HEADER LYASE 07-SEP-04 1XDM
TITLE STRUCTURE OF HUMAN ALDOLASE B ASSOCIATED WITH HEREDITARY FRUCTOSE
TITLE 2 INTOLERANCE (A149P), AT 291K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE B;
COMPND 3 CHAIN: A, B, C, D, W, X, Y, Z;
COMPND 4 SYNONYM: LIVER-TYPE ALDOLASE;
COMPND 5 EC: 4.1.2.13;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDOB, ALDB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5-ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-AP
KEYWDS ALPHA/BETA BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.D.MALAY,K.N.ALLEN,D.R.TOLAN
REVDAT 4 23-AUG-23 1XDM 1 REMARK
REVDAT 3 20-OCT-21 1XDM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1XDM 1 VERSN
REVDAT 1 22-MAR-05 1XDM 0
JRNL AUTH A.D.MALAY,K.N.ALLEN,D.R.TOLAN
JRNL TITL STRUCTURE OF THE THERMOLABILE MUTANT ALDOLASE B, A149P:
JRNL TITL 2 MOLECULAR BASIS OF HEREDITARY FRUCTOSE INTOLERANCE.
JRNL REF J.MOL.BIOL. V. 347 135 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15733923
JRNL DOI 10.1016/J.JMB.2005.01.008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.D.MALAY,S.L.PROCIOUS,D.R.TOLAN
REMARK 1 TITL THE TEMPERATURE DEPENDENCE OF ACTIVITY AND STRUCTURE FOR THE
REMARK 1 TITL 2 MOST PREVALENT MUTANT ALDOLASE B ASSOCIATED WITH HEREDITARY
REMARK 1 TITL 3 FRUCTOSE INTOLERANCE
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 408 295 2002
REMARK 1 REFN ISSN 0003-9861
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 295432.840
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 79141
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) : 0.271
REMARK 3 FREE R VALUE : 0.319
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7920
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.11
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5370
REMARK 3 BIN R VALUE (WORKING SET) : 0.4370
REMARK 3 BIN FREE R VALUE : 0.4480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 650
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18475
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 16.20000
REMARK 3 B22 (A**2) : 12.39000
REMARK 3 B33 (A**2) : -28.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 1.02
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
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 : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 13.42
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED NCS RESTRAINTS BETWEEN MONOMERS
REMARK 4
REMARK 4 1XDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83595
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QO5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, 1,8-DIAMINOOCTANE,
REMARK 280 PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 76.71050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.73750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.71050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.73750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 BIOLOGICAL UNIT OF AP-ALDOLASE IS A DIMER,
