP GLU LEU ILE THR THR PRO ASP GLY
SEQRES 42 B 644 TYR TYR GLN MET LYS ASP THR VAL SER GLY LYS CYS LEU
SEQRES 43 B 644 ALA LEU PHE THR GLY SER LYS HIS LEU ASP VAL VAL THR
SEQRES 44 B 644 GLN VAL GLY ALA ARG PRO GLU LEU ARG ASN CYS ALA ASP
SEQRES 45 B 644 VAL SER VAL GLY GLN ASP GLN ARG ASN THR ALA ASN GLU
SEQRES 46 B 644 ARG ASN THR GLN LYS TRP GLN ILE ARG ALA ASP LYS ASP
SEQRES 47 B 644 GLY LYS TYR THR ILE SER PRO ALA LEU THR GLN GLN ARG
SEQRES 48 B 644 LEU ALA ILE ALA THR GLY ASN GLU GLN ASN ILE ASP LEU
SEQRES 49 B 644 GLU THR HIS ARG PRO ALA ALA GLY THR VAL ALA GLN PHE
SEQRES 50 B 644 PRO ALA ASP LEU VAL SER ASP
HET GAL A 701 11
HET NGT A 702 14
HET SO4 A 703 5
HET SO4 A 704 5
HET SO4 A 705 5
HET SO4 A 706 5
HET GAL B 701 11
HET NGT B 702 14
HET SO4 B 703 5
HET SO4 B 704 5
HET SO4 B 705 5
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM NGT 3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-
HETNAM 2 NGT TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL
HETNAM SO4 SULFATE ION
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 3 GAL 2(C6 H12 O6)
FORMUL 4 NGT 2(C8 H13 N O4 S)
FORMUL 5 SO4 7(O4 S 2-)
FORMUL 14 HOH *403(H2 O)
HELIX 1 1 LEU A 83 ASP A 99 1 17
HELIX 2 2 LYS A 122 GLY A 127 1 6
HELIX 3 3 THR A 146 ARG A 162 1 17
HELIX 4 4 SER A 194 LEU A 208 1 15
HELIX 5 5 THR A 226 ALA A 230 5 5
HELIX 6 6 THR A 236 TYR A 250 1 15
HELIX 7 7 MET A 264 GLU A 269 1 6
HELIX 8 8 TYR A 271 GLU A 273 5 3
HELIX 9 9 ASN A 292 GLY A 308 1 17
HELIX 10 10 SER A 327 ASN A 330 5 4
HELIX 11 11 TYR A 331 GLY A 343 1 13
HELIX 12 12 THR A 347 ALA A 365 1 19
HELIX 13 13 ASP A 375 ILE A 377 5 3
HELIX 14 14 LYS A 400 GLY A 408 1 9
HELIX 15 15 THR A 415 ALA A 417 5 3
HELIX 16 16 ASN A 430 ASN A 437 1 8
HELIX 17 17 SER A 468 GLN A 472 5 5
HELIX 18 18 THR A 473 SER A 494 1 22
HELIX 19 19 THR A 501 GLY A 513 1 13
HELIX 20 20 PRO A 515 TYR A 521 1 7
HELIX 21 21 ILE A 533 LYS A 537 5 5
HELIX 22 22 GLN A 598 ASN A 600 5 3
HELIX 23 23 THR A 601 THR A 607 1 7
HELIX 24 24 ASN A 640 HIS A 646 1 7
HELIX 25 25 PRO A 657 VAL A 661 5 5
HELIX 26 26 LEU B 83 ASP B 99 1 17
HELIX 27 27 LYS B 122 GLY B 127 1 6
HELIX 28 28 THR B 146 ARG B 162 1 17
HELIX 29 29 SER B 194 LEU B 208 1 15
HELIX 30 30 THR B 226 ALA B 230 5 5
HELIX 31 31 THR B 236 TYR B 250 1 15
HELIX 32 32 MET B 264 GLU B 269 1 6
HELIX 33 33 TYR B 271 GLU B 273 5 3
HELIX 34 34 ASN B 292 GLY B 308 1 17
HELIX 35 35 SER B 327 ASN B 330 5 4
HELIX 36 36 TYR B 331 GLY B 343 1 13
