HEADER GLYCOGEN PHOSPHORYLASE 07-JUL-92 1PYG
TITLE STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY
TITLE 2 ADENOSINE MONOPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE B;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.4.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986
KEYWDS GLYCOGEN PHOSPHORYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SPRANG
REVDAT 3 13-JUL-11 1PYG 1 VERSN
REVDAT 2 24-FEB-09 1PYG 1 VERSN
REVDAT 1 31-JAN-94 1PYG 0
JRNL AUTH S.R.SPRANG,S.G.WITHERS,E.J.GOLDSMITH,R.J.FLETTERICK,
JRNL AUTH 2 N.B.MADSEN
JRNL TITL STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN
JRNL TITL 2 PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE.
JRNL REF SCIENCE V. 254 1367 1991
JRNL REFN ISSN 0036-8075
JRNL PMID 1962195
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.R.SPRANG,N.B.MADSEN,S.G.WITHERS
REMARK 1 TITL MULTIPLE PHOSPHATE POSITIONS IN THE CATALYTIC SITE OF
REMARK 1 TITL 2 GLYCOGEN PHOSPHORYLASE: STRUCTURE OF THE
REMARK 1 TITL 3 PYRIDOXAL-5'-PYROPHOSPHATE COENZYME-SUBSTRATE ANALOG
REMARK 1 REF PROTEIN SCI. V. 1 1100 1992
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.J.GOLDSMITH,S.R.SPRANG,R.HAMLIN,N.-H.XUONG,R.J.FLETTERICK
REMARK 1 TITL DOMAIN SEPARATION IN THE ACTIVATION OF GLYCOGEN
REMARK 1 TITL 2 PHOSPHORYLASE A
REMARK 1 REF SCIENCE V. 245 528 1989
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.R.SPRANG,K.R.ACHARYA,E.J.GOLDSMITH,D.I.STUART,K.VARVILL,
REMARK 1 AUTH 2 R.J.FLETTERICK,N.B.MADSEN,L.N.JOHNSON
REMARK 1 TITL STRUCTURAL CHANGES IN GLYCOGEN PHOSPHORYLASE INDUCED BY
REMARK 1 TITL 2 PHOSPHORYLATION
REMARK 1 REF NATURE V. 336 215 1988
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.SPRANG,E.GOLDSMITH,R.FLETTERICK
REMARK 1 TITL STRUCTURE OF THE NUCLEOTIDE ACTIVATION SWITCH IN GLYCOGEN
REMARK 1 TITL 2 PHOSPHORYLASE A
REMARK 1 REF SCIENCE V. 237 1012 1987
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 5
REMARK 1 AUTH S.G.WITHERS,N.B.MADSEN,S.R.SPRANG,R.J.FLETTERICK
REMARK 1 TITL CATALYTIC SITE OF GLYCOGEN PHOSPHORYLASE: STRUCTURAL CHANGES
REMARK 1 TITL 2 DURING ACTIVATION AND MECHANISTIC IMPLICATIONS
REMARK 1 REF BIOCHEMISTRY V. 21 5372 1982
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 6
REMARK 1 AUTH S.G.WITHERS,N.B.MADSEN,B.D.SYKES,M.TAKAGI,S.SHIMOMURA,
REMARK 1 AUTH 2 T.FUKUI
REMARK 1 TITL EVIDENCE FOR DIRECT PHOSPHATE-PHOSPHATE INTERACTION BETWEEN
REMARK 1 TITL 2 PYRIDOXAL PHOSPHATE AND SUBSTRATE IN THE GLYCOGEN
REMARK 1 TITL 3 PHOSPHORYLASE CATALYTIC MECHANISM
REMARK 1 REF J.BIOL.CHEM. V. 256 10759 1981
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 7
REMARK 1 AUTH S.SPRANG,R.J.FLETTERICK
REMARK 1 TITL THE STRUCTURE OF GLYCOGEN PHOSPHORYLASE A AT 2.5 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 131 523 1979
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 25970
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 168
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 3.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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 : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 84.95000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 104.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 84.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 104.95000
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 300 REMARK: THE TRANSFORMATION PRESENTED AS *MTRIX 1* BELOW WILL YIELD
REMARK 300 APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN
REMARK 300 *A*. THE TRANSFORMATION PRESENTED AS *MTRIX 2* BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *C* WHEN APPLIED TO
REMARK 300 CHAIN *A*. THE TRANSFORMATION PRESENTED AS *MTRIX 3* BELOW
REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *D* WHEN
REMARK 300 APPLIED TO CHAIN *A*.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 PLPP-GPB IS STABILIZED IN THE CATALYTICALLY ACTIVE R-STATE
REMARK 400 BY ADENOSINE MONOPHOSPHATE. IN THE ABSENCE OF GLYCOGEN,
REMARK 400 PHOSPHORYLASE DIMERS ASSOCIATE TO FORM TETRAMERS WITH 222
REMARK 400 SYMMETRY. THE ASYMETRIC UNIT CONTAINS ONE TETRAMER OF
REMARK 400 PHOSPHORYLASE. SUBUNITS ARE NUMBERED AS CHAINS A, B, C,
REMARK 400 AND D. THE PYROPHOSPHORYL GROUP OF THE COENZYME ANALOG
REMARK 400 IS FOUND IN TWO CONFORMATIONS, GIVEN CHAIN LOCATION
REMARK 400 INDICATORS A AND B.
