HEADER ECOLI 10-APR-97 1AHP
TITLE OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN
TITLE 2 PHSPHORYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E.COLI MALTODEXTRIN PHOSPHORYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MALP;
COMPND 5 EC: 2.4.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: PYRIDOXAL PHOSPHATE COFACTOR ATTACHED TO LYS 645
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM
KEYWDS ECOLI, PHOSPHORYLASE, OLIGOSACCHARIDE, INDUCED-FIT, SUBSTRATE,
KEYWDS 2 MALTODEXTRIN, STACKING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.O'REILLY,K.A.WATSON,R.SCHINZEL,D.PALM,L.N.JOHNSON
REVDAT 4 13-JUL-11 1AHP 1 VERSN
REVDAT 3 24-FEB-09 1AHP 1 VERSN
REVDAT 2 01-APR-03 1AHP 1 JRNL
REVDAT 1 15-OCT-97 1AHP 0
JRNL AUTH M.O'REILLY,K.A.WATSON,R.SCHINZEL,D.PALM,L.N.JOHNSON
JRNL TITL OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI
JRNL TITL 2 MALTODEXTRIN PHOSPHORYLASE.
JRNL REF NAT.STRUCT.BIOL. V. 4 405 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9145112
JRNL DOI 10.1038/NSB0597-405
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 73.0
REMARK 3 NUMBER OF REFLECTIONS : 29121
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 SET) : 0.232
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 608
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.017
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2844
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 59
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12732
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.30
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUPED B
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : STRICT
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : SO4.PARAM
REMARK 3 PARAMETER FILE 3 : PLP.PARAM
REMARK 3 PARAMETER FILE 4 : OLI.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : SO4.TOP
REMARK 3 TOPOLOGY FILE 3 : PLP.TOP
REMARK 3 TOPOLOGY FILE 4 : OLI.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 COORDINATES FOR MOLECULE A WERE PROVIDED BY THE DEPOSITOR.
REMARK 3 MOLECULE B WAS GENERATED BY THE PDB USING NCS SYMMETRY.
REMARK 4
REMARK 4 1AHP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-95
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33108
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.7
REMARK 200 DATA REDUNDANCY : 1.600
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.00
