HEADER TRANSFERASE 06-OCT-04 1XOI
TITLE HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH CHLOROINDOLOYL
TITLE 2 GLYCINE AMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS ALLOSTERIC ENZYME, GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.WRIGHT,V.L.RATH,E.M.GIBBS,J.L.TREADWAY
REVDAT 3 13-JUL-11 1XOI 1 VERSN
REVDAT 2 24-FEB-09 1XOI 1 VERSN
REVDAT 1 12-APR-05 1XOI 0
JRNL AUTH S.W.WRIGHT,V.L.RATH,P.E.GENEREUX,D.L.HAGEMAN,C.B.LEVY,
JRNL AUTH 2 L.D.MCCLURE,S.C.MCCOID,R.K.MCPHERSON,T.M.SCHELHORN,
JRNL AUTH 3 D.E.WILDER,W.J.ZAVADOSKI,E.M.GIBBS,J.L.TREADWAY
JRNL TITL 5-CHLOROINDOLOYL GLYCINE AMIDE INHIBITORS OF GLYCOGEN
JRNL TITL 2 PHOSPHORYLASE: SYNTHESIS, IN VITRO, IN VIVO, AND X-RAY
JRNL TITL 3 CRYSTALLOGRAPHIC CHARACTERIZATION.
JRNL REF BIOORG.MED.CHEM.LETT. V. 15 459 2005
JRNL REFN ISSN 0960-894X
JRNL PMID 15603973
JRNL DOI 10.1016/J.BMCL.2004.10.048
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 114216
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) : 0.206
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300
REMARK 3 FREE R VALUE TEST SET COUNT : 11451
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 : 13016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 636
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1XOI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS - B4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121683
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.03433
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 82.06867
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: 8350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 ALA A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 THR A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 ARG A 10
REMARK 465 ARG A 11
REMARK 465 GLN A 12
REMARK 465 ILE A 13
REMARK 465 SER A 14
REMARK 465 ILE A 15
REMARK 465 ARG A 16
REMARK 465 GLY A 17
REMARK 465 ILE A 18
REMARK 465 VAL A 19
REMARK 465 GLY A 20
REMARK 465 VAL A 21
REMARK 465 GLU A 22
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 ARG 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 ASP A 261
REMARK 465 GLU A 839
REMARK 465 SER A 840
REMARK 465 ASN A 841
REMARK 465 LYS A 842
REMARK 465 VAL A 843
REMARK 465 ASN A 844
REMARK 465 GLY A 845
REMARK 465 ASN A 846
REMARK 465 ALA B 1001
REMARK 465 LYS B 1002
REMARK 465 PRO B 1003
REMARK 465 LEU B 1004
REMARK 465 THR B 1005
REMARK 465 ASP B 1006
REMARK 465 GLN B 1007
REMARK 465 GLU B 1008
REMARK 465 LYS B 1009
REMARK 465 ARG B 1010
REMARK 465 ARG B 1011
REMARK 465 GLN B 1012
REMARK 465 ILE B 1013
REMARK 465 SER B 1014
REMARK 465 ILE B 1015
REMARK 465 ARG B 1016
REMARK 465 GLY B 1017
REMARK 465 ILE B 1018
REMARK 465 VAL B 1019
REMARK 465 GLY B 1020
REMARK 465 VAL B 1021
REMARK 465 GLU B 1022
REMARK 465 ASN B 1250
REMARK 465 ASP B 1251
REMARK 465 PHE B 1252
REMARK 465 ASN B 1253
REMARK 465 LEU B 1254
REMARK 465 ARG B 1255
REMARK 465 ASP B 1256
REMARK 465 PHE B 1257
REMARK 465 ASN B 1258
REMARK 465 VAL B 1259
REMARK 465 GLY B 1260
REMARK 465 ASP B 1261
REMARK 465 GLU B 1839
REMARK 465 SER B 1840
REMARK 465 ASN B 1841
REMARK 465 LYS B 1842
REMARK 465 VAL B 1843
REMARK 465 ASN B 1844
REMARK 465 GLY B 1845
REMARK 465 ASN B 1846
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 PRO B1755 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 131 43.93 -86.99
REMARK 500 PHE A 166 150.57 -49.82
REMARK 500 ARG A 193 72.38 -119.57
REMARK 500 TYR A 203 -132.00 53.87
REMARK 500 ASN A 235 11.95 -144.52
REMARK 500 PRO A 281 25.71 -70.72
REMARK 500 LYS A 315 17.29 59.66
REMARK 500 PHE A 316 158.74 -34.12
REMARK 500 SER A 318 103.78 42.43
REMARK 500 ARG A 320 129.75 -15.10
REMARK 500 ALA A 322 -88.05 47.47
REMARK 500 THR A 324 34.04 33.48
REMARK 500 VAL A 325 -86.27 78.40