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 SER A 1
REMARK 465 ARG A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 ASN A 250
REMARK 465 ASP A 251
REMARK 465 PHE A 252
REMARK 465 ASN A 253
REMARK 465 LEU A 254
REMARK 465 LYS A 255
REMARK 465 ASP A 256
REMARK 465 PHE A 257
REMARK 465 ASN A 258
REMARK 465 VAL A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 TYR A 262
REMARK 465 ILE A 263
REMARK 465 ARG A 277
REMARK 465 VAL A 278
REMARK 465 LEU A 279
REMARK 465 TYR A 280
REMARK 465 PRO A 281
REMARK 465 ASN A 282
REMARK 465 ASP A 283
REMARK 465 ASN A 284
REMARK 465 PHE A 285
REMARK 465 PHE A 286
REMARK 465 GLU A 287
REMARK 465 GLY A 288
REMARK 465 PRO A 837
REMARK 465 ASP A 838
REMARK 465 GLU A 839
REMARK 465 LYS A 840
REMARK 465 ILE A 841
REMARK 465 PRO A 842
REMARK 465 SER B 1
REMARK 465 ARG B 2
REMARK 465 PRO B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 ASP B 6
REMARK 465 GLN B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 ARG B 10
REMARK 465 LYS B 11
REMARK 465 GLN B 12
REMARK 465 ILE B 13
REMARK 465 SER B 14
REMARK 465 VAL B 15
REMARK 465 ARG B 16
REMARK 465 GLY B 17
REMARK 465 LEU B 18
REMARK 465 ALA B 19
REMARK 465 ASN B 250
REMARK 465 ASP B 251
REMARK 465 PHE B 252
REMARK 465 ASN B 253
REMARK 465 LEU B 254
REMARK 465 LYS B 255
REMARK 465 ASP B 256
REMARK 465 PHE B 257
REMARK 465 ASN B 258
REMARK 465 VAL B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 TYR B 262
REMARK 465 ILE B 263
REMARK 465 ARG B 277
REMARK 465 VAL B 278
REMARK 465 LEU B 279
REMARK 465 TYR B 280
REMARK 465 PRO B 281
REMARK 465 ASN B 282
REMARK 465 ASP B 283
REMARK 465 ASN B 284
REMARK 465 PHE B 285
REMARK 465 PHE B 286
REMARK 465 GLU B 287
REMARK 465 GLY B 288
REMARK 465 PRO B 837
REMARK 465 ASP B 838
REMARK 465 GLU B 839
REMARK 465 LYS B 840
REMARK 465 ILE B 841
REMARK 465 PRO B 842
REMARK 465 SER C 1
REMARK 465 ARG C 2
REMARK 465 PRO C 3
REMARK 465 LEU C 4
REMARK 465 SER C 5
REMARK 465 ASP C 6
REMARK 465 GLN C 7
REMARK 465 GLU C 8
REMARK 465 LYS C 9
REMARK 465 ASN C 250
REMARK 465 ASP C 251
REMARK 465 PHE C 252
REMARK 465 ASN C 253
REMARK 465 LEU C 254
REMARK 465 LYS C 255
REMARK 465 ASP C 256
REMARK 465 PHE C 257
REMARK 465 ASN C 258
REMARK 465 VAL C 259
REMARK 465 GLY C 260
REMARK 465 GLY C 261
REMARK 465 TYR C 262
REMARK 465 ILE C 263
REMARK 465 ARG C 277
REMARK 465 VAL C 278
REMARK 465 LEU C 279
REMARK 465 TYR C 280
REMARK 465 PRO C 281
REMARK 465 ASN C 282
REMARK 465 ASP C 283
REMARK 465 ASN C 284
REMARK 465 PHE C 285
REMARK 465 PHE C 286
REMARK 465 GLU C 287
REMARK 465 GLY C 288
REMARK 465 PRO C 837
REMARK 465 ASP C 838
REMARK 465 GLU C 839
REMARK 465 LYS C 840
REMARK 465 ILE C 841
REMARK 465 PRO C 842
REMARK 465 SER D 1
REMARK 465 ARG D 2
REMARK 465 PRO D 3
REMARK 465 LEU D 4
REMARK 465 SER D 5
REMARK 465 ASP D 6
REMARK 465 GLN D 7
REMARK 465 GLU D 8
REMARK 465 LYS D 9
REMARK 465 ASN D 250
REMARK 465 ASP D 251
REMARK 465 PHE D 252
REMARK 465 ASN D 253
REMARK 465 LEU D 254
REMARK 465 LYS D 255
REMARK 465 ASP D 256
REMARK 465 PHE D 257
REMARK 465 ASN D 258
REMARK 465 VAL D 259
REMARK 465 GLY D 260
REMARK 465 GLY D 261
REMARK 465 TYR D 262
REMARK 465 ILE D 263
REMARK 465 ARG D 277
REMARK 465 VAL D 278
REMARK 465 LEU D 279
REMARK 465 TYR D 280
REMARK 465 PRO D 281
REMARK 465 ASN D 282
REMARK 465 ASP D 283
REMARK 465 ASN D 284
REMARK 465 PHE D 285
REMARK 465 PHE D 286
REMARK 465 GLU D 287
REMARK 465 GLY D 288
REMARK 465 PRO D 837
REMARK 465 ASP D 838
REMARK 465 GLU D 839
REMARK 465 LYS D 840
REMARK 465 ILE D 841
REMARK 465 PRO D 842
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 34 NE2 HIS A 34 CD2 -0.081
REMARK 500 HIS A 36 NE2 HIS A 36 CD2 -0.073
REMARK 500 HIS A 62 NE2 HIS A 62 CD2 -0.073
REMARK 500 HIS A 73 NE2 HIS A 73 CD2 -0.070
REMARK 500 HIS A 201 NE2 HIS A 201 CD2 -0.079
REMARK 500 HIS A 341 NE2 HIS A 341 CD2 -0.068
REMARK 500 HIS A 377 NE2 HIS A 377 CD2 -0.082
REMARK 500 HIS A 399 NE2 HIS A 399 CD2 -0.075
REMARK 500 HIS A 443 NE2 HIS A 443 CD2 -0.073
REMARK 500 HIS A 450 NE2 HIS A 450 CD2 -0.069
REMARK 500 HIS A 459 NE2 HIS A 459 CD2 -0.083
REMARK 500 HIS A 477 NE2 HIS A 477 CD2 -0.067
REMARK 500 HIS A 571 NE2 HIS A 571 CD2 -0.077
REMARK 500 HIS A 582 NE2 HIS A 582 CD2 -0.070
REMARK 500 HIS B 34 NE2 HIS B 34 CD2 -0.072
REMARK 500 HIS B 36 NE2 HIS B 36 CD2 -0.080
REMARK 500 HIS B 57 NE2 HIS B 57 CD2 -0.068
REMARK 500 HIS B 73 NE2 HIS B 73 CD2 -0.073
REMARK 500 HIS B 201 NE2 HIS B 201 CD2 -0.075
REMARK 500 HIS B 208 NE2 HIS B 208 CD2 -0.066
REMARK 500 HIS B 341 NE2 HIS B 341 CD2 -0.077
REMARK 500 HIS B 377 NE2 HIS B 377 CD2 -0.075
REMARK 500 HIS B 399 NE2 HIS B 399 CD2 -0.074
REMARK 500 HIS B 443 NE2 HIS B 443 CD2 -0.070
REMARK 500 HIS B 459 NE2 HIS B 459 CD2 -0.079
REMARK 500 HIS B 477 NE2 HIS B 477 CD2 -0.067
REMARK 500 HIS B 571 NE2 HIS B 571 CD2 -0.075
REMARK 500 HIS B 632 NE2 HIS B 632 CD2 -0.073
REMARK 500 HIS B 767 NE2 HIS B 767 CD2 -0.074
REMARK 500 HIS C 34 NE2 HIS C 34 CD2 -0.074
REMARK 500 HIS C 36 NE2 HIS C 36 CD2 -0.068
REMARK 500 HIS C 57 NE2 HIS C 57 CD2 -0.067
REMARK 500 HIS C 341 NE2 HIS C 341 CD2 -0.083
REMARK 500 HIS C 377 NE2 HIS C 377 CD2 -0.077
REMARK 500 HIS C 399 NE2 HIS C 399 CD2 -0.069
REMARK 500 HIS C 443 NE2 HIS C 443 CD2 -0.075
REMARK 500 HIS C 459 NE2 HIS C 459 CD2 -0.072
REMARK 500 HIS C 477 NE2 HIS C 477 CD2 -0.070
REMARK 500 HIS C 556 NE2 HIS C 556 CD2 -0.072
REMARK 500 HIS C 571 NE2 HIS C 571 CD2 -0.071
REMARK 500 HIS C 632 NE2 HIS C 632 CD2 -0.072
REMARK 500 HIS C 768 NE2 HIS C 768 CD2 -0.069
REMARK 500 HIS D 34 NE2 HIS D 34 CD2 -0.079
REMARK 500 HIS D 36 NE2 HIS D 36 CD2 -0.086
REMARK 500 HIS D 57 NE2 HIS D 57 CD2 -0.068
REMARK 500 HIS D 73 NE2 HIS D 73 CD2 -0.073
REMARK 500 HIS D 201 NE2 HIS D 201 CD2 -0.077
REMARK 500 HIS D 341 NE2 HIS D 341 CD2 -0.071
REMARK 500 HIS D 377 NE2 HIS D 377 CD2 -0.073
REMARK 500 HIS D 390 NE2 HIS D 390 CD2 -0.068
REMARK 500
REMARK 500 THIS ENTRY HAS 58 BOND DEVIATIONS.