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: MALP NATIVE STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NATARTRATE, PH 6.4, 24% PEG 3350,
REMARK 280 1MM SODIUM AZIDE, 16 DEG CELCIUS, 50MM MALTOHEXAOSE STOCK,
REMARK 280 16.5MG/ML PROTEIN STOCK, HANGING DROPS 1MICRO LITRE WELL & 0.5
REMARK 280 MICRO LITRE MALTOHEXAOSE 0.5 MICRO LITRE PROTEIN, VAPOR DIFFUSION
REMARK 280 - HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 86.60000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 86.60000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 56.20000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 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 0
REMARK 465 MET B 0
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 998
DBREF 1AHP A 1 796 UNP P00490 PHSM_ECOLI 1 796
DBREF 1AHP B 1 796 UNP P00490 PHSM_ECOLI 1 796
SEQADV 1AHP ALA A 112 UNP P00490 ASN 112 ENGINEERED
SEQADV 1AHP ALA A 184 UNP P00490 LYS 184 CONFLICT
SEQADV 1AHP ASP A 497 UNP P00490 GLN 497 CONFLICT
SEQADV 1AHP ARG A 547 UNP P00490 HIS 547 CONFLICT
SEQADV 1AHP LYS A 681 UNP P00490 GLU 681 CONFLICT
SEQADV 1AHP ALA A 795 UNP P00490 LYS 795 CONFLICT
SEQADV 1AHP ALA B 112 UNP P00490 ASN 112 ENGINEERED
SEQADV 1AHP ALA B 184 UNP P00490 LYS 184 CONFLICT
SEQADV 1AHP ASP B 497 UNP P00490 GLN 497 CONFLICT
SEQADV 1AHP ARG B 547 UNP P00490 HIS 547 CONFLICT
SEQADV 1AHP LYS B 681 UNP P00490 GLU 681 CONFLICT
SEQADV 1AHP ALA B 795 UNP P00490 LYS 795 CONFLICT
SEQRES 1 A 797 MET SER GLN PRO ILE PHE ASN ASP LYS GLN PHE GLN GLU
SEQRES 2 A 797 ALA LEU SER ARG GLN TRP GLN ARG TYR GLY LEU ASN SER
SEQRES 3 A 797 ALA ALA GLU MET THR PRO ARG GLN TRP TRP LEU ALA VAL
SEQRES 4 A 797 SER GLU ALA LEU ALA GLU MET LEU ARG ALA GLN PRO PHE
SEQRES 5 A 797 ALA LYS PRO VAL ALA ASN GLN ARG HIS VAL ASN TYR ILE
SEQRES 6 A 797 SER MET GLU PHE LEU ILE GLY ARG LEU THR GLY ASN ASN
SEQRES 7 A 797 LEU LEU ASN LEU GLY TRP TYR GLN ASP VAL GLN ASP SER
SEQRES 8 A 797 LEU LYS ALA TYR ASP ILE ASN LEU THR ASP LEU LEU GLU
SEQRES 9 A 797 GLU GLU ILE ASP PRO ALA LEU GLY ALA GLY GLY LEU GLY
SEQRES 10 A 797 ARG LEU ALA ALA CYS PHE LEU ASP SER MET ALA THR VAL
SEQRES 11 A 797 GLY GLN SER ALA THR GLY TYR GLY LEU ASN TYR GLN TYR
SEQRES 12 A 797 GLY LEU PHE ARG GLN SER PHE VAL ASP GLY LYS GLN VAL
SEQRES 13 A 797 GLU ALA PRO ASP ASP TRP HIS ARG SER ASN TYR PRO TRP
SEQRES 14 A 797 PHE ARG HIS ASN GLU ALA LEU ASP VAL GLN VAL GLY ILE
