HEADER ISOMERASE 15-MAR-02 1L7K
TITLE X-RAY STRUCTURE OF GALACTOSE MUTAROTASE FROM LACTOCOCCUS LACTIS
TITLE 2 COMPLEXED WITH GALACTOSE
CAVEAT 1L7K GLA A 500 HAS WRONG CHIRALITY AT ATOM C1 GLA B 501 HAS WRONG
CAVEAT 2 1L7K CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALACTOSE MUTAROTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALDOSE 1-EPIMERASE;
COMPND 5 EC: 5.1.3.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS;
SOURCE 3 ORGANISM_TAXID: 1358;
SOURCE 4 GENE: GALM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS MUTAROTASE, EPIMERASE, GALACTOSE METABOLISM, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.HOLDEN,J.B.THODEN
REVDAT 8 16-AUG-23 1L7K 1 REMARK
REVDAT 7 27-OCT-21 1L7K 1 SEQADV HETSYN
REVDAT 6 29-JUL-20 1L7K 1 CAVEAT COMPND REMARK SEQADV
REVDAT 6 2 1 HETNAM LINK SITE
REVDAT 5 11-OCT-17 1L7K 1 REMARK
REVDAT 4 24-FEB-09 1L7K 1 VERSN
REVDAT 3 01-APR-03 1L7K 1 JRNL
REVDAT 2 19-JUN-02 1L7K 1 JRNL
REVDAT 1 24-APR-02 1L7K 0
JRNL AUTH J.B.THODEN,H.M.HOLDEN
JRNL TITL HIGH RESOLUTION X-RAY STRUCTURE OF GALACTOSE MUTAROTASE FROM
JRNL TITL 2 LACTOCOCCUS LACTIS.
JRNL REF J.BIOL.CHEM. V. 277 20854 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11907040
JRNL DOI 10.1074/JBC.M111778200
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 51652
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5081
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1610
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1570
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 5081
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 51652
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5364
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 452
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.013 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.100 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : ENGH & HUBER
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GOEBEL OPTICS
REMARK 200 OPTICS : GOEBEL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : FRAMBO
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51652
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: PDB ENTRY 1L7J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-5000-O-METHYLETHER, SODIUM
REMARK 280 CHLORIDE, MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 22.60000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.25000
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 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 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 GLU A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 MET B 1
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 GLU A 56 CD GLU A 56 OE2 0.088
REMARK 500 GLU A 99 CD GLU A 99 OE2 0.067
REMARK 500 GLU A 100 CD GLU A 100 OE2 0.073
REMARK 500 GLU A 156 CD GLU A 156 OE2 0.073
REMARK 500 GLU A 184 CD GLU A 184 OE2 0.079
REMARK 500 GLU A 234 CD GLU A 234 OE1 -0.087
REMARK 500 GLU A 256 CD GLU A 256 OE2 0.067
REMARK 500 GLU A 292 CD GLU A 292 OE2 0.076
REMARK 500 GLU A 326 CD GLU A 326 OE2 0.077
REMARK 500 GLU B 99 CD GLU B 99 OE2 0.075
REMARK 500 GLU B 292 CD GLU B 292 OE2 0.071
REMARK 500 GLU B 316 CD GLU B 316 OE2 0.087
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 7 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 7 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 36 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 40 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP A 113 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 113 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 LYS A 136 CB - CA - C ANGL. DEV. = -14.2 DEGREES
REMARK 500 LYS A 136 N - CA - CB ANGL. DEV. = -18.1 DEGREES
REMARK 500 ASP A 146 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 146 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP A 147 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 147 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 148 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 148 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 160 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 160 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 178 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 178 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 189 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 200 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 200 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 211 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 218 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 249 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 249 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP A 272 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 272 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 285 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 6 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP B 7 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 7 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG B 33 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 ASP B 36 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP B 36 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP B 40 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 49 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP B 49 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 58 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP B 83 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 83 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP B 113 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP B 128 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP B 128 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 146 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 146 CB - CG - OD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP B 147 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 147 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 64 ANGLE DEVIATIONS.