REMARK 500 PHE A 326 -5.50 54.29
REMARK 500 ASP A 339 -174.54 69.97
REMARK 500 VAL A 379 -60.20 -124.63
REMARK 500 GLU A 434 131.85 -37.47
REMARK 500 ALA A 456 141.28 -172.13
REMARK 500 LYS A 466 -76.18 -115.14
REMARK 500 PRO A 476 -71.89 -48.41
REMARK 500 ASP A 477 -8.98 -46.63
REMARK 500 LEU A 492 -70.37 -154.77
REMARK 500 LYS A 568 170.61 175.27
REMARK 500 ASP A 593 67.84 -150.01
REMARK 500 PRO A 594 -7.76 -46.98
REMARK 500 SER A 674 -57.86 -148.54
REMARK 500 SER A 751 64.07 -155.11
REMARK 500 LYS A 753 3.31 -66.64
REMARK 500 GLN A 754 72.79 -165.33
REMARK 500 ILE A 824 -54.37 -132.64
REMARK 500 LEU A 832 -153.64 -136.47
REMARK 500 LYS A 833 107.89 -176.76
REMARK 500 ILE A 834 100.70 -54.17
REMARK 500 LEU A 836 -87.39 -125.36
REMARK 500 SER A 837 -169.84 -76.17
REMARK 500 LEU B1131 44.57 -87.13
REMARK 500 ARG B1193 71.01 -117.19
REMARK 500 TYR B1203 -131.00 53.92
REMARK 500 ASN B1235 11.35 -143.14
REMARK 500 PRO B1281 25.65 -70.67
REMARK 500 LYS B1315 83.59 34.74
REMARK 500 SER B1318 119.32 57.63
REMARK 500 ARG B1320 -93.95 -32.15
REMARK 500 ALA B1322 -72.97 13.34
REMARK 500 THR B1324 35.47 -70.70
REMARK 500 VAL B1325 -49.42 70.76
REMARK 500 PHE B1326 -0.46 46.57
REMARK 500 ASP B1339 -174.84 70.11
REMARK 500 THR B1378 144.66 179.63
REMARK 500 GLU B1434 132.16 -37.70
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2302 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH B2497 DISTANCE = 5.33 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PLP A 860
REMARK 610 PLP B 1860
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG A 861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 1861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 288 A 862
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 288 B 1862
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EM6 RELATED DB: PDB
REMARK 900 RELATED ID: 1EXV RELATED DB: PDB
DBREF 1XOI A 1 846 UNP P06737 PHS1_HUMAN 1 846
DBREF 1XOI B 1001 1846 UNP P06737 PHS1_HUMAN 1 846
SEQADV 1XOI ALA A 323 UNP P06737 GLY 323 CONFLICT
SEQADV 1XOI ALA B 1323 UNP P06737 GLY 323 CONFLICT
SEQRES 1 A 846 ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE
SEQRES 2 A 846 SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU
SEQRES 3 A 846 LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 A 846 VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR
SEQRES 5 A 846 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 A 846 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS
SEQRES 7 A 846 PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 A 846 GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU
SEQRES 9 A 846 GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU
SEQRES 10 A 846 ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 A 846 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 A 846 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 A 846 TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS
SEQRES 14 A 846 ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP
SEQRES 15 A 846 LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU
SEQRES 16 A 846 PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS
SEQRES 17 A 846 THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL
SEQRES 18 A 846 LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET
SEQRES 19 A 846 ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG
SEQRES 20 A 846 ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY
SEQRES 21 A 846 ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 A 846 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 A 846 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 A 846 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 A 846 ALA SER LYS PHE GLY SER THR ARG GLY ALA ALA THR VAL