SEQRES 15 A 797 GLY GLY ALA VAL THR LYS ASP GLY ARG TRP GLU PRO GLU
SEQRES 16 A 797 PHE THR ILE THR GLY GLN ALA TRP ASP LEU PRO VAL VAL
SEQRES 17 A 797 GLY TYR ARG ASN GLY VAL ALA GLN PRO LEU ARG LEU TRP
SEQRES 18 A 797 GLN ALA THR HIS ALA HIS PRO PHE ASP LEU THR LYS PHE
SEQRES 19 A 797 ASN ASP GLY ASP PHE LEU ARG ALA GLU GLN GLN GLY ILE
SEQRES 20 A 797 ASN ALA GLU LYS LEU THR LYS VAL LEU TYR PRO ASN ASP
SEQRES 21 A 797 ASN HIS THR ALA GLY LYS LYS LEU ARG LEU MET GLN GLN
SEQRES 22 A 797 TYR PHE GLN CYS ALA CYS SER VAL ALA ASP ILE LEU ARG
SEQRES 23 A 797 ARG HIS HIS LEU ALA GLY ARG GLU LEU HIS GLU LEU ALA
SEQRES 24 A 797 ASP TYR GLU VAL ILE GLN LEU ASN ASP THR HIS PRO THR
SEQRES 25 A 797 ILE ALA ILE PRO GLU LEU LEU ARG VAL LEU ILE ASP GLU
SEQRES 26 A 797 HIS GLN MET SER TRP ASP ASP ALA TRP ALA ILE THR SER
SEQRES 27 A 797 LYS THR PHE ALA TYR THR ASN HIS THR LEU MET PRO GLU
SEQRES 28 A 797 ALA LEU GLU ARG TRP ASP VAL LYS LEU VAL LYS GLY LEU
SEQRES 29 A 797 LEU PRO ARG HIS MET GLN ILE ILE ASN GLU ILE ASN THR
SEQRES 30 A 797 ARG PHE LYS THR LEU VAL GLU LYS THR TRP PRO GLY ASP
SEQRES 31 A 797 GLU LYS VAL TRP ALA LYS LEU ALA VAL VAL HIS ASP LYS
SEQRES 32 A 797 GLN VAL HIS MET ALA ASN LEU CYS VAL VAL GLY GLY PHE
SEQRES 33 A 797 ALA VAL ASN GLY VAL ALA ALA LEU HIS SER ASP LEU VAL
SEQRES 34 A 797 VAL LYS ASP LEU PHE PRO GLU TYR HIS GLN LEU TRP PRO
SEQRES 35 A 797 ASN LYS PHE HIS ASN VAL THR ASN GLY ILE THR PRO ARG
SEQRES 36 A 797 ARG TRP ILE LYS GLN CYS ASN PRO ALA LEU ALA ALA LEU
SEQRES 37 A 797 LEU ASP LYS SER LEU GLN LYS GLU TRP ALA ASN ASP LEU
SEQRES 38 A 797 ASP GLN LEU ILE ASN LEU VAL LYS LEU ALA ASP ASP ALA
SEQRES 39 A 797 LYS PHE ARG ASP LEU TYR ARG VAL ILE LYS GLN ALA ASN
SEQRES 40 A 797 LYS VAL ARG LEU ALA GLU PHE VAL LYS VAL ARG THR GLY
SEQRES 41 A 797 ILE ASP ILE ASN PRO GLN ALA ILE PHE ASP ILE GLN ILE
SEQRES 42 A 797 LYS ARG LEU HIS GLU TYR LYS ARG GLN HIS LEU ASN LEU
SEQRES 43 A 797 LEU ARG ILE LEU ALA LEU TYR LYS GLU ILE ARG GLU ASN
SEQRES 44 A 797 PRO GLN ALA ASP ARG VAL PRO ARG VAL PHE LEU PHE GLY
SEQRES 45 A 797 ALA LYS ALA ALA PRO GLY TYR TYR LEU ALA LYS ASN ILE
SEQRES 46 A 797 ILE PHE ALA ILE ASN LYS VAL ALA ASP VAL ILE ASN ASN
SEQRES 47 A 797 ASP PRO LEU VAL GLY ASP LYS LEU LYS VAL VAL PHE LEU
SEQRES 48 A 797 PRO ASP TYR CYS VAL SER ALA ALA GLU LYS LEU ILE PRO
SEQRES 49 A 797 ALA ALA ASP ILE SER GLU GLN ILE SER THR ALA GLY LYS