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 32 61.06 38.76
REMARK 500 ASP A 58 112.83 -167.25
REMARK 500 ASP A 74 15.23 56.19
REMARK 500 THR A 163 -158.15 -157.34
REMARK 500 ASN A 166 67.80 -162.99
REMARK 500 ASN A 174 89.70 -167.91
REMARK 500 ASP A 200 -163.52 -167.43
REMARK 500 LYS A 240 40.52 71.25
REMARK 500 ASP A 243 59.95 -160.44
REMARK 500 ASP A 263 -128.13 61.43
REMARK 500 THR A 280 37.05 -93.78
REMARK 500 GLU A 292 -5.38 77.17
REMARK 500 GLN A 306 -175.44 -178.63
REMARK 500 LEU B 10 9.21 55.97
REMARK 500 LYS B 57 -62.34 -96.74
REMARK 500 SER B 101 -168.94 -79.34
REMARK 500 THR B 163 -159.89 -147.16
REMARK 500 ASN B 166 69.26 -168.20
REMARK 500 HIS B 170 31.21 -96.97
REMARK 500 ASP B 200 -167.45 -172.78
REMARK 500 ASP B 243 57.25 -161.15
REMARK 500 ASP B 263 -120.62 56.16
REMARK 500 THR B 280 39.60 -97.48
REMARK 500 ASN B 282 47.42 -81.14
REMARK 500 GLN B 306 -177.75 -172.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE O1 ATOM OF GAL HAS TWO ALTERNATE POSITIONS.
REMARK 600 ALTERNATE POSITION A IS FOR ALPHA-D-GALACTOSE.
REMARK 600 ALTERNATE POSITION B IS FOR BETA-D-GALACTOSE.
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 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 HOH A 507 O 90.7
REMARK 620 3 ASP B 13 OD1 163.7 74.4
REMARK 620 4 HIS B 346 NE2 93.7 73.2 88.1
REMARK 620 5 HOH B 504 O 89.1 177.7 106.1 104.6
REMARK 620 N 1 2 3 4
DBREF 1L7K A 1 339 UNP Q9ZB17 Q9ZB17_9LACT 1 339
DBREF 1L7K B 1 339 UNP Q9ZB17 Q9ZB17_9LACT 1 339
SEQADV 1L7K SER A 2 UNP Q9ZB17 GLU 2 ENGINEERED MUTATION
SEQADV 1L7K LEU A 340 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K GLU A 341 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS A 342 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS A 343 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS A 344 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS A 345 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS A 346 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS A 347 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K SER B 2 UNP Q9ZB17 GLU 2 ENGINEERED MUTATION
SEQADV 1L7K LEU B 340 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K GLU B 341 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS B 342 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS B 343 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS B 344 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS B 345 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS B 346 UNP Q9ZB17 EXPRESSION TAG
SEQADV 1L7K HIS B 347 UNP Q9ZB17 EXPRESSION TAG
SEQRES 1 A 347 MET SER ILE LYS ILE ARG ASP PHE GLY LEU GLY SER ASP
SEQRES 2 A 347 LEU ILE SER LEU THR ASN LYS ALA GLY VAL THR ILE SER