SEQRES 26 A 846 PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN
SEQRES 27 A 846 ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 A 846 ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA
SEQRES 29 A 846 TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS
SEQRES 30 A 846 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP
SEQRES 31 A 846 LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE
SEQRES 32 A 846 TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA
SEQRES 33 A 846 LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 A 846 LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA
SEQRES 35 A 846 HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 A 846 ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE
SEQRES 37 A 846 LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN
SEQRES 38 A 846 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU
SEQRES 39 A 846 CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE
SEQRES 40 A 846 GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS
SEQRES 41 A 846 LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU
SEQRES 42 A 846 LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER
SEQRES 43 A 846 GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO
SEQRES 44 A 846 SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 A 846 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 A 846 MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE
SEQRES 47 A 846 VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 A 846 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 A 846 SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY
SEQRES 50 A 846 SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 A 846 SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER
SEQRES 52 A 846 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 A 846 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 A 846 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 A 846 ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE
SEQRES 56 A 846 ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA
SEQRES 57 A 846 LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL
SEQRES 58 A 846 ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN
SEQRES 59 A 846 PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR
SEQRES 60 A 846 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR
SEQRES 61 A 846 VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN
SEQRES 62 A 846 PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA
SEQRES 63 A 846 ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU
SEQRES 64 A 846 TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU
SEQRES 65 A 846 LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY
SEQRES 66 A 846 ASN
SEQRES 1 B 846 ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE
SEQRES 2 B 846 SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU
SEQRES 3 B 846 LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 B 846 VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR
SEQRES 5 B 846 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 B 846 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS
SEQRES 7 B 846 PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 B 846 GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU
SEQRES 9 B 846 GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU
SEQRES 10 B 846 ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 B 846 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 B 846 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 B 846 TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS
SEQRES 14 B 846 ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP
SEQRES 15 B 846 LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU
SEQRES 16 B 846 PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS
SEQRES 17 B 846 THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL
SEQRES 18 B 846 LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET
SEQRES 19 B 846 ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG
SEQRES 20 B 846 ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY
SEQRES 21 B 846 ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 B 846 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 B 846 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 B 846 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 B 846 ALA SER LYS PHE GLY SER THR ARG GLY ALA ALA THR VAL
SEQRES 26 B 846 PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN
SEQRES 27 B 846 ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 B 846 ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA
SEQRES 29 B 846 TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS
SEQRES 30 B 846 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP
SEQRES 31 B 846 LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE
SEQRES 32 B 846 TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA
SEQRES 33 B 846 LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 B 846 LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA
SEQRES 35 B 846 HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 B 846 ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE
SEQRES 37 B 846 LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN
SEQRES 38 B 846 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU
SEQRES 39 B 846 CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE
SEQRES 40 B 846 GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS
SEQRES 41 B 846 LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU
SEQRES 42 B 846 LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER
SEQRES 43 B 846 GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO
SEQRES 44 B 846 SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 B 846 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 B 846 MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE
SEQRES 47 B 846 VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 B 846 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 B 846 SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY
SEQRES 50 B 846 SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 B 846 SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER
SEQRES 52 B 846 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 B 846 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 B 846 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 B 846 ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE
SEQRES 56 B 846 ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA
SEQRES 57 B 846 LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL
SEQRES 58 B 846 ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN
SEQRES 59 B 846 PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR
SEQRES 60 B 846 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR
SEQRES 61 B 846 VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN
SEQRES 62 B 846 PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA
SEQRES 63 B 846 ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU
SEQRES 64 B 846 TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU
SEQRES 65 B 846 LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY
SEQRES 66 B 846 ASN
HET NBG A 861 15
HET NBG B1861 15
HET PLP A 860 15
HET PLP B1860 15
HET 288 A 862 25
HET 288 B1862 25
HETNAM NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM 288 5-CHLORO-1H-INDOLE-2-CARBOXYLIC ACID{[CYCLOPENTYL-(2-
HETNAM 2 288 HYDROXY-ETHYL)-CARBAMOYL]-METHYL}-AMIDE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 NBG 2(C8 H15 N O6)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 7 288 2(C18 H24 CL N3 O3)