HELIX 37 37 THR B 347 ALA B 365 1 19
HELIX 38 38 ASP B 375 ILE B 377 5 3
HELIX 39 39 LYS B 400 GLY B 408 1 9
HELIX 40 40 THR B 415 ALA B 417 5 3
HELIX 41 41 ASN B 430 ASN B 437 1 8
HELIX 42 42 SER B 468 GLN B 472 5 5
HELIX 43 43 THR B 473 SER B 494 1 22
HELIX 44 44 THR B 501 GLY B 513 1 13
HELIX 45 45 PRO B 515 GLU B 520 1 6
HELIX 46 46 ILE B 533 LYS B 537 5 5
HELIX 47 47 GLN B 598 ASN B 600 5 3
HELIX 48 48 THR B 601 THR B 607 1 7
HELIX 49 49 ASN B 640 HIS B 646 1 7
HELIX 50 50 PRO B 657 VAL B 661 5 5
SHEET 1 A 4 VAL A 34 PRO A 35 0
SHEET 2 A 4 GLY B 529 ASP B 532 -1 O ASP B 532 N VAL A 34
SHEET 3 A 4 TRP B 544 THR B 548 -1 O LEU B 546 N GLY B 529
SHEET 4 A 4 TYR B 554 ASP B 558 -1 O LYS B 557 N GLU B 545
SHEET 1 B 8 GLY A 41 SER A 43 0
SHEET 2 B 8 THR A 63 THR A 70 -1 O THR A 70 N GLY A 41
SHEET 3 B 8 THR A 167 THR A 175 -1 O LEU A 168 N TRP A 69
SHEET 4 B 8 PHE A 131 GLY A 136 -1 N ILE A 135 O GLY A 171
SHEET 5 B 8 GLY A 139 GLY A 144 -1 O GLU A 141 N ASN A 134
SHEET 6 B 8 ILE A 114 LEU A 118 1 N SER A 115 O VAL A 142
SHEET 7 B 8 ARG A 76 VAL A 78 1 N VAL A 78 O ILE A 114
SHEET 8 B 8 LYS A 103 ALA A 105 1 O ALA A 105 N VAL A 77
SHEET 1 C10 TYR A 419 SER A 421 0
SHEET 2 C10 LEU A 457 TRP A 465 1 O SER A 463 N TRP A 420
SHEET 3 C10 LEU A 411 ASN A 413 1 N LEU A 411 O THR A 458
SHEET 4 C10 VAL A 390 TYR A 393 1 N TYR A 393 O MET A 412
SHEET 5 C10 GLN A 369 TRP A 373 1 N ILE A 372 O GLU A 392
SHEET 6 C10 TYR A 314 GLY A 318 1 N GLY A 318 O TRP A 373
SHEET 7 C10 ASP A 253 SER A 260 1 N SER A 260 O MET A 317
SHEET 8 C10 TYR A 212 GLU A 216 1 N VAL A 213 O ILE A 255
SHEET 9 C10 GLU A 181 CYS A 187 1 N LEU A 186 O LEU A 214
SHEET 10 C10 LEU A 457 TRP A 465 1 O ILE A 464 N THR A 185
SHEET 1 D 2 GLN A 275 ALA A 277 0
SHEET 2 D 2 LYS A 283 LEU A 288 -1 O LYS A 287 N LEU A 276
SHEET 1 E 2 THR A 443 PHE A 444 0
SHEET 2 E 2 ARG A 448 GLN A 449 -1 O ARG A 448 N PHE A 444
SHEET 1 F 4 TYR A 554 ASP A 558 0
SHEET 2 F 4 TRP A 544 THR A 548 -1 N GLU A 545 O LYS A 557
SHEET 3 F 4 GLY A 529 ASP A 532 -1 N GLY A 529 O LEU A 546
SHEET 4 F 4 VAL B 34 PRO B 35 -1 O VAL B 34 N ASP A 532
SHEET 1 G 2 CYS A 564 ALA A 566 0
SHEET 2 G 2 GLU A 585 ARG A 587 -1 O ARG A 587 N CYS A 564
SHEET 1 H 2 LYS A 572 HIS A 573 0
SHEET 2 H 2 VAL A 576 VAL A 577 -1 O VAL A 576 N HIS A 573
SHEET 1 I 2 TRP A 610 ALA A 614 0
SHEET 2 I 2 TYR A 620 PRO A 624 -1 O SER A 623 N GLN A 611
SHEET 1 J 2 ARG A 630 ILE A 633 0