SEQRES 3 A 347 PHE THR ASN LEU GLY ALA ARG ILE VAL ASP TRP GLN LYS
SEQRES 4 A 347 ASP GLY LYS HIS LEU ILE LEU GLY PHE ASP SER ALA LYS
SEQRES 5 A 347 GLU TYR LEU GLU LYS ASP ALA TYR PRO GLY ALA THR VAL
SEQRES 6 A 347 GLY PRO THR ALA GLY ARG ILE LYS ASP GLY LEU VAL LYS
SEQRES 7 A 347 ILE SER GLY LYS ASP TYR ILE LEU ASN GLN ASN GLU GLY
SEQRES 8 A 347 PRO GLN THR LEU HIS GLY GLY GLU GLU SER ILE HIS THR
SEQRES 9 A 347 LYS LEU TRP THR TYR GLU VAL THR ASP LEU GLY ALA GLU
SEQRES 10 A 347 VAL GLN VAL LYS PHE SER LEU VAL SER ASN ASP GLY THR
SEQRES 11 A 347 ASN GLY TYR PRO GLY LYS ILE GLU MET SER VAL THR HIS
SEQRES 12 A 347 SER PHE ASP ASP ASP ASN LYS TRP LYS ILE HIS TYR GLU
SEQRES 13 A 347 ALA ILE SER ASP LYS ASP THR VAL PHE ASN PRO THR GLY
SEQRES 14 A 347 HIS VAL TYR PHE ASN LEU ASN GLY ASP ALA SER GLU SER
SEQRES 15 A 347 VAL GLU ASN HIS GLY LEU ARG LEU ALA ALA SER ARG PHE
SEQRES 16 A 347 VAL PRO LEU LYS ASP GLN THR GLU ILE VAL ARG GLY ASP
SEQRES 17 A 347 ILE VAL ASP ILE LYS ASN THR ASP LEU ASP PHE ARG GLN
SEQRES 18 A 347 GLU LYS GLN LEU SER ASN ALA PHE ASN SER ASN MET GLU
SEQRES 19 A 347 GLN VAL GLN LEU VAL LYS GLY ILE ASP HIS PRO PHE LEU
SEQRES 20 A 347 LEU ASP GLN LEU GLY LEU ASP LYS GLU GLN ALA ARG LEU
SEQRES 21 A 347 THR LEU ASP ASP THR SER ILE SER VAL PHE THR ASP GLN
SEQRES 22 A 347 PRO SER ILE VAL ILE PHE THR ALA ASN PHE GLY ASP LEU
SEQRES 23 A 347 GLY THR LEU TYR HIS GLU LYS LYS GLN VAL HIS HIS GLY
SEQRES 24 A 347 GLY ILE THR PHE GLU CYS GLN VAL SER PRO GLY SER GLU
SEQRES 25 A 347 GLN ILE PRO GLU LEU GLY ASP ILE SER LEU LYS ALA GLY
SEQRES 26 A 347 GLU LYS TYR GLN ALA THR THR ILE TYR SER LEU HIS THR
SEQRES 27 A 347 LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 347 MET SER ILE LYS ILE ARG ASP PHE GLY LEU GLY SER ASP
SEQRES 2 B 347 LEU ILE SER LEU THR ASN LYS ALA GLY VAL THR ILE SER
SEQRES 3 B 347 PHE THR ASN LEU GLY ALA ARG ILE VAL ASP TRP GLN LYS
SEQRES 4 B 347 ASP GLY LYS HIS LEU ILE LEU GLY PHE ASP SER ALA LYS
SEQRES 5 B 347 GLU TYR LEU GLU LYS ASP ALA TYR PRO GLY ALA THR VAL
SEQRES 6 B 347 GLY PRO THR ALA GLY ARG ILE LYS ASP GLY LEU VAL LYS
SEQRES 7 B 347 ILE SER GLY LYS ASP TYR ILE LEU ASN GLN ASN GLU GLY
SEQRES 8 B 347 PRO GLN THR LEU HIS GLY GLY GLU GLU SER ILE HIS THR
SEQRES 9 B 347 LYS LEU TRP THR TYR GLU VAL THR ASP LEU GLY ALA GLU
SEQRES 10 B 347 VAL GLN VAL LYS PHE SER LEU VAL SER ASN ASP GLY THR
SEQRES 11 B 347 ASN GLY TYR PRO GLY LYS ILE GLU MET SER VAL THR HIS
SEQRES 12 B 347 SER PHE ASP ASP ASP ASN LYS TRP LYS ILE HIS TYR GLU
SEQRES 13 B 347 ALA ILE SER ASP LYS ASP THR VAL PHE ASN PRO THR GLY
SEQRES 14 B 347 HIS VAL TYR PHE ASN LEU ASN GLY ASP ALA SER GLU SER