REMARK 300 CORRESPONDING TO MONOMER PAIRS AB, CD, WX, AND YZ. THE WILD-TYPE
REMARK 300 ENZYME IS TETRAMERIC.
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: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
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: 2040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
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: 2060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z
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 GLY A -1
REMARK 465 SER A 0
REMARK 465 ALA A 1
REMARK 465 HIS A 2
REMARK 465 ARG A 3
REMARK 465 PHE A 4
REMARK 465 GLN A 110
REMARK 465 GLY A 111
REMARK 465 GLY A 112
REMARK 465 ALA A 113
REMARK 465 PRO A 114
REMARK 465 LEU A 115
REMARK 465 ALA A 116
REMARK 465 GLY A 117
REMARK 465 THR A 118
REMARK 465 ASN A 119
REMARK 465 LYS A 120
REMARK 465 GLU A 121
REMARK 465 THR A 122
REMARK 465 THR A 123
REMARK 465 ILE A 124
REMARK 465 GLN A 125
REMARK 465 VAL A 150
REMARK 465 LEU A 151
REMARK 465 ARG A 152
REMARK 465 ILE A 153
REMARK 465 ALA A 154
REMARK 465 ASP A 155
REMARK 465 GLN A 156
REMARK 465 CYS A 157
REMARK 465 PRO A 158
REMARK 465 PRO A 192
REMARK 465 ASP A 193
REMARK 465 GLY A 194
REMARK 465 GLY A 236
REMARK 465 HIS A 237
REMARK 465 ALA A 238
REMARK 465 CYS A 239
REMARK 465 THR A 240
REMARK 465 LYS A 241
REMARK 465 LYS A 242
REMARK 465 VAL A 343
REMARK 465 HIS A 344
REMARK 465 THR A 345
REMARK 465 GLY A 346
REMARK 465 SER A 347
REMARK 465 SER A 348
REMARK 465 GLY A 349
REMARK 465 ALA A 350
REMARK 465 ALA A 351
REMARK 465 SER A 352
REMARK 465 THR A 353
REMARK 465 GLN A 354
REMARK 465 SER A 355
REMARK 465 LEU A 356
REMARK 465 PHE A 357
REMARK 465 THR A 358
REMARK 465 ALA A 359
REMARK 465 CYS A 360
REMARK 465 TYR A 361
REMARK 465 THR A 362
REMARK 465 TYR A 363
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ALA B 1
REMARK 465 HIS B 2
REMARK 465 ARG B 3
REMARK 465 PHE B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 110
REMARK 465 GLY B 111
REMARK 465 GLY B 112
REMARK 465 ALA B 113
REMARK 465 PRO B 114
REMARK 465 LEU B 115
REMARK 465 ALA B 116
REMARK 465 GLY B 117
REMARK 465 THR B 118
REMARK 465 ASN B 119
REMARK 465 LYS B 120
REMARK 465 GLU B 121
REMARK 465 THR B 122
REMARK 465 THR B 123
REMARK 465 ILE B 124
REMARK 465 GLN B 125
REMARK 465 GLY B 126
REMARK 465 LEU B 127
REMARK 465 VAL B 150
REMARK 465 LEU B 151
REMARK 465 ARG B 152
REMARK 465 ILE B 153
REMARK 465 ALA B 154
REMARK 465 ASP B 155
REMARK 465 GLN B 156
REMARK 465 CYS B 157
REMARK 465 PRO B 158
REMARK 465 GLY B 194
REMARK 465 ASP B 195
REMARK 465 HIS B 196
REMARK 465 ALA B 235
REMARK 465 GLY B 236
REMARK 465 HIS B 237
REMARK 465 ALA B 238
REMARK 465 CYS B 239
REMARK 465 THR B 240
REMARK 465 GLY B 346
REMARK 465 SER B 347
REMARK 465 SER B 348
REMARK 465 GLY B 349
REMARK 465 ALA B 350
REMARK 465 ALA B 351
REMARK 465 SER B 352
REMARK 465 THR B 353
REMARK 465 GLN B 354
REMARK 465 SER B 355
REMARK 465 LEU B 356
REMARK 465 PHE B 357
REMARK 465 THR B 358
REMARK 465 ALA B 359
REMARK 465 CYS B 360