SEQRES 50 A 797 GLU ALA SER GLY THR GLY ASN MET LYS LEU ALA LEU ASN
SEQRES 51 A 797 GLY ALA LEU THR VAL GLY THR LEU ASP GLY ALA ASN VAL
SEQRES 52 A 797 GLU ILE ALA GLU LYS VAL GLY GLU GLU ASN ILE PHE ILE
SEQRES 53 A 797 PHE GLY HIS THR VAL LYS GLN VAL LYS ALA ILE LEU ALA
SEQRES 54 A 797 LYS GLY TYR ASP PRO VAL LYS TRP ARG LYS LYS ASP LYS
SEQRES 55 A 797 VAL LEU ASP ALA VAL LEU LYS GLU LEU GLU SER GLY LYS
SEQRES 56 A 797 TYR SER ASP GLY ASP LYS HIS ALA PHE ASP GLN MET LEU
SEQRES 57 A 797 HIS SER ILE GLY LYS GLN GLY GLY ASP PRO TYR LEU VAL
SEQRES 58 A 797 MET ALA ASP PHE ALA ALA TYR VAL GLU ALA GLN LYS GLN
SEQRES 59 A 797 VAL ASP VAL LEU TYR ARG ASP GLN GLU ALA TRP THR ARG
SEQRES 60 A 797 ALA ALA ILE LEU ASN THR ALA ARG CYS GLY MET PHE SER
SEQRES 61 A 797 SER ASP ARG SER ILE ARG ASP TYR GLN ALA ARG ILE TRP
SEQRES 62 A 797 GLN ALA ALA ARG
SEQRES 1 B 797 MET SER GLN PRO ILE PHE ASN ASP LYS GLN PHE GLN GLU
SEQRES 2 B 797 ALA LEU SER ARG GLN TRP GLN ARG TYR GLY LEU ASN SER
SEQRES 3 B 797 ALA ALA GLU MET THR PRO ARG GLN TRP TRP LEU ALA VAL
SEQRES 4 B 797 SER GLU ALA LEU ALA GLU MET LEU ARG ALA GLN PRO PHE
SEQRES 5 B 797 ALA LYS PRO VAL ALA ASN GLN ARG HIS VAL ASN TYR ILE
SEQRES 6 B 797 SER MET GLU PHE LEU ILE GLY ARG LEU THR GLY ASN ASN
SEQRES 7 B 797 LEU LEU ASN LEU GLY TRP TYR GLN ASP VAL GLN ASP SER
SEQRES 8 B 797 LEU LYS ALA TYR ASP ILE ASN LEU THR ASP LEU LEU GLU
SEQRES 9 B 797 GLU GLU ILE ASP PRO ALA LEU GLY ALA GLY GLY LEU GLY
SEQRES 10 B 797 ARG LEU ALA ALA CYS PHE LEU ASP SER MET ALA THR VAL
SEQRES 11 B 797 GLY GLN SER ALA THR GLY TYR GLY LEU ASN TYR GLN TYR
SEQRES 12 B 797 GLY LEU PHE ARG GLN SER PHE VAL ASP GLY LYS GLN VAL
SEQRES 13 B 797 GLU ALA PRO ASP ASP TRP HIS ARG SER ASN TYR PRO TRP
SEQRES 14 B 797 PHE ARG HIS ASN GLU ALA LEU ASP VAL GLN VAL GLY ILE
SEQRES 15 B 797 GLY GLY ALA VAL THR LYS ASP GLY ARG TRP GLU PRO GLU
SEQRES 16 B 797 PHE THR ILE THR GLY GLN ALA TRP ASP LEU PRO VAL VAL
SEQRES 17 B 797 GLY TYR ARG ASN GLY VAL ALA GLN PRO LEU ARG LEU TRP
SEQRES 18 B 797 GLN ALA THR HIS ALA HIS PRO PHE ASP LEU THR LYS PHE
SEQRES 19 B 797 ASN ASP GLY ASP PHE LEU ARG ALA GLU GLN GLN GLY ILE
SEQRES 20 B 797 ASN ALA GLU LYS LEU THR LYS VAL LEU TYR PRO ASN ASP
SEQRES 21 B 797 ASN HIS THR ALA GLY LYS LYS LEU ARG LEU MET GLN GLN
SEQRES 22 B 797 TYR PHE GLN CYS ALA CYS SER VAL ALA ASP ILE LEU ARG