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 60 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TRP A 67 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 67 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 81 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 90 CA - CB - CG ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 160 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TRP A 174 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP A 174 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 182 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 182 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 189 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP A 189 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TYR A 203 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TRP A 215 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP A 215 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TYR A 226 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 233 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 244 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 244 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP A 244 CG - CD2 - CE3 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 310 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 TRP A 361 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 361 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 365 CD1 - CG - CD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 TRP A 365 CB - CG - CD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 TRP A 365 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 365 CE2 - CD2 - CG ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP A 365 CG - CD2 - CE3 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP A 387 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 387 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 387 CG - CD2 - CE3 ANGL. DEV. = 5.8 DEGREES
REMARK 500 VAL A 422 CA - CB - CG1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 427 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 457 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TYR A 472 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 489 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 489 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 490 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 TRP A 491 CD1 - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP A 491 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 506 CA - CB - CG ANGL. DEV. = -14.9 DEGREES
REMARK 500 ARG A 519 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 307 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 LYS A 11 -65.77 72.28
REMARK 500 ARG A 16 -50.10 -25.60
REMARK 500 LEU A 18 -44.10 -9.84
REMARK 500 HIS A 36 -69.78 -92.44
REMARK 500 PRO A 79 -179.71 -60.01
REMARK 500 ALA A 103 33.93 73.25
REMARK 500 ALA A 129 92.57 -69.17
REMARK 500 ASN A 133 -28.69 -162.60
REMARK 500 ILE A 165 78.38 -65.29
REMARK 500 PHE A 166 -174.15 38.43
REMARK 500 TYR A 203 -141.76 52.19
REMARK 500 ARG A 234 15.30 49.14
REMARK 500 SER A 313 62.69 -108.20
REMARK 500 PRO A 321 -166.50 -59.89
REMARK 500 VAL A 322 -45.00 161.54
REMARK 500 ASP A 339 -176.43 80.74
REMARK 500 TRP A 361 -60.57 -22.08
REMARK 500 ALA A 435 -49.84 75.65
REMARK 500 ALA A 456 144.95 -176.88
REMARK 500 THR A 466 -75.45 -135.47
REMARK 500 ASN A 484 172.80 -55.15
REMARK 500 LEU A 492 -67.51 -127.40
REMARK 500 ASP A 514 67.44 -156.77
REMARK 500 ARG A 551 42.63 -72.28
REMARK 500 GLU A 552 -84.84 -169.19
REMARK 500 TYR A 553 4.03 -60.39
REMARK 500 LYS A 554 45.35 36.30
REMARK 500 PRO A 559 3.59 -62.39
REMARK 500 GLN A 665 60.91 -102.05
REMARK 500 ILE A 666 36.38 -99.34
REMARK 500 SER A 674 -124.28 -129.79
REMARK 500 ASN A 684 30.74 -95.49
REMARK 500 PHE A 709 64.41 -111.50
REMARK 500 SER A 751 42.93 -153.12
REMARK 500 HIS A 767 -19.25 -144.80
REMARK 500 ASN B 23 118.47 -170.13
REMARK 500 ALA B 153 72.77 -67.69
REMARK 500 PHE B 166 176.86 44.69
REMARK 500 ARG B 193 78.47 -112.69
REMARK 500 TYR B 203 -139.29 54.99
REMARK 500 ARG B 234 18.16 49.18
REMARK 500 SER B 313 59.75 -92.77
REMARK 500 PRO B 321 -114.36 -58.16
REMARK 500 VAL B 322 -48.17 106.71
REMARK 500 PHE B 326 8.47 -62.81
REMARK 500 ASP B 339 167.02 68.85
REMARK 500 PRO B 342 28.50 -75.16
REMARK 500 ASP B 421 33.08 -21.64
REMARK 500 VAL B 422 -18.54 -46.88
REMARK 500 ALA B 435 -85.39 65.57
REMARK 500
REMARK 500 THIS ENTRY HAS 133 RAMACHANDRAN OUTLIERS.
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 LEU B 834 PRO B 835 149.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 52 0.07 SIDE CHAIN
REMARK 500 TYR A 297 0.07 SIDE CHAIN
REMARK 500 TYR B 52 0.07 SIDE CHAIN
REMARK 500 TYR C 52 0.08 SIDE CHAIN
REMARK 500 TYR C 791 0.08 SIDE CHAIN
REMARK 500 TYR D 511 0.07 SIDE CHAIN
REMARK 500 TYR D 524 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PRO A 835 24.2 L L OUTSIDE RANGE
REMARK 500 LYS C 554 25.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 PYRIDOXAL-5'-PYROPHOSPHORYL GLYCOGEN PHOSPHORYLASE B
REMARK 600 (PLPP-GPB) IS A COVALENT ANALOG OF THE ENZYME-SUBSTRATE
REMARK 600 COMPLEX WHERE THE SUBSTRATE IS INORGANIC PHOSPHATE.