REMARK 465 TYR B 361
REMARK 465 THR B 362
REMARK 465 TYR B 363
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 ALA C 1
REMARK 465 HIS C 2
REMARK 465 ARG C 3
REMARK 465 PHE C 4
REMARK 465 PRO C 5
REMARK 465 GLN C 110
REMARK 465 GLY C 111
REMARK 465 GLY C 112
REMARK 465 ALA C 113
REMARK 465 PRO C 114
REMARK 465 LEU C 115
REMARK 465 ALA C 116
REMARK 465 GLY C 117
REMARK 465 THR C 118
REMARK 465 ASN C 119
REMARK 465 LYS C 120
REMARK 465 GLU C 121
REMARK 465 THR C 122
REMARK 465 THR C 123
REMARK 465 ILE C 124
REMARK 465 GLN C 125
REMARK 465 GLY C 126
REMARK 465 LEU C 127
REMARK 465 ASP C 128
REMARK 465 GLY C 129
REMARK 465 ARG C 148
REMARK 465 PRO C 149
REMARK 465 VAL C 150
REMARK 465 LEU C 151
REMARK 465 ARG C 152
REMARK 465 ILE C 153
REMARK 465 ALA C 154
REMARK 465 ASP C 155
REMARK 465 GLN C 156
REMARK 465 CYS C 157
REMARK 465 PRO C 158
REMARK 465 ASP C 193
REMARK 465 GLY C 194
REMARK 465 ASP C 195
REMARK 465 HIS C 196
REMARK 465 ALA C 235
REMARK 465 GLY C 236
REMARK 465 HIS C 237
REMARK 465 ALA C 238
REMARK 465 CYS C 239
REMARK 465 THR C 240
REMARK 465 GLY C 346
REMARK 465 SER C 347
REMARK 465 SER C 348
REMARK 465 GLY C 349
REMARK 465 ALA C 350
REMARK 465 ALA C 351
REMARK 465 SER C 352
REMARK 465 THR C 353
REMARK 465 GLN C 354
REMARK 465 SER C 355
REMARK 465 LEU C 356
REMARK 465 PHE C 357
REMARK 465 THR C 358
REMARK 465 ALA C 359
REMARK 465 CYS C 360
REMARK 465 TYR C 361
REMARK 465 THR C 362
REMARK 465 TYR C 363
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 ALA D 1
REMARK 465 HIS D 2
REMARK 465 ARG D 3
REMARK 465 PHE D 4
REMARK 465 PRO D 5
REMARK 465 GLN D 110
REMARK 465 GLY D 111
REMARK 465 GLY D 112
REMARK 465 ALA D 113
REMARK 465 PRO D 114
REMARK 465 LEU D 115
REMARK 465 ALA D 116
REMARK 465 GLY D 117
REMARK 465 THR D 118
REMARK 465 ASN D 119
REMARK 465 LYS D 120
REMARK 465 GLU D 121
REMARK 465 THR D 122
REMARK 465 THR D 123
REMARK 465 ILE D 124
REMARK 465 GLN D 125
REMARK 465 GLY D 126
REMARK 465 LEU D 127
REMARK 465 VAL D 150
REMARK 465 LEU D 151
REMARK 465 ARG D 152
REMARK 465 ILE D 153
REMARK 465 ALA D 154
REMARK 465 ASP D 155
REMARK 465 GLN D 156
REMARK 465 CYS D 157
REMARK 465 VAL D 190
REMARK 465 ILE D 191
REMARK 465 PRO D 192
REMARK 465 ASP D 193
REMARK 465 GLY D 194
REMARK 465 ASP D 195
REMARK 465 HIS D 196
REMARK 465 ALA D 235
REMARK 465 GLY D 236
REMARK 465 HIS D 237
REMARK 465 ALA D 238
REMARK 465 CYS D 239
REMARK 465 THR D 240
REMARK 465 LYS D 241
REMARK 465 LYS D 242
REMARK 465 VAL D 343
REMARK 465 HIS D 344
REMARK 465 THR D 345
REMARK 465 GLY D 346
REMARK 465 SER D 347
REMARK 465 SER D 348
REMARK 465 GLY D 349
REMARK 465 ALA D 350
REMARK 465 ALA D 351
REMARK 465 SER D 352
REMARK 465 THR D 353
REMARK 465 GLN D 354
REMARK 465 SER D 355
REMARK 465 LEU D 356
REMARK 465 PHE D 357
REMARK 465 THR D 358
REMARK 465 ALA D 359
REMARK 465 CYS D 360
REMARK 465 TYR D 361
REMARK 465 THR D 362
REMARK 465 TYR D 363
REMARK 465 GLY W -1
REMARK 465 SER W 0
REMARK 465 ALA W 1
REMARK 465 HIS W 2
REMARK 465 ARG W 3
REMARK 465 PHE W 4