SEQRES 23 B 797 ARG HIS HIS LEU ALA GLY ARG GLU LEU HIS GLU LEU ALA
SEQRES 24 B 797 ASP TYR GLU VAL ILE GLN LEU ASN ASP THR HIS PRO THR
SEQRES 25 B 797 ILE ALA ILE PRO GLU LEU LEU ARG VAL LEU ILE ASP GLU
SEQRES 26 B 797 HIS GLN MET SER TRP ASP ASP ALA TRP ALA ILE THR SER
SEQRES 27 B 797 LYS THR PHE ALA TYR THR ASN HIS THR LEU MET PRO GLU
SEQRES 28 B 797 ALA LEU GLU ARG TRP ASP VAL LYS LEU VAL LYS GLY LEU
SEQRES 29 B 797 LEU PRO ARG HIS MET GLN ILE ILE ASN GLU ILE ASN THR
SEQRES 30 B 797 ARG PHE LYS THR LEU VAL GLU LYS THR TRP PRO GLY ASP
SEQRES 31 B 797 GLU LYS VAL TRP ALA LYS LEU ALA VAL VAL HIS ASP LYS
SEQRES 32 B 797 GLN VAL HIS MET ALA ASN LEU CYS VAL VAL GLY GLY PHE
SEQRES 33 B 797 ALA VAL ASN GLY VAL ALA ALA LEU HIS SER ASP LEU VAL
SEQRES 34 B 797 VAL LYS ASP LEU PHE PRO GLU TYR HIS GLN LEU TRP PRO
SEQRES 35 B 797 ASN LYS PHE HIS ASN VAL THR ASN GLY ILE THR PRO ARG
SEQRES 36 B 797 ARG TRP ILE LYS GLN CYS ASN PRO ALA LEU ALA ALA LEU
SEQRES 37 B 797 LEU ASP LYS SER LEU GLN LYS GLU TRP ALA ASN ASP LEU
SEQRES 38 B 797 ASP GLN LEU ILE ASN LEU VAL LYS LEU ALA ASP ASP ALA
SEQRES 39 B 797 LYS PHE ARG ASP LEU TYR ARG VAL ILE LYS GLN ALA ASN
SEQRES 40 B 797 LYS VAL ARG LEU ALA GLU PHE VAL LYS VAL ARG THR GLY
SEQRES 41 B 797 ILE ASP ILE ASN PRO GLN ALA ILE PHE ASP ILE GLN ILE
SEQRES 42 B 797 LYS ARG LEU HIS GLU TYR LYS ARG GLN HIS LEU ASN LEU
SEQRES 43 B 797 LEU ARG ILE LEU ALA LEU TYR LYS GLU ILE ARG GLU ASN
SEQRES 44 B 797 PRO GLN ALA ASP ARG VAL PRO ARG VAL PHE LEU PHE GLY
SEQRES 45 B 797 ALA LYS ALA ALA PRO GLY TYR TYR LEU ALA LYS ASN ILE
SEQRES 46 B 797 ILE PHE ALA ILE ASN LYS VAL ALA ASP VAL ILE ASN ASN
SEQRES 47 B 797 ASP PRO LEU VAL GLY ASP LYS LEU LYS VAL VAL PHE LEU
SEQRES 48 B 797 PRO ASP TYR CYS VAL SER ALA ALA GLU LYS LEU ILE PRO
SEQRES 49 B 797 ALA ALA ASP ILE SER GLU GLN ILE SER THR ALA GLY LYS
SEQRES 50 B 797 GLU ALA SER GLY THR GLY ASN MET LYS LEU ALA LEU ASN
SEQRES 51 B 797 GLY ALA LEU THR VAL GLY THR LEU ASP GLY ALA ASN VAL
SEQRES 52 B 797 GLU ILE ALA GLU LYS VAL GLY GLU GLU ASN ILE PHE ILE
SEQRES 53 B 797 PHE GLY HIS THR VAL LYS GLN VAL LYS ALA ILE LEU ALA
SEQRES 54 B 797 LYS GLY TYR ASP PRO VAL LYS TRP ARG LYS LYS ASP LYS
SEQRES 55 B 797 VAL LEU ASP ALA VAL LEU LYS GLU LEU GLU SER GLY LYS
SEQRES 56 B 797 TYR SER ASP GLY ASP LYS HIS ALA PHE ASP GLN MET LEU
SEQRES 57 B 797 HIS SER ILE GLY LYS GLN GLY GLY ASP PRO TYR LEU VAL
SEQRES 58 B 797 MET ALA ASP PHE ALA ALA TYR VAL GLU ALA GLN LYS GLN