SHEET 2 J 2 VAL A 653 PHE A 656 -1 O PHE A 656 N ARG A 630
SHEET 1 K 8 GLY B 41 SER B 43 0
SHEET 2 K 8 THR B 63 THR B 70 -1 O THR B 70 N GLY B 41
SHEET 3 K 8 THR B 167 THR B 175 -1 O LEU B 168 N TRP B 69
SHEET 4 K 8 PHE B 131 GLY B 136 -1 N ILE B 135 O GLY B 171
SHEET 5 K 8 GLY B 139 GLY B 144 -1 O GLU B 141 N ASN B 134
SHEET 6 K 8 ILE B 114 LEU B 118 1 N SER B 115 O VAL B 142
SHEET 7 K 8 ARG B 76 SER B 79 1 N VAL B 78 O ILE B 114
SHEET 8 K 8 LYS B 103 THR B 106 1 O LYS B 103 N VAL B 77
SHEET 1 L10 TYR B 419 SER B 421 0
SHEET 2 L10 LEU B 457 TRP B 465 1 O TRP B 465 N TRP B 420
SHEET 3 L10 LEU B 411 ASN B 413 1 N LEU B 411 O THR B 458
SHEET 4 L10 VAL B 390 TYR B 393 1 N TYR B 393 O MET B 412
SHEET 5 L10 GLN B 369 TRP B 373 1 N ILE B 372 O GLU B 392
SHEET 6 L10 TYR B 314 GLY B 318 1 N GLY B 318 O TRP B 373
SHEET 7 L10 ASP B 253 SER B 260 1 N SER B 260 O MET B 317
SHEET 8 L10 TYR B 212 GLU B 216 1 N LEU B 215 O ILE B 255
SHEET 9 L10 GLU B 181 CYS B 187 1 N LEU B 186 O LEU B 214
SHEET 10 L10 LEU B 457 TRP B 465 1 O VAL B 462 N THR B 185
SHEET 1 M 2 GLN B 275 ALA B 277 0
SHEET 2 M 2 LYS B 283 LEU B 288 -1 O LYS B 287 N LEU B 276
SHEET 1 N 2 THR B 443 PHE B 444 0
SHEET 2 N 2 ARG B 448 GLN B 449 -1 O ARG B 448 N PHE B 444
SHEET 1 O 2 CYS B 564 ALA B 566 0
SHEET 2 O 2 GLU B 585 ARG B 587 -1 O ARG B 587 N CYS B 564
SHEET 1 P 2 LYS B 572 HIS B 573 0
SHEET 2 P 2 VAL B 576 VAL B 577 -1 O VAL B 576 N HIS B 573
SHEET 1 Q 2 TRP B 610 ALA B 614 0
SHEET 2 Q 2 TYR B 620 PRO B 624 -1 O SER B 623 N GLN B 611
SHEET 1 R 2 ARG B 630 ILE B 633 0
SHEET 2 R 2 VAL B 653 PHE B 656 -1 O PHE B 656 N ARG B 630
SSBOND 1 CYS A 187 CYS A 189 1555 1555 2.07
SSBOND 2 CYS A 564 CYS A 589 1555 1555 2.18
SSBOND 3 CYS B 187 CYS B 189 1555 1555 2.06
SSBOND 4 CYS B 564 CYS B 589 1555 1555 2.15
LINK C1 GAL A 701 O3 NGT A 702 1555 1555 1.42
LINK C1 GAL B 701 O3 NGT B 702 1555 1555 1.42
CISPEP 1 VAL A 56 PRO A 57 0 -4.03
CISPEP 2 TRP A 232 SER A 233 0 10.14
CISPEP 3 SER A 260 PRO A 261 0 -1.77
CISPEP 4 GLY A 542 PRO A 543 0 12.34
CISPEP 5 LYS A 616 ASP A 617 0 -19.15
CISPEP 6 VAL B 56 PRO B 57 0 -3.05
CISPEP 7 GLY B 107 SER B 108 0 13.64
CISPEP 8 TRP B 232 SER B 233 0 -2.79
CISPEP 9 SER B 260 PRO B 261 0 4.49
CISPEP 10 GLY B 542 PRO B 543 0 8.19
CRYST1 116.524 131.557 104.762 90.00 90.00 90.00 P 21 21 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 0.008582 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009545 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