FORMUL 9 HOH *636(H2 O)
HELIX 1 1 ASN A 23 THR A 38 1 16
HELIX 2 2 THR A 47 CYS A 78 1 32
HELIX 3 3 THR A 94 LEU A 102 1 9
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 PRO A 194 MET A 197 5 4
HELIX 8 8 TYR A 262 ASP A 268 1 7
HELIX 9 9 ARG A 269 ASN A 274 1 6
HELIX 10 10 ILE A 275 ARG A 277 5 3
HELIX 11 11 LYS A 289 LYS A 312 1 24
HELIX 12 12 ALA A 328 GLN A 332 1 5
HELIX 13 13 LEU A 344 ILE A 356 1 13
HELIX 14 14 PRO A 360 THR A 371 1 12
HELIX 15 15 LEU A 380 LEU A 384 5 5
HELIX 16 16 VAL A 389 LEU A 396 1 8
HELIX 17 17 LEU A 396 PHE A 418 1 23
HELIX 18 18 ASP A 421 SER A 429 1 9
HELIX 19 19 MET A 441 SER A 449 1 9
HELIX 20 20 ALA A 456 LYS A 466 1 11
HELIX 21 21 PHE A 468 GLU A 475 1 8
HELIX 22 22 ASN A 496 GLY A 508 1 13
HELIX 23 23 GLU A 509 LYS A 513 5 5
HELIX 24 24 ASP A 514 LEU A 525 5 12
HELIX 25 25 ASP A 527 TYR A 553 1 27
HELIX 26 26 ARG A 575 ASP A 593 1 19
HELIX 27 27 TYR A 613 ASP A 633 1 21
HELIX 28 28 VAL A 636 SER A 638 5 3
HELIX 29 29 ARG A 649 ILE A 657 1 9
HELIX 30 30 PRO A 658 THR A 660 5 3
HELIX 31 31 THR A 676 ASN A 684 1 9
HELIX 32 32 ALA A 695 GLY A 704 1 10
HELIX 33 33 GLU A 705 LEU A 708 5 4
HELIX 34 34 ARG A 714 GLY A 725 1 12
HELIX 35 35 GLU A 727 LEU A 735 1 9
HELIX 36 36 LEU A 735 GLY A 748 1 14
HELIX 37 37 PHE A 758 HIS A 768 1 11
HELIX 38 38 LYS A 772 MET A 792 1 21
HELIX 39 39 ASN A 793 ALA A 807 1 15
HELIX 40 40 SER A 808 PHE A 811 5 4
HELIX 41 41 SER A 812 ILE A 824 1 13
HELIX 42 42 ASN B 1023 THR B 1038 1 16
HELIX 43 43 THR B 1047 CYS B 1078 1 32
HELIX 44 44 THR B 1094 LEU B 1102 1 9
HELIX 45 45 LEU B 1104 LEU B 1115 1 12
HELIX 46 46 ASP B 1118 GLU B 1126 1 9
HELIX 47 47 GLY B 1134 LEU B 1150 1 17
HELIX 48 48 PRO B 1194 MET B 1197 5 4
HELIX 49 49 TYR B 1262 ASP B 1268 1 7
HELIX 50 50 ARG B 1269 ASN B 1274 1 6
HELIX 51 51 ILE B 1275 ARG B 1277 5 3
HELIX 52 52 LYS B 1289 ALA B 1313 1 25
HELIX 53 53 ALA B 1328 GLN B 1332 1 5
HELIX 54 54 LEU B 1344 ILE B 1356 1 13
HELIX 55 55 PRO B 1360 THR B 1371 1 12
HELIX 56 56 LEU B 1380 LEU B 1384 5 5
HELIX 57 57 VAL B 1389 LEU B 1396 1 8
HELIX 58 58 LEU B 1396 PHE B 1418 1 23
HELIX 59 59 ASP B 1421 SER B 1429 1 9
HELIX 60 60 MET B 1441 SER B 1449 1 9
HELIX 61 61 ALA B 1456 LYS B 1466 1 11
HELIX 62 62 PHE B 1468 GLU B 1475 1 8
HELIX 63 63 ASN B 1496 GLY B 1508 1 13
HELIX 64 64 GLU B 1509 LYS B 1513 5 5
HELIX 65 65 ASP B 1514 LEU B 1525 5 12
HELIX 66 66 ASP B 1527 TYR B 1553 1 27
HELIX 67 67 HIS B 1571 LYS B 1574 5 4
HELIX 68 68 ARG B 1575 ASP B 1593 1 19
HELIX 69 69 TYR B 1613 ASP B 1633 1 21
HELIX 70 70 VAL B 1636 SER B 1638 5 3
HELIX 71 71 ARG B 1649 ILE B 1657 1 9
HELIX 72 72 PRO B 1658 THR B 1660 5 3
HELIX 73 73 THR B 1676 ASN B 1684 1 9
HELIX 74 74 ALA B 1695 GLY B 1704 1 10
HELIX 75 75 GLU B 1705 LEU B 1708 5 4
HELIX 76 76 ARG B 1714 GLY B 1725 1 12
HELIX 77 77 GLU B 1727 LEU B 1735 1 9
HELIX 78 78 LEU B 1735 GLY B 1748 1 14
HELIX 79 79 PHE B 1758 HIS B 1768 1 11
HELIX 80 80 LYS B 1772 MET B 1792 1 21
HELIX 81 81 ASN B 1793 ALA B 1807 1 15
HELIX 82 82 SER B 1808 PHE B 1811 5 4
HELIX 83 83 SER B 1812 ILE B 1824 1 13
SHEET 1 A 3 LYS A 191 SER A 192 0
SHEET 2 A 3 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 A 3 LEU A 198 PHE A 202 -1 N LEU A 198 O ALA A 223
SHEET 1 B 9 LYS A 191 SER A 192 0
SHEET 2 B 9 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 B 9 VAL A 238 ARG A 247 -1 O ARG A 247 N LEU A 222
SHEET 4 B 9 ALA A 154 ILE A 159 1 N GLY A 156 O ARG A 242
SHEET 5 B 9 ARG A 81 LEU A 85 1 N TYR A 84 O TYR A 155
SHEET 6 B 9 VAL A 333 ASN A 338 1 O ALA A 334 N TYR A 83
SHEET 7 B 9 PHE A 372 THR A 375 1 O ALA A 373 N LEU A 337
SHEET 8 B 9 VAL A 452 GLY A 454 1 O ASN A 453 N TYR A 374
SHEET 9 B 9 PHE A 479 ASN A 481 1 O GLN A 480 N VAL A 452