SEQRES 59 B 797 VAL ASP VAL LEU TYR ARG ASP GLN GLU ALA TRP THR ARG
SEQRES 60 B 797 ALA ALA ILE LEU ASN THR ALA ARG CYS GLY MET PHE SER
SEQRES 61 B 797 SER ASP ARG SER ILE ARG ASP TYR GLN ALA ARG ILE TRP
SEQRES 62 B 797 GLN ALA ALA ARG
HET MAL A1006 23
HET MAL B1006 23
HET SO4 A 997 5
HET SO4 B 997 5
HET PLP A 999 15
HET PLP B 999 15
HET GOL A 998 6
HET GOL B 998 6
HETNAM MAL MALTOSE
HETNAM SO4 SULFATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM GOL GLYCEROL
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MAL 2(C12 H22 O11)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 PLP 2(C8 H10 N O6 P)
FORMUL 9 GOL 2(C3 H8 O3)
HELIX 1 1 ASP A 7 TYR A 21 1 15
HELIX 2 2 ALA A 26 GLU A 28 5 3
HELIX 3 3 PRO A 31 ALA A 48 1 18
HELIX 4 4 THR A 74 LEU A 81 1 8
HELIX 5 5 TRP A 83 TYR A 94 1 12
HELIX 6 6 LEU A 98 GLU A 104 1 7
HELIX 7 7 GLY A 114 VAL A 129 1 16
HELIX 8 8 ARG A 163 ASN A 165 5 3
HELIX 9 9 GLU A 173 LEU A 175 5 3
HELIX 10 10 LEU A 230 ASN A 234 1 5
HELIX 11 11 PHE A 238 THR A 252 1 15
HELIX 12 12 THR A 262 LEU A 289 1 28
HELIX 13 13 LEU A 297 TYR A 300 1 4
HELIX 14 14 PRO A 310 HIS A 325 5 16
HELIX 15 15 TRP A 329 THR A 339 1 11
HELIX 16 16 PRO A 349 ALA A 351 5 3
HELIX 17 17 VAL A 357 LEU A 363 1 7
HELIX 18 18 PRO A 365 THR A 385 1 21
HELIX 19 19 GLU A 390 LEU A 396 5 7
HELIX 20 20 MET A 406 GLY A 413 1 8
HELIX 21 21 ALA A 422 ASP A 431 1 10
HELIX 22 22 PRO A 434 LEU A 439 1 6
HELIX 23 23 PRO A 453 TRP A 456 1 4
HELIX 24 24 PRO A 462 SER A 471 1 10
HELIX 25 25 LEU A 480 ALA A 490 5 11
HELIX 26 26 ALA A 493 THR A 518 1 26
HELIX 27 27 GLN A 541 GLU A 557 1 17
HELIX 28 28 TYR A 579 ASN A 597 1 19
HELIX 29 29 GLY A 602 LYS A 604 5 3
HELIX 30 30 VAL A 615 ALA A 624 1 10
HELIX 31 31 GLY A 642 LEU A 648 1 7
HELIX 32 32 GLY A 659 VAL A 668 5 10
HELIX 33 33 GLU A 670 ASN A 672 5 3
HELIX 34 34 VAL A 680 ALA A 688 1 9
HELIX 35 35 PRO A 693 LYS A 699 1 7
HELIX 36 36 LYS A 701 GLU A 711 1 11
HELIX 37 37 LYS A 714 SER A 716 5 3
HELIX 38 38 ASP A 724 ILE A 730 1 7
HELIX 39 39 VAL A 740 ARG A 759 1 20
HELIX 40 40 GLN A 761 PHE A 778 1 18
HELIX 41 41 SER A 780 ARG A 790 1 11
HELIX 42 42 ASP B 7 TYR B 21 1 15
HELIX 43 43 ALA B 26 GLU B 28 5 3
HELIX 44 44 PRO B 31 ALA B 48 1 18
HELIX 45 45 THR B 74 LEU B 81 1 8
HELIX 46 46 TRP B 83 TYR B 94 1 12
HELIX 47 47 LEU B 98 GLU B 104 1 7
HELIX 48 48 GLY B 114 VAL B 129 1 16