SEQRES 15 B 347 VAL GLU ASN HIS GLY LEU ARG LEU ALA ALA SER ARG PHE
SEQRES 16 B 347 VAL PRO LEU LYS ASP GLN THR GLU ILE VAL ARG GLY ASP
SEQRES 17 B 347 ILE VAL ASP ILE LYS ASN THR ASP LEU ASP PHE ARG GLN
SEQRES 18 B 347 GLU LYS GLN LEU SER ASN ALA PHE ASN SER ASN MET GLU
SEQRES 19 B 347 GLN VAL GLN LEU VAL LYS GLY ILE ASP HIS PRO PHE LEU
SEQRES 20 B 347 LEU ASP GLN LEU GLY LEU ASP LYS GLU GLN ALA ARG LEU
SEQRES 21 B 347 THR LEU ASP ASP THR SER ILE SER VAL PHE THR ASP GLN
SEQRES 22 B 347 PRO SER ILE VAL ILE PHE THR ALA ASN PHE GLY ASP LEU
SEQRES 23 B 347 GLY THR LEU TYR HIS GLU LYS LYS GLN VAL HIS HIS GLY
SEQRES 24 B 347 GLY ILE THR PHE GLU CYS GLN VAL SER PRO GLY SER GLU
SEQRES 25 B 347 GLN ILE PRO GLU LEU GLY ASP ILE SER LEU LYS ALA GLY
SEQRES 26 B 347 GLU LYS TYR GLN ALA THR THR ILE TYR SER LEU HIS THR
SEQRES 27 B 347 LYS LEU GLU HIS HIS HIS HIS HIS HIS
HET GLA A 500 13
HET NA A 501 1
HET GLA B 501 13
HETNAM GLA ALPHA-D-GALACTOPYRANOSE
HETNAM NA SODIUM ION
HETSYN GLA ALPHA-D-GALACTOSE; D-GALACTOSE; GALACTOSE; ALPHA D-
HETSYN 2 GLA GALACTOSE
FORMUL 3 GLA 2(C6 H12 O6)
FORMUL 4 NA NA 1+
FORMUL 6 HOH *452(H2 O)
HELIX 1 1 SER A 50 LYS A 57 1 8
HELIX 2 2 SER A 101 LYS A 105 5 5
HELIX 3 3 GLY A 129 TYR A 133 5 5
HELIX 4 4 SER A 182 ASN A 185 5 4
HELIX 5 5 LEU A 225 ASN A 230 1 6
HELIX 6 6 MET A 233 LYS A 240 1 8
HELIX 7 7 ILE A 314 GLY A 318 5 5
HELIX 8 8 SER B 50 LYS B 57 1 8
HELIX 9 9 SER B 101 LYS B 105 5 5
HELIX 10 10 GLY B 129 TYR B 133 5 5
HELIX 11 11 SER B 182 ASN B 185 5 4
HELIX 12 12 LEU B 225 ASN B 230 1 6
HELIX 13 13 MET B 233 LYS B 240 1 8
HELIX 14 14 ILE B 314 GLY B 318 5 5
SHEET 1 A 5 ILE A 3 GLY A 9 0
SHEET 2 A 5 SER A 12 THR A 18 -1 O SER A 16 N LYS A 4
SHEET 3 A 5 THR A 24 THR A 28 -1 O ILE A 25 N LEU A 17
SHEET 4 A 5 ARG A 33 LYS A 39 -1 O VAL A 35 N SER A 26
SHEET 5 A 5 LYS A 42 HIS A 43 -1 O LYS A 42 N LYS A 39
SHEET 1 B 2 THR A 64 VAL A 65 0
SHEET 2 B 2 THR A 168 GLY A 169 -1 O THR A 168 N VAL A 65
SHEET 1 C 2 ARG A 71 ILE A 72 0
SHEET 2 C 2 THR A 94 LEU A 95 -1 O THR A 94 N ILE A 72
SHEET 1 D 2 LEU A 76 ILE A 79 0
SHEET 2 D 2 LYS A 82 ILE A 85 -1 O LYS A 82 N ILE A 79
SHEET 1 E 9 THR A 108 ASP A 113 0
SHEET 2 E 9 GLU A 117 SER A 126 -1 O GLN A 119 N THR A 112
SHEET 3 E 9 ILE A 137 ASP A 146 -1 O VAL A 141 N PHE A 122
SHEET 4 E 9 LYS A 150 SER A 159 -1 O ILE A 158 N GLU A 138
SHEET 5 E 9 TYR A 328 THR A 338 -1 O TYR A 334 N TRP A 151
SHEET 6 E 9 THR A 265 THR A 271 -1 N PHE A 270 O ILE A 333
SHEET 7 E 9 ALA A 258 LEU A 262 -1 N LEU A 260 O ILE A 267
SHEET 8 E 9 GLY A 187 LEU A 190 -1 N GLY A 187 O THR A 261
SHEET 9 E 9 LYS A 223 GLN A 224 -1 O LYS A 223 N LEU A 188
SHEET 1 F 2 THR A 163 VAL A 164 0
SHEET 2 F 2 SER A 321 LEU A 322 -1 O LEU A 322 N THR A 163