REMARK 600 PHOSPHORYLASE CATALYSES THE PHOSPHOROLYTIC DEGRADATION OF
REMARK 600 GLYCOGEN, A POLYMER OF GLUCOSE UNITS CONNECTED BY
REMARK 600 ALPHA-D-(1,4) LINKAGES. THE PRODUCT, GLUCOSE-1-PHOSPHATE
REMARK 600 (G-1-P), IS GENERATED BY NUCLEOPHILIC SUBSTITUTION BY
REMARK 600 PHOSPHATE AT THE 1' POSITION OF THE NON-REDUCING HEXOSE,
REMARK 600 WITH PROTONATION OF THE O4' OXYGEN OF THE POLYMERIC LEAVING
REMARK 600 GROUP. THE REACTION MECHANISM IS KNOWN TO INVOLVE CLOSE
REMARK 600 APPROXIMATION BETWEEN THE PHOSPHATE GROUP OF THE COENZYME
REMARK 600 (PYRIDOXAL PHOSPHATE) AND THE SUBSTRATE PHOSPHATE (THE
REMARK 600 REACTION IS FREELY REVERSIBLE WITH A K EQ NEAR 1.
REMARK 600 THE REVERSE REACTION LENGTHENS THE AMYLOSE CHAIN BY ONE
REMARK 600 UNIT WITH OLIGOSACCHARIDE AND G-1-P AS SUBSTRATES). THUS,
REMARK 600 PYRIDOXAL-5'-PYROPHOSPHORYL IS A COVALENT MIMIC OF THE
REMARK 600 PHOSPHATE-PHOSPHATE BRIDGE THOUGHT TO FORM NEAR THE
REMARK 600 TRANSITION STATE. SPECIFICALLY, PLPP MIMICS THE CLOSE
REMARK 600 CONTACT EXPECTED FOR A PSEUDO-BOND BETWEEN THE PHOSPHATE
REMARK 600 GROUPS WITH PYRIMIDALIZATION OF THE PLP PHOSPHATE, AS
REMARK 600 PROPOSED FOR AN ELECTROPHILIC CATALYTIC ROLE OF THE PLP.
REMARK 600
REMARK 600 PLPP IS ATTACHED TO LYSINE 680 BY A SHIFF BASE LINKAGE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 843
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDP A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B 843
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDP B 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 843
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDP C 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP D 843
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDP D 860
DBREF 1PYG A 1 842 UNP P00489 PHS2_RABIT 1 842
DBREF 1PYG B 1 842 UNP P00489 PHS2_RABIT 1 842
DBREF 1PYG C 1 842 UNP P00489 PHS2_RABIT 1 842
DBREF 1PYG D 1 842 UNP P00489 PHS2_RABIT 1 842
SEQRES 1 A 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE
SEQRES 2 A 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU
SEQRES 3 A 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 A 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR
SEQRES 5 A 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 A 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP
SEQRES 7 A 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 A 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU
SEQRES 9 A 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU
SEQRES 10 A 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 A 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 A 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 A 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS
SEQRES 14 A 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP
SEQRES 15 A 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU
SEQRES 16 A 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS
SEQRES 17 A 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL
SEQRES 18 A 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG
SEQRES 19 A 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS
SEQRES 20 A 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY
SEQRES 21 A 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 A 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 A 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 A 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 A 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN
SEQRES 26 A 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN
SEQRES 27 A 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 A 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA
SEQRES 29 A 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS
SEQRES 30 A 842 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS
SEQRES 31 A 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE
SEQRES 32 A 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA
SEQRES 33 A 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 A 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA
SEQRES 35 A 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 A 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE
SEQRES 37 A 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN
SEQRES 38 A 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU
SEQRES 39 A 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE
SEQRES 40 A 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS
SEQRES 41 A 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP
SEQRES 42 A 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA
SEQRES 43 A 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO
SEQRES 44 A 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 A 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 A 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL
SEQRES 47 A 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 A 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 A 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY
SEQRES 50 A 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 A 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER
SEQRES 52 A 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 A 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 A 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 A 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL
SEQRES 56 A 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA
SEQRES 57 A 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE
SEQRES 58 A 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN
SEQRES 59 A 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS
SEQRES 60 A 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR
SEQRES 61 A 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN
SEQRES 62 A 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA
SEQRES 63 A 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN
SEQRES 64 A 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN
SEQRES 65 A 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO
SEQRES 1 B 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE
SEQRES 2 B 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU
SEQRES 3 B 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 B 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR
SEQRES 5 B 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 B 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP
SEQRES 7 B 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 B 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU
SEQRES 9 B 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU
SEQRES 10 B 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 B 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 B 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 B 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS
SEQRES 14 B 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP
SEQRES 15 B 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU
SEQRES 16 B 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS
SEQRES 17 B 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL
SEQRES 18 B 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG
SEQRES 19 B 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS
SEQRES 20 B 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY
SEQRES 21 B 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 B 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 B 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 B 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 B 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN
SEQRES 26 B 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN
SEQRES 27 B 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 B 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA
SEQRES 29 B 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS
SEQRES 30 B 842 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS
SEQRES 31 B 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE
SEQRES 32 B 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA
SEQRES 33 B 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 B 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA
SEQRES 35 B 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 B 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE
SEQRES 37 B 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN
SEQRES 38 B 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU
SEQRES 39 B 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE
SEQRES 40 B 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS
SEQRES 41 B 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP
SEQRES 42 B 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA
SEQRES 43 B 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO
SEQRES 44 B 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 B 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 B 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL
SEQRES 47 B 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 B 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 B 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY
SEQRES 50 B 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 B 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER
SEQRES 52 B 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 B 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 B 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 B 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL
SEQRES 56 B 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA
SEQRES 57 B 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE
SEQRES 58 B 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN
SEQRES 59 B 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS
SEQRES 60 B 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR
SEQRES 61 B 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN
SEQRES 62 B 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA
SEQRES 63 B 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN
SEQRES 64 B 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN
SEQRES 65 B 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO
SEQRES 1 C 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE
SEQRES 2 C 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU
SEQRES 3 C 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 C 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR
SEQRES 5 C 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 C 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP
SEQRES 7 C 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 C 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU
SEQRES 9 C 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU
SEQRES 10 C 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 C 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 C 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 C 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS
SEQRES 14 C 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP
SEQRES 15 C 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU
SEQRES 16 C 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS
SEQRES 17 C 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL
SEQRES 18 C 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG
SEQRES 19 C 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS
SEQRES 20 C 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY
SEQRES 21 C 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 C 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 C 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 C 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 C 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN
SEQRES 26 C 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN
SEQRES 27 C 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 C 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA
SEQRES 29 C 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS
SEQRES 30 C 842 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS
SEQRES 31 C 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE
SEQRES 32 C 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA
SEQRES 33 C 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 C 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA
SEQRES 35 C 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 C 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE
SEQRES 37 C 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN
SEQRES 38 C 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU
SEQRES 39 C 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE
SEQRES 40 C 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS
SEQRES 41 C 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP
SEQRES 42 C 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA
SEQRES 43 C 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO
SEQRES 44 C 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 C 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 C 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL
SEQRES 47 C 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 C 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 C 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY
SEQRES 50 C 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 C 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER
SEQRES 52 C 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 C 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 C 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 C 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL
SEQRES 56 C 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA
SEQRES 57 C 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE
SEQRES 58 C 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN
SEQRES 59 C 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS
SEQRES 60 C 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR
SEQRES 61 C 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN
SEQRES 62 C 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA
SEQRES 63 C 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN
SEQRES 64 C 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN
SEQRES 65 C 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO
SEQRES 1 D 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE
SEQRES 2 D 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU
SEQRES 3 D 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 D 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR
SEQRES 5 D 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 D 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP
SEQRES 7 D 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 D 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU
SEQRES 9 D 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU
SEQRES 10 D 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 D 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 D 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 D 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS
SEQRES 14 D 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP
SEQRES 15 D 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU
SEQRES 16 D 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS
SEQRES 17 D 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL
SEQRES 18 D 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG
SEQRES 19 D 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS
SEQRES 20 D 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY
SEQRES 21 D 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 D 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 D 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 D 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 D 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN
SEQRES 26 D 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN
SEQRES 27 D 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 D 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA
SEQRES 29 D 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS
SEQRES 30 D 842 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS
SEQRES 31 D 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE
SEQRES 32 D 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA
SEQRES 33 D 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 D 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA
SEQRES 35 D 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 D 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE
SEQRES 37 D 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN
SEQRES 38 D 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU
SEQRES 39 D 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE
SEQRES 40 D 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS
SEQRES 41 D 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP
SEQRES 42 D 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA
SEQRES 43 D 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO
SEQRES 44 D 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 D 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 D 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL
SEQRES 47 D 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 D 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 D 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY
SEQRES 50 D 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 D 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER
SEQRES 52 D 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 D 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 D 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 D 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL
SEQRES 56 D 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA
SEQRES 57 D 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE
SEQRES 58 D 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN
SEQRES 59 D 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS
SEQRES 60 D 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR
SEQRES 61 D 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN
SEQRES 62 D 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA
SEQRES 63 D 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN
SEQRES 64 D 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN
SEQRES 65 D 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO
HET AMP A 843 23
HET PDP A 860 38
HET AMP B 843 23
HET PDP B 860 38
HET AMP C 843 23
HET PDP C 860 38
HET AMP D 843 23
HET PDP D 860 38
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM PDP PYRIDOXAL-5'-DIPHOSPHATE
FORMUL 5 AMP 4(C10 H14 N5 O7 P)
FORMUL 6 PDP 4(C8 H11 N O9 P2)
HELIX 1 1 ASN A 23 PHE A 37 1 15
HELIX 2 2 THR A 47 ASP A 78 1 32
HELIX 3 3 THR A 94 ALA A 103 1 10
HELIX 4 4 LEU A 104 LEU A 115 1 12
HELIX 5 5 ASP A 118 GLU A 124 1 7
HELIX 6 6 GLY A 134 LEU A 150 1 17
HELIX 7 7 ASP A 181 GLY A 186 5 6
HELIX 8 8 PRO A 194 THR A 197 5 4
HELIX 9 9 GLN A 264 ASN A 274 1 11
HELIX 10 10 LYS A 289 SER A 313 1 25
HELIX 11 11 ASN A 325 ASP A 327 5 3
HELIX 12 12 ALA A 328 LYS A 332 1 5
HELIX 13 13 LEU A 344 LEU A 356 1 13
HELIX 14 14 ASP A 360 THR A 371 1 12
HELIX 15 15 VAL A 389 LEU A 396 1 8
HELIX 16 16 LEU A 396 PHE A 418 1 23
HELIX 17 17 ASP A 421 MET A 428 1 8
HELIX 18 18 MET A 441 SER A 449 1 9
HELIX 19 19 ALA A 456 THR A 466 1 11
HELIX 20 20 PHE A 468 GLU A 475 1 8
HELIX 21 21 ASN A 496 GLY A 508 1 13
HELIX 22 22 GLU A 509 ASP A 514 5 6
HELIX 23 23 ASP A 514 ASP A 526 5 13
HELIX 24 24 ASP A 527 ARG A 551 1 25
HELIX 25 25 HIS A 571 LYS A 574 5 4
HELIX 26 26 ARG A 575 GLU A 593 1 19
HELIX 27 27 TYR A 613 ASN A 631 1 19
HELIX 28 28 VAL A 636 ASP A 638 5 3
HELIX 29 29 ARG A 649 ILE A 657 1 9