HELIX 49 49 ARG B 163 ASN B 165 5 3
HELIX 50 50 GLU B 173 LEU B 175 5 3
HELIX 51 51 LEU B 230 ASN B 234 1 5
HELIX 52 52 PHE B 238 THR B 252 1 15
HELIX 53 53 THR B 262 LEU B 289 1 28
HELIX 54 54 LEU B 297 TYR B 300 1 4
HELIX 55 55 PRO B 310 HIS B 325 5 16
HELIX 56 56 TRP B 329 THR B 339 1 11
HELIX 57 57 PRO B 349 ALA B 351 5 3
HELIX 58 58 VAL B 357 LEU B 363 1 7
HELIX 59 59 PRO B 365 THR B 385 1 21
HELIX 60 60 GLU B 390 LEU B 396 5 7
HELIX 61 61 MET B 406 GLY B 413 1 8
HELIX 62 62 ALA B 422 ASP B 431 1 10
HELIX 63 63 PRO B 434 LEU B 439 1 6
HELIX 64 64 PRO B 453 TRP B 456 1 4
HELIX 65 65 PRO B 462 SER B 471 1 10
HELIX 66 66 LEU B 480 ALA B 490 5 11
HELIX 67 67 ALA B 493 THR B 518 1 26
HELIX 68 68 GLN B 541 GLU B 557 1 17
HELIX 69 69 TYR B 579 ASN B 597 1 19
HELIX 70 70 GLY B 602 LYS B 604 5 3
HELIX 71 71 VAL B 615 ALA B 624 1 10
HELIX 72 72 GLY B 642 LEU B 648 1 7
HELIX 73 73 GLY B 659 VAL B 668 5 10
HELIX 74 74 GLU B 670 ASN B 672 5 3
HELIX 75 75 VAL B 680 ALA B 688 1 9
HELIX 76 76 PRO B 693 LYS B 699 1 7
HELIX 77 77 LYS B 701 GLU B 711 1 11
HELIX 78 78 LYS B 714 SER B 716 5 3
HELIX 79 79 ASP B 724 ILE B 730 1 7
HELIX 80 80 VAL B 740 ARG B 759 1 20
HELIX 81 81 GLN B 761 PHE B 778 1 18
HELIX 82 82 SER B 780 ARG B 790 1 11
SHEET 1 A 7 VAL A 177 ILE A 181 0
SHEET 2 A 7 PHE A 195 VAL A 207 -1 N GLY A 199 O VAL A 177
SHEET 3 A 7 ALA A 214 THR A 223 -1 N THR A 223 O THR A 198
SHEET 4 A 7 ALA A 133 LEU A 138 1 N GLY A 135 O ARG A 218
SHEET 5 A 7 HIS A 60 ILE A 64 1 N VAL A 61 O THR A 134
SHEET 6 A 7 GLU A 301 ASN A 306 1 N VAL A 302 O HIS A 60
SHEET 7 A 7 PHE A 340 THR A 343 1 N ALA A 341 O ILE A 303
SHEET 1 B 2 ARG A 146 VAL A 150 0
SHEET 2 B 2 LYS A 153 ALA A 157 -1 N ALA A 157 O ARG A 146
SHEET 1 C 2 ARG A 354 ASP A 356 0
SHEET 2 C 2 GLN A 403 HIS A 405 -1 N VAL A 404 O TRP A 355
SHEET 1 D 2 VAL A 417 GLY A 419 0
SHEET 2 D 2 PHE A 444 ASN A 446 1 N HIS A 445 O VAL A 417
SHEET 1 E 3 ILE A 527 ILE A 532 0
SHEET 2 E 3 ARG A 566 GLY A 571 1 N VAL A 567 O ILE A 527
SHEET 3 E 3 VAL A 607 LEU A 610 1 N VAL A 608 O PHE A 568
SHEET 1 F 3 ILE A 627 GLN A 630 0
SHEET 2 F 3 LEU A 652 THR A 656 1 N LEU A 652 O SER A 628
SHEET 3 F 3 PHE A 674 PHE A 676 1 N PHE A 674 O GLY A 655
SHEET 1 G 7 VAL B 177 ILE B 181 0
SHEET 2 G 7 PHE B 195 VAL B 207 -1 N GLY B 199 O VAL B 177
SHEET 3 G 7 ALA B 214 THR B 223 -1 N THR B 223 O THR B 198
SHEET 4 G 7 ALA B 133 LEU B 138 1 N GLY B 135 O ARG B 218