SHEET 1 C 2 PHE A 89 GLY A 92 0
SHEET 2 C 2 ALA A 129 LEU A 131 -1 O LEU A 131 N PHE A 89
SHEET 1 D 2 ASN A 167 ARG A 171 0
SHEET 2 D 2 TRP A 174 GLU A 178 -1 O VAL A 176 N LYS A 169
SHEET 1 E 2 LYS A 205 THR A 209 0
SHEET 2 E 2 GLY A 212 ILE A 216 -1 O LYS A 214 N GLU A 207
SHEET 1 F 3 ARG A 386 PRO A 388 0
SHEET 2 F 3 ARG A 438 ASN A 440 -1 O ILE A 439 N TRP A 387
SHEET 3 F 3 ILE A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 G 6 LEU A 640 LEU A 645 0
SHEET 2 G 6 ARG A 601 GLY A 606 1 N VAL A 603 O LYS A 641
SHEET 3 G 6 MET A 562 VAL A 567 1 N ASP A 564 O ILE A 604
SHEET 4 G 6 LEU A 662 GLN A 665 1 O LEU A 662 N VAL A 565
SHEET 5 G 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 G 6 PHE A 709 ILE A 710 1 O PHE A 709 N THR A 688
SHEET 1 H 3 LYS B1191 SER B1192 0
SHEET 2 H 3 GLN B1219 PRO B1231 -1 O ASP B1227 N LYS B1191
SHEET 3 H 3 LEU B1198 PHE B1202 -1 N LEU B1198 O ALA B1223
SHEET 1 I 9 LYS B1191 SER B1192 0
SHEET 2 I 9 GLN B1219 PRO B1231 -1 O ASP B1227 N LYS B1191
SHEET 3 I 9 VAL B1238 ARG B1247 -1 O ARG B1247 N LEU B1222
SHEET 4 I 9 ALA B1154 ILE B1159 1 N GLY B1156 O ARG B1242
SHEET 5 I 9 ARG B1081 LEU B1085 1 N TYR B1084 O TYR B1155
SHEET 6 I 9 VAL B1333 ASN B1338 1 O ALA B1334 N TYR B1083
SHEET 7 I 9 PHE B1372 THR B1375 1 O ALA B1373 N LEU B1337
SHEET 8 I 9 VAL B1452 GLY B1454 1 O ASN B1453 N TYR B1374
SHEET 9 I 9 PHE B1479 ASN B1481 1 O GLN B1480 N VAL B1452
SHEET 1 J 2 PHE B1089 GLY B1092 0
SHEET 2 J 2 ALA B1129 LEU B1131 -1 O LEU B1131 N PHE B1089
SHEET 1 K 2 ASN B1167 ARG B1171 0
SHEET 2 K 2 TRP B1174 GLU B1178 -1 O VAL B1176 N LYS B1169
SHEET 1 L 2 LYS B1205 THR B1209 0
SHEET 2 L 2 GLY B1212 ILE B1216 -1 O LYS B1214 N GLU B1207
SHEET 1 M 3 ARG B1386 PRO B1388 0
SHEET 2 M 3 ARG B1438 ASN B1440 -1 O ILE B1439 N TRP B1387
SHEET 3 M 3 ILE B1431 GLU B1432 -1 N GLU B1432 O ARG B1438
SHEET 1 N 6 LEU B1640 LEU B1645 0
SHEET 2 N 6 ARG B1601 GLY B1606 1 N VAL B1603 O LYS B1641
SHEET 3 N 6 MET B1562 VAL B1567 1 N ASP B1564 O ILE B1604
SHEET 4 N 6 LEU B1662 GLN B1665 1 O LEU B1662 N VAL B1565
SHEET 5 N 6 LEU B1687 GLY B1690 1 O LEU B1687 N SER B1663
SHEET 6 N 6 PHE B1709 ILE B1710 1 O PHE B1709 N THR B1688
SITE 1 AC1 12 ASN A 284 HIS A 377 VAL A 455 ASN A 484
SITE 2 AC1 12 TYR A 573 GLU A 672 ALA A 673 SER A 674
SITE 3 AC1 12 GLY A 675 HOH A1981 HOH A2115 HOH A2223
SITE 1 AC2 17 GLY B1135 LEU B1136 ASN B1284 ASP B1339
SITE 2 AC2 17 HIS B1377 THR B1378 VAL B1455 ASN B1484
SITE 3 AC2 17 TYR B1573 GLU B1672 ALA B1673 SER B1674
SITE 4 AC2 17 GLY B1675 HOH B1864 HOH B2086 HOH B2253
SITE 5 AC2 17 HOH B2254
SITE 1 AC3 17 GLY A 134 GLY A 135 LYS A 568 LYS A 574
SITE 2 AC3 17 TYR A 648 ARG A 649 VAL A 650 GLY A 675
SITE 3 AC3 17 THR A 676 GLY A 677 LYS A 680 HOH A1886
SITE 4 AC3 17 HOH A1891 HOH A1981 HOH A2053 HOH A2063
SITE 5 AC3 17 HOH A2154
SITE 1 AC4 17 GLY B1134 GLY B1135 TRP B1491 LYS B1568
SITE 2 AC4 17 LYS B1574 TYR B1648 ARG B1649 VAL B1650
SITE 3 AC4 17 GLY B1675 THR B1676 GLY B1677 LYS B1680
SITE 4 AC4 17 HOH B1907 HOH B1920 HOH B1936 HOH B2015
SITE 5 AC4 17 HOH B2182
SITE 1 AC5 19 ARG A 60 LEU A 63 VAL A 64 TRP A 67
SITE 2 AC5 19 PRO A 188 GLU A 190 LYS A 191 SER A 192
SITE 3 AC5 19 PRO A 194 HOH A1991 HOH A1994 THR B1038
SITE 4 AC5 19 VAL B1040 HIS B1057 TYR B1185 GLY B1186
SITE 5 AC5 19 ASN B1187 PRO B1188 HOH B2228
SITE 1 AC6 16 THR A 38 VAL A 40 HIS A 57 TYR A 185
SITE 2 AC6 16 PRO A 188 ARG B1060 LEU B1063 VAL B1064
SITE 3 AC6 16 TRP B1067 PRO B1188 GLU B1190 LYS B1191
SITE 4 AC6 16 SER B1192 HOH B1911 HOH B1948 HOH B2068
CRYST1 123.906 123.906 123.103 90.00 90.00 120.00 P 31 6
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 0.008071 0.004660 0.000000 0.00000
SCALE2 0.000000 0.009319 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