HELIX 30 30 PRO A 658 ALA A 660 5 3
HELIX 31 31 GLY A 675 ASN A 684 1 10
HELIX 32 32 ALA A 695 GLY A 704 1 10
HELIX 33 33 GLU A 705 PHE A 708 5 4
HELIX 34 34 ARG A 714 GLY A 725 1 12
HELIX 35 35 ALA A 728 ILE A 735 1 8
HELIX 36 36 ILE A 735 SER A 747 1 13
HELIX 37 37 PHE A 758 HIS A 768 1 11
HELIX 38 38 LYS A 772 LYS A 792 1 21
HELIX 39 39 ASN A 793 SER A 808 1 16
HELIX 40 40 GLY A 809 PHE A 811 5 3
HELIX 41 41 SER A 812 ILE A 824 1 13
HELIX 42 42 ASN B 23 PHE B 37 1 15
HELIX 43 43 THR B 47 ASP B 78 1 32
HELIX 44 44 ARG B 93 LEU B 102 1 10
HELIX 45 45 LEU B 104 LEU B 115 1 12
HELIX 46 46 ASP B 118 GLU B 124 1 7
HELIX 47 47 GLY B 134 LEU B 150 1 17
HELIX 48 48 PRO B 194 THR B 197 5 4
HELIX 49 49 GLN B 264 ASN B 274 1 11
HELIX 50 50 LYS B 289 SER B 313 1 25
HELIX 51 51 ASN B 325 ASP B 327 5 3
HELIX 52 52 ALA B 328 LYS B 332 1 5
HELIX 53 53 THR B 340 SER B 343 5 4
HELIX 54 54 LEU B 344 LEU B 356 1 13
HELIX 55 55 ASP B 360 THR B 371 1 12
HELIX 56 56 LEU B 380 LEU B 384 5 5
HELIX 57 57 VAL B 389 LEU B 396 1 8
HELIX 58 58 LEU B 396 PHE B 418 1 23
HELIX 59 59 ASP B 421 SER B 429 1 9
HELIX 60 60 MET B 441 SER B 449 1 9
HELIX 61 61 ALA B 456 THR B 466 1 11
HELIX 62 62 PHE B 468 GLU B 475 1 8
HELIX 63 63 ASN B 496 GLY B 508 1 13
HELIX 64 64 GLU B 509 ASP B 514 5 6
HELIX 65 65 ASP B 514 VAL B 525 5 12
HELIX 66 66 ASP B 527 LYS B 554 1 28
HELIX 67 67 HIS B 571 LYS B 574 5 4
HELIX 68 68 ARG B 575 GLU B 593 1 19
HELIX 69 69 TYR B 613 ASP B 633 1 21
HELIX 70 70 VAL B 636 ASP B 638 5 3
HELIX 71 71 ARG B 649 ILE B 657 1 9
HELIX 72 72 PRO B 658 ALA B 660 5 3
HELIX 73 73 GLY B 675 ASN B 684 1 10
HELIX 74 74 ASP B 693 GLY B 704 1 12
HELIX 75 75 GLU B 705 PHE B 708 5 4
HELIX 76 76 ARG B 714 GLY B 725 1 12
HELIX 77 77 ASN B 727 ILE B 735 1 9
HELIX 78 78 ILE B 735 GLY B 748 1 14
HELIX 79 79 PHE B 758 HIS B 768 1 11
HELIX 80 80 VAL B 773 LYS B 792 1 20
HELIX 81 81 ASN B 793 SER B 808 1 16
HELIX 82 82 GLY B 809 PHE B 811 5 3
HELIX 83 83 SER B 812 ILE B 824 1 13
HELIX 84 84 ASN C 23 THR C 38 1 16
HELIX 85 85 THR C 47 ASP C 78 1 32
HELIX 86 86 ARG C 93 LEU C 102 1 10
HELIX 87 87 LEU C 104 LEU C 115 1 12
HELIX 88 88 ASP C 118 GLU C 124 1 7
HELIX 89 89 GLY C 134 LEU C 150 1 17
HELIX 90 90 ASP C 181 GLY C 186 5 6
HELIX 91 91 PRO C 194 THR C 197 5 4
HELIX 92 92 VAL C 266 ASN C 274 1 9
HELIX 93 93 LYS C 289 SER C 313 1 25
HELIX 94 94 ASN C 325 ASP C 327 5 3
HELIX 95 95 ALA C 328 LYS C 332 1 5
HELIX 96 96 LEU C 344 ASP C 355 1 12
HELIX 97 97 ASP C 360 THR C 371 1 12
HELIX 98 98 VAL C 389 LEU C 396 1 8
HELIX 99 99 LEU C 396 PHE C 418 1 23
HELIX 100 100 ASP C 421 SER C 429 1 9
HELIX 101 101 MET C 441 SER C 449 1 9
HELIX 102 102 ALA C 456 THR C 466 1 11
HELIX 103 103 PHE C 468 GLU C 475 1 8
HELIX 104 104 ASN C 496 GLY C 508 1 13
HELIX 105 105 GLU C 509 ASP C 514 5 6
HELIX 106 106 ASP C 514 VAL C 525 5 12
HELIX 107 107 ASP C 527 GLU C 552 1 26
HELIX 108 108 ARG C 575 GLU C 593 1 19
HELIX 109 109 TYR C 613 ASN C 631 1 19
HELIX 110 110 VAL C 636 ASP C 638 5 3
HELIX 111 111 ARG C 649 ILE C 657 1 9
HELIX 112 112 PRO C 658 ALA C 660 5 3
HELIX 113 113 GLY C 675 ASN C 684 1 10
HELIX 114 114 GLY C 694 GLY C 704 1 11
HELIX 115 115 GLU C 705 PHE C 708 5 4
HELIX 116 116 ARG C 714 GLY C 725 1 12
HELIX 117 117 ASN C 727 ILE C 735 1 9
HELIX 118 118 ILE C 735 SER C 747 1 13
HELIX 119 119 PHE C 758 HIS C 768 1 11
HELIX 120 120 LYS C 772 ASN C 793 1 22
HELIX 121 121 ASN C 793 ALA C 806 1 14
HELIX 122 122 THR C 807 PHE C 811 5 5
HELIX 123 123 SER C 812 ILE C 824 1 13
HELIX 124 124 ASN D 23 PHE D 37 1 15
HELIX 125 125 THR D 47 ASP D 78 1 32
HELIX 126 126 ARG D 93 LEU D 102 1 10
HELIX 127 127 LEU D 104 LEU D 115 1 12
HELIX 128 128 ASP D 118 GLU D 124 1 7
HELIX 129 129 GLY D 134 LEU D 150 1 17
HELIX 130 130 PRO D 194 THR D 197 5 4
HELIX 131 131 GLN D 264 ASN D 274 1 11
HELIX 132 132 LYS D 289 SER D 313 1 25
HELIX 133 133 ASN D 325 ASP D 327 5 3
HELIX 134 134 ALA D 328 LYS D 332 1 5
HELIX 135 135 LEU D 344 ASP D 355 1 12
HELIX 136 136 ASP D 360 THR D 371 1 12
HELIX 137 137 LEU D 380 LEU D 384 5 5
HELIX 138 138 VAL D 389 LEU D 396 1 8
HELIX 139 139 LEU D 396 PHE D 418 1 23
HELIX 140 140 ASP D 421 SER D 429 1 9
HELIX 141 141 MET D 441 SER D 449 1 9
HELIX 142 142 ALA D 456 THR D 466 1 11
HELIX 143 143 PHE D 468 GLU D 475 1 8
HELIX 144 144 ASN D 496 GLY D 508 1 13
HELIX 145 145 GLU D 509 SER D 513 5 5
HELIX 146 146 ASP D 514 VAL D 525 5 12
HELIX 147 147 ASP D 527 GLU D 552 1 26
HELIX 148 148 HIS D 571 LYS D 574 5 4
HELIX 149 149 ARG D 575 GLU D 593 1 19
HELIX 150 150 TYR D 613 ASN D 631 1 19
HELIX 151 151 HIS D 632 GLY D 637 5 6
HELIX 152 152 ARG D 649 ALA D 660 1 12
HELIX 153 153 GLY D 675 ASN D 684 1 10
HELIX 154 154 ALA D 695 GLY D 704 1 10
HELIX 155 155 GLU D 705 PHE D 708 5 4
HELIX 156 156 ARG D 714 GLY D 725 1 12
HELIX 157 157 ALA D 728 ILE D 735 1 8
HELIX 158 158 ILE D 735 GLY D 748 1 14
HELIX 159 159 PHE D 758 HIS D 768 1 11
HELIX 160 160 LYS D 772 LYS D 792 1 21
HELIX 161 161 ASN D 793 SER D 808 1 16
HELIX 162 162 GLY D 809 PHE D 811 5 3
HELIX 163 163 SER D 812 ILE D 824 1 13
SHEET 1 A 9 PHE A 479 ASN A 481 0
SHEET 2 A 9 VAL A 452 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 A 9 CYS A 372 THR A 375 1 O TYR A 374 N ASN A 453
SHEET 4 A 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 A 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 A 9 ALA A 154 ILE A 159 1 O TYR A 155 N TYR A 84
SHEET 7 A 9 VAL A 238 LYS A 247 1 O THR A 240 N GLY A 156
SHEET 8 A 9 GLN A 219 PRO A 231 -1 O LEU A 222 N LYS A 247
SHEET 9 A 9 LYS A 191 ALA A 192 -1 O LYS A 191 N ASP A 227
SHEET 1 B 9 PHE A 479 ASN A 481 0
SHEET 2 B 9 VAL A 452 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 B 9 CYS A 372 THR A 375 1 O TYR A 374 N ASN A 453
SHEET 4 B 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 B 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 B 9 ALA A 154 ILE A 159 1 O TYR A 155 N TYR A 84
SHEET 7 B 9 VAL A 238 LYS A 247 1 O THR A 240 N GLY A 156
SHEET 8 B 9 GLN A 219 PRO A 231 -1 O LEU A 222 N LYS A 247
SHEET 9 B 9 LEU A 198 PHE A 202 -1 O LEU A 198 N ALA A 223
SHEET 1 C 2 GLY A 164 CYS A 171 0
SHEET 2 C 2 TRP A 174 ASP A 180 -1 O TRP A 174 N CYS A 171
SHEET 1 D 2 ARG A 205 HIS A 208 0
SHEET 2 D 2 ALA A 213 VAL A 216 -1 O LYS A 214 N GLU A 207
SHEET 1 E 3 ARG A 386 PRO A 388 0
SHEET 2 E 3 ARG A 438 ASN A 440 -1 N ILE A 439 O TRP A 387
SHEET 3 E 3 VAL A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 F 6 LEU A 640 PHE A 644 0
SHEET 2 F 6 ARG A 601 GLY A 606 1 O ARG A 601 N ARG A 641
SHEET 3 F 6 LEU A 562 VAL A 567 1 O LEU A 562 N THR A 602
SHEET 4 F 6 LEU A 662 GLN A 665 1 O LEU A 662 N VAL A 565