SHEET 5 G 7 HIS B 60 ILE B 64 1 N VAL B 61 O THR B 134
SHEET 6 G 7 GLU B 301 ASN B 306 1 N VAL B 302 O HIS B 60
SHEET 7 G 7 PHE B 340 THR B 343 1 N ALA B 341 O ILE B 303
SHEET 1 H 2 ARG B 146 VAL B 150 0
SHEET 2 H 2 LYS B 153 ALA B 157 -1 N ALA B 157 O ARG B 146
SHEET 1 I 2 ARG B 354 ASP B 356 0
SHEET 2 I 2 GLN B 403 HIS B 405 -1 N VAL B 404 O TRP B 355
SHEET 1 J 2 VAL B 417 GLY B 419 0
SHEET 2 J 2 PHE B 444 ASN B 446 1 N HIS B 445 O VAL B 417
SHEET 1 K 3 ILE B 527 ILE B 532 0
SHEET 2 K 3 ARG B 566 GLY B 571 1 N VAL B 567 O ILE B 527
SHEET 3 K 3 VAL B 607 LEU B 610 1 N VAL B 608 O PHE B 568
SHEET 1 L 3 ILE B 627 GLN B 630 0
SHEET 2 L 3 LEU B 652 THR B 656 1 N LEU B 652 O SER B 628
SHEET 3 L 3 PHE B 674 PHE B 676 1 N PHE B 674 O GLY B 655
LINK C4A PLP A 999 NZ LYS A 645 1555 1555 1.36
LINK C4A PLP B 999 NZ LYS B 645 1555 1555 1.36
SITE 1 AC1 14 GLU A 67 GLY A 113 GLY A 114 LEU A 115
SITE 2 AC1 14 TYR A 256 ARG A 268 ASP A 307 HIS A 309
SITE 3 AC1 14 HIS A 345 THR A 346 GLU A 350 ARG A 534
SITE 4 AC1 14 LYS A 573 SO4 A 997
SITE 1 AC2 14 GLU B 67 GLY B 113 GLY B 114 LEU B 115
SITE 2 AC2 14 TYR B 256 ARG B 268 ASP B 307 HIS B 309
SITE 3 AC2 14 HIS B 345 THR B 346 GLU B 350 ARG B 534
SITE 4 AC2 14 LYS B 573 SO4 B 997
SITE 1 AC3 8 GLY A 114 LEU A 115 ARG A 534 TYR A 538
SITE 2 AC3 8 LYS A 539 GOL A 998 PLP A 999 MAL A1006
SITE 1 AC4 8 GLY B 114 LEU B 115 ARG B 534 TYR B 538
SITE 2 AC4 8 LYS B 539 GOL B 998 PLP B 999 MAL B1006
SITE 1 AC5 12 LEU A 69 ARG A 117 TRP A 456 LYS A 533
SITE 2 AC5 12 TYR A 613 VAL A 615 ALA A 618 GLY A 640
SITE 3 AC5 12 THR A 641 GLY A 642 LYS A 645 SO4 A 997
SITE 1 AC6 12 LEU B 69 ARG B 117 TRP B 456 LYS B 533
SITE 2 AC6 12 TYR B 613 VAL B 615 ALA B 618 GLY B 640
SITE 3 AC6 12 THR B 641 GLY B 642 LYS B 645 SO4 B 997
SITE 1 AC7 7 HIS A 345 VAL A 420 ASN A 449 GLU A 637
SITE 2 AC7 7 SER A 639 GLY A 640 SO4 A 997
SITE 1 AC8 7 HIS B 345 VAL B 420 ASN B 449 GLU B 637
SITE 2 AC8 7 SER B 639 GLY B 640 SO4 B 997
CRYST1 173.200 112.400 121.700 90.00 119.70 90.00 C 1 2 1 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 0.005774 0.000000 0.003293 0.00000
SCALE2 0.000000 0.008897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009460 0.00000
MTRIX1 1 -0.726932 -0.000378 -0.686708 69.40787 1
MTRIX2 1 -0.031532 -0.998926 0.033929 -0.83145 1
MTRIX3 1 -0.685985 0.046317 0.726140 27.74960 1
(ATOM LINES ARE NOT SHOWN.)
END