SHEET 1 G 2 TYR A 172 PHE A 173 0
SHEET 2 G 2 ILE A 301 THR A 302 -1 O ILE A 301 N PHE A 173
SHEET 1 H 5 VAL A 210 ASP A 211 0
SHEET 2 H 5 ALA A 192 PHE A 195 -1 N PHE A 195 O VAL A 210
SHEET 3 H 5 ASP A 243 LEU A 248 -1 O LEU A 247 N ARG A 194
SHEET 4 H 5 SER A 275 PHE A 279 -1 O ILE A 278 N HIS A 244
SHEET 5 H 5 GLU A 304 GLN A 306 -1 O GLU A 304 N VAL A 277
SHEET 1 I 2 LEU A 289 TYR A 290 0
SHEET 2 I 2 LYS A 293 LYS A 294 -1 O LYS A 293 N TYR A 290
SHEET 1 J 5 ILE B 3 GLY B 9 0
SHEET 2 J 5 SER B 12 THR B 18 -1 O SER B 16 N LYS B 4
SHEET 3 J 5 THR B 24 THR B 28 -1 O ILE B 25 N LEU B 17
SHEET 4 J 5 ARG B 33 LYS B 39 -1 O VAL B 35 N SER B 26
SHEET 5 J 5 LYS B 42 HIS B 43 -1 O LYS B 42 N LYS B 39
SHEET 1 K 2 THR B 64 VAL B 65 0
SHEET 2 K 2 THR B 168 GLY B 169 -1 O THR B 168 N VAL B 65
SHEET 1 L 2 ARG B 71 ILE B 72 0
SHEET 2 L 2 THR B 94 LEU B 95 -1 O THR B 94 N ILE B 72
SHEET 1 M 2 LEU B 76 ILE B 79 0
SHEET 2 M 2 LYS B 82 ILE B 85 -1 O LYS B 82 N ILE B 79
SHEET 1 N 9 THR B 108 ASP B 113 0
SHEET 2 N 9 GLU B 117 SER B 126 -1 O GLN B 119 N THR B 112
SHEET 3 N 9 ILE B 137 ASP B 146 -1 O HIS B 143 N VAL B 120
SHEET 4 N 9 LYS B 150 SER B 159 -1 O ILE B 158 N GLU B 138
SHEET 5 N 9 TYR B 328 THR B 338 -1 O TYR B 328 N ALA B 157
SHEET 6 N 9 THR B 265 THR B 271 -1 N PHE B 270 O ILE B 333
SHEET 7 N 9 ALA B 258 LEU B 262 -1 N ALA B 258 O VAL B 269
SHEET 8 N 9 GLY B 187 LEU B 190 -1 N GLY B 187 O THR B 261
SHEET 9 N 9 LYS B 223 GLN B 224 -1 O LYS B 223 N LEU B 188
SHEET 1 O 2 THR B 163 VAL B 164 0
SHEET 2 O 2 SER B 321 LEU B 322 -1 O LEU B 322 N THR B 163
SHEET 1 P 2 TYR B 172 PHE B 173 0
SHEET 2 P 2 ILE B 301 THR B 302 -1 O ILE B 301 N PHE B 173
SHEET 1 Q 5 VAL B 210 ASP B 211 0
SHEET 2 Q 5 ALA B 192 PHE B 195 -1 N PHE B 195 O VAL B 210
SHEET 3 Q 5 ASP B 243 LEU B 248 -1 O LEU B 247 N ARG B 194
SHEET 4 Q 5 SER B 275 PHE B 279 -1 O ILE B 278 N HIS B 244
SHEET 5 Q 5 GLU B 304 GLN B 306 -1 O GLU B 304 N VAL B 277
SHEET 1 R 2 LEU B 289 TYR B 290 0
SHEET 2 R 2 LYS B 293 LYS B 294 -1 O LYS B 293 N TYR B 290
LINK OD1 ASP A 13 NA NA A 501 1555 1555 2.35
LINK NA NA A 501 O HOH A 507 1555 1555 2.61
LINK NA NA A 501 OD1 ASP B 13 1555 1555 2.37
LINK NA NA A 501 NE2 HIS B 346 1555 3655 2.45
LINK NA NA A 501 O HOH B 504 1555 1555 2.45
CISPEP 1 GLY A 66 PRO A 67 0 1.64
CISPEP 2 GLY A 135 LYS A 136 0 -1.92
CISPEP 3 GLY B 66 PRO B 67 0 0.92
CISPEP 4 GLY B 135 LYS B 136 0 1.16
CRYST1 45.200 76.500 211.600 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 0.022124 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013072 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004726 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