SHEET 5 F 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 F 6 PHE A 709 ILE A 710 1 O PHE A 709 N GLY A 690
SHEET 1 G 3 LEU B 198 THR B 209 0
SHEET 2 G 3 GLY B 212 PRO B 231 -1 N GLY B 212 O THR B 209
SHEET 3 G 3 LYS B 191 ALA B 192 -1 O LYS B 191 N ASP B 227
SHEET 1 H 9 LEU B 198 THR B 209 0
SHEET 2 H 9 GLY B 212 PRO B 231 -1 N GLY B 212 O THR B 209
SHEET 3 H 9 VAL B 238 LYS B 247 -1 N ASN B 239 O VAL B 230
SHEET 4 H 9 ALA B 154 ILE B 159 1 O ALA B 154 N THR B 240
SHEET 5 H 9 ARG B 81 LEU B 85 1 O ILE B 82 N TYR B 155
SHEET 6 H 9 VAL B 333 ASN B 338 1 O ALA B 334 N TYR B 83
SHEET 7 H 9 CYS B 372 THR B 375 1 O ALA B 373 N LEU B 337
SHEET 8 H 9 VAL B 452 GLY B 454 1 N ASN B 453 O TYR B 374
SHEET 9 H 9 PHE B 479 ASN B 481 1 N GLN B 480 O VAL B 452
SHEET 1 I 2 ASN B 167 CYS B 171 0
SHEET 2 I 2 TRP B 174 GLU B 178 -1 O TRP B 174 N CYS B 171
SHEET 1 J 3 ARG B 386 PRO B 388 0
SHEET 2 J 3 ARG B 438 ASN B 440 -1 N ILE B 439 O TRP B 387
SHEET 3 J 3 VAL B 431 GLU B 432 -1 N GLU B 432 O ARG B 438
SHEET 1 K 6 LEU B 640 LEU B 645 0
SHEET 2 K 6 ARG B 601 GLY B 606 1 O ARG B 601 N ARG B 641
SHEET 3 K 6 LEU B 562 VAL B 567 1 O LEU B 562 N THR B 602
SHEET 4 K 6 LEU B 662 GLN B 665 1 O LEU B 662 N VAL B 565
SHEET 5 K 6 LEU B 687 GLY B 690 1 O LEU B 687 N SER B 663
SHEET 6 K 6 PHE B 709 ILE B 710 1 O PHE B 709 N GLY B 690
SHEET 1 L 9 PHE C 479 ASN C 481 0
SHEET 2 L 9 VAL C 452 GLY C 454 1 O VAL C 452 N GLN C 480
SHEET 3 L 9 CYS C 372 THR C 375 1 O TYR C 374 N ASN C 453
SHEET 4 L 9 VAL C 333 ASN C 338 1 O ILE C 335 N ALA C 373
SHEET 5 L 9 ARG C 81 LEU C 85 1 O ARG C 81 N ALA C 334
SHEET 6 L 9 ALA C 154 ILE C 159 1 O TYR C 155 N TYR C 84
SHEET 7 L 9 VAL C 238 LYS C 247 1 O THR C 240 N GLY C 156
SHEET 8 L 9 GLN C 219 PRO C 231 -1 O LEU C 222 N LYS C 247
SHEET 9 L 9 LYS C 191 ALA C 192 -1 O LYS C 191 N ASP C 227
SHEET 1 M 9 PHE C 479 ASN C 481 0
SHEET 2 M 9 VAL C 452 GLY C 454 1 O VAL C 452 N GLN C 480
SHEET 3 M 9 CYS C 372 THR C 375 1 O TYR C 374 N ASN C 453
SHEET 4 M 9 VAL C 333 ASN C 338 1 O ILE C 335 N ALA C 373
SHEET 5 M 9 ARG C 81 LEU C 85 1 O ARG C 81 N ALA C 334
SHEET 6 M 9 ALA C 154 ILE C 159 1 O TYR C 155 N TYR C 84
SHEET 7 M 9 VAL C 238 LYS C 247 1 O THR C 240 N GLY C 156
SHEET 8 M 9 GLN C 219 PRO C 231 -1 O LEU C 222 N LYS C 247
SHEET 9 M 9 LEU C 198 PHE C 202 -1 O LEU C 198 N ALA C 223
SHEET 1 N 2 GLY C 164 CYS C 171 0
SHEET 2 N 2 TRP C 174 ASP C 180 -1 N TRP C 174 O CYS C 171
SHEET 1 O 2 ARG C 205 HIS C 208 0
SHEET 2 O 2 ALA C 213 VAL C 216 -1 N LYS C 214 O GLU C 207
SHEET 1 P 3 ARG C 386 PRO C 388 0
SHEET 2 P 3 ARG C 438 ASN C 440 -1 N ILE C 439 O TRP C 387
SHEET 3 P 3 VAL C 431 GLU C 432 -1 N GLU C 432 O ARG C 438
SHEET 1 Q 6 LEU C 640 PHE C 644 0
SHEET 2 Q 6 ARG C 601 GLY C 606 1 O ARG C 601 N ARG C 641
SHEET 3 Q 6 LEU C 562 VAL C 567 1 O LEU C 562 N THR C 602
SHEET 4 Q 6 LEU C 662 GLN C 665 1 N LEU C 662 O PHE C 563
SHEET 5 Q 6 LEU C 687 GLY C 690 1 O LEU C 687 N SER C 663
SHEET 6 Q 6 PHE C 709 ILE C 710 1 O PHE C 709 N GLY C 690
SHEET 1 R 3 LEU D 198 HIS D 208 0
SHEET 2 R 3 ALA D 213 PRO D 231 -1 N LYS D 214 O GLU D 207
SHEET 3 R 3 LYS D 191 ALA D 192 -1 O LYS D 191 N ASP D 227
SHEET 1 S 9 LEU D 198 HIS D 208 0
SHEET 2 S 9 ALA D 213 PRO D 231 -1 N LYS D 214 O GLU D 207
SHEET 3 S 9 VAL D 238 LYS D 247 -1 N ASN D 239 O VAL D 230
SHEET 4 S 9 ALA D 153 ILE D 159 1 O ALA D 154 N THR D 240
SHEET 5 S 9 ARG D 81 LEU D 85 1 N ILE D 82 O ALA D 153
SHEET 6 S 9 VAL D 333 ASN D 338 1 O ALA D 334 N TYR D 83
SHEET 7 S 9 CYS D 372 THR D 375 1 O ALA D 373 N LEU D 337
SHEET 8 S 9 VAL D 452 GLY D 454 1 N ASN D 453 O TYR D 374
SHEET 9 S 9 PHE D 479 ASN D 481 1 O GLN D 480 N GLY D 454
SHEET 1 T 2 GLY D 164 CYS D 171 0
SHEET 2 T 2 TRP D 174 ASP D 180 -1 O TRP D 174 N CYS D 171
SHEET 1 U 3 ARG D 386 PRO D 388 0
SHEET 2 U 3 ARG D 438 ASN D 440 -1 N ILE D 439 O TRP D 387
SHEET 3 U 3 VAL D 431 GLU D 432 -1 N GLU D 432 O ARG D 438
SHEET 1 V 6 VAL D 642 LEU D 645 0
SHEET 2 V 6 ARG D 601 GLY D 606 1 O VAL D 603 N ILE D 643
SHEET 3 V 6 LEU D 562 VAL D 567 1 O LEU D 562 N THR D 602
SHEET 4 V 6 LEU D 662 GLN D 665 1 O LEU D 662 N VAL D 565
SHEET 5 V 6 LEU D 687 GLY D 690 1 O LEU D 687 N SER D 663
SHEET 6 V 6 PHE D 709 ILE D 710 1 N PHE D 709 O THR D 688
LINK NZ LYS A 680 C4AAPDP A 860 1555 1555 1.59
LINK NZ LYS A 680 C4ABPDP A 860 1555 1555 1.44
LINK NZ LYS B 680 C4AAPDP B 860 1555 1555 1.46
LINK NZ LYS B 680 C4ABPDP B 860 1555 1555 1.45
LINK NZ LYS C 680 C4ABPDP C 860 1555 1555 1.43
LINK NZ LYS C 680 C4AAPDP C 860 1555 1555 1.56
LINK NZ LYS D 680 C4ABPDP D 860 1555 1555 1.35
LINK NZ LYS D 680 C4AAPDP D 860 1555 1555 1.45
SITE 1 AC1 12 TRP A 67 GLN A 71 TYR A 75 ARG A 309
SITE 2 AC1 12 ARG A 310 LYS A 315 PHE A 316 GLY A 317
SITE 3 AC1 12 CYS A 318 ASP B 42 ASN B 44 VAL B 45
SITE 1 AC2 13 TYR A 90 GLY A 135 TRP A 491 LYS A 568
SITE 2 AC2 13 ARG A 569 LYS A 574 ARG A 649 VAL A 650
SITE 3 AC2 13 ALA A 653 GLY A 675 THR A 676 GLY A 677
SITE 4 AC2 13 LYS A 680
SITE 1 AC3 12 ASP A 42 ASN A 44 VAL A 45 TRP B 67
SITE 2 AC3 12 GLN B 71 TYR B 75 ARG B 309 ARG B 310
SITE 3 AC3 12 LYS B 315 PHE B 316 GLY B 317 CYS B 318
SITE 1 AC4 15 TYR B 90 GLY B 135 TRP B 491 LYS B 568
SITE 2 AC4 15 ARG B 569 LYS B 574 TYR B 648 ARG B 649
SITE 3 AC4 15 VAL B 650 ALA B 653 GLY B 675 THR B 676
SITE 4 AC4 15 GLY B 677 ASN B 678 LYS B 680
SITE 1 AC5 12 TRP C 67 GLN C 71 TYR C 75 ARG C 309
SITE 2 AC5 12 ARG C 310 LYS C 315 PHE C 316 GLY C 317
SITE 3 AC5 12 CYS C 318 ASP D 42 ASN D 44 VAL D 45
SITE 1 AC6 12 TYR C 90 TRP C 491 LYS C 568 ARG C 569
SITE 2 AC6 12 LYS C 574 TYR C 648 ARG C 649 VAL C 650
SITE 3 AC6 12 GLY C 675 THR C 676 GLY C 677 LYS C 680
SITE 1 AC7 11 ASP C 42 ASN C 44 VAL C 45 GLN D 71
SITE 2 AC7 11 TYR D 75 ARG D 309 ARG D 310 LYS D 315
SITE 3 AC7 11 PHE D 316 GLY D 317 CYS D 318
SITE 1 AC8 13 TYR D 90 GLY D 135 TRP D 491 LYS D 568
SITE 2 AC8 13 ARG D 569 LYS D 574 TYR D 648 ARG D 649
SITE 3 AC8 13 VAL D 650 THR D 676 GLY D 677 ASN D 678
SITE 4 AC8 13 LYS D 680
CRYST1 169.900 209.900 123.400 90.00 90.00 90.00 P 21 21 2 16
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 0.005886 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008104 0.00000
MTRIX1 1 -0.350535 -0.933351 0.077341 131.83342 1
MTRIX2 1 -0.934715 0.343488 -0.091235 97.40679 1
MTRIX3 1 0.058589 -0.104273 -0.992821 73.89686 1
MTRIX1 2 0.353237 0.935351 0.018495 -25.14774 1
MTRIX2 2 0.935352 -0.353489 0.012713 35.31074 1
MTRIX3 2 0.018429 0.012808 -0.999748 68.63091 1
MTRIX1 3 -0.994780 0.008122 -0.101724 114.06797 1
MTRIX2 3 -0.015958 -0.996945 0.076459 127.50858 1
MTRIX3 3 -0.100792 0.077683 0.991870 0.79177 1
(ATOM LINES ARE NOT SHOWN.)
END