REMARK 465 PRO W 5
REMARK 465 ASP W 109
REMARK 465 GLN W 110
REMARK 465 GLY W 111
REMARK 465 GLY W 112
REMARK 465 ALA W 113
REMARK 465 PRO W 114
REMARK 465 LEU W 115
REMARK 465 ALA W 116
REMARK 465 GLY W 117
REMARK 465 THR W 118
REMARK 465 ASN W 119
REMARK 465 LYS W 120
REMARK 465 GLU W 121
REMARK 465 THR W 122
REMARK 465 THR W 123
REMARK 465 ILE W 124
REMARK 465 GLN W 125
REMARK 465 GLY W 126
REMARK 465 LEU W 127
REMARK 465 ASP W 128
REMARK 465 VAL W 150
REMARK 465 LEU W 151
REMARK 465 ARG W 152
REMARK 465 ILE W 153
REMARK 465 ALA W 154
REMARK 465 ASP W 155
REMARK 465 GLN W 156
REMARK 465 CYS W 157
REMARK 465 ILE W 191
REMARK 465 PRO W 192
REMARK 465 ASP W 193
REMARK 465 GLY W 194
REMARK 465 ASP W 195
REMARK 465 ALA W 235
REMARK 465 GLY W 236
REMARK 465 HIS W 237
REMARK 465 ALA W 238
REMARK 465 CYS W 239
REMARK 465 THR W 240
REMARK 465 LYS W 241
REMARK 465 LYS W 242
REMARK 465 HIS W 344
REMARK 465 THR W 345
REMARK 465 GLY W 346
REMARK 465 SER W 347
REMARK 465 SER W 348
REMARK 465 GLY W 349
REMARK 465 ALA W 350
REMARK 465 ALA W 351
REMARK 465 SER W 352
REMARK 465 THR W 353
REMARK 465 GLN W 354
REMARK 465 SER W 355
REMARK 465 LEU W 356
REMARK 465 PHE W 357
REMARK 465 THR W 358
REMARK 465 ALA W 359
REMARK 465 CYS W 360
REMARK 465 TYR W 361
REMARK 465 THR W 362
REMARK 465 TYR W 363
REMARK 465 GLY X -1
REMARK 465 SER X 0
REMARK 465 ALA X 1
REMARK 465 HIS X 2
REMARK 465 ARG X 3
REMARK 465 PHE X 4
REMARK 465 PRO X 5
REMARK 465 GLN X 110
REMARK 465 GLY X 111
REMARK 465 GLY X 112
REMARK 465 ALA X 113
REMARK 465 PRO X 114
REMARK 465 LEU X 115
REMARK 465 ALA X 116
REMARK 465 GLY X 117
REMARK 465 THR X 118
REMARK 465 ASN X 119
REMARK 465 LYS X 120
REMARK 465 GLU X 121
REMARK 465 THR X 122
REMARK 465 THR X 123
REMARK 465 ILE X 124
REMARK 465 GLN X 125
REMARK 465 GLY X 126
REMARK 465 LEU X 127
REMARK 465 ASP X 128
REMARK 465 GLY X 129
REMARK 465 ARG X 148
REMARK 465 PRO X 149
REMARK 465 VAL X 150
REMARK 465 LEU X 151
REMARK 465 ARG X 152
REMARK 465 ILE X 153
REMARK 465 ALA X 154
REMARK 465 ASP X 155
REMARK 465 GLN X 156
REMARK 465 CYS X 157
REMARK 465 PRO X 158
REMARK 465 ASP X 193
REMARK 465 GLY X 194
REMARK 465 ASP X 195
REMARK 465 HIS X 196
REMARK 465 GLY X 236
REMARK 465 HIS X 237
REMARK 465 THR X 345
REMARK 465 GLY X 346
REMARK 465 SER X 347
REMARK 465 SER X 348
REMARK 465 GLY X 349
REMARK 465 ALA X 350
REMARK 465 ALA X 351
REMARK 465 SER X 352
REMARK 465 THR X 353
REMARK 465 GLN X 354
REMARK 465 SER X 355
REMARK 465 LEU X 356
REMARK 465 PHE X 357
REMARK 465 THR X 358
REMARK 465 ALA X 359
REMARK 465 CYS X 360
REMARK 465 TYR X 361
REMARK 465 THR X 362
REMARK 465 TYR X 363
REMARK 465 GLY Y -1
REMARK 465 SER Y 0
REMARK 465 ALA Y 1
REMARK 465 HIS Y 2
REMARK 465 ARG Y 3
REMARK 465 PHE Y 4
REMARK 465 PRO Y 5
REMARK 465 GLN Y 110
REMARK 465 GLY Y 111
REMARK 465 GLY Y 112
REMARK 465 ALA Y 113
REMARK 465 PRO Y 114
REMARK 465 LEU Y 115
REMARK 465 ALA Y 116
REMARK 465 GLY Y 117
REMARK 465 THR Y 118
REMARK 465 ASN Y 119
REMARK 465 LYS Y 120
REMARK 465 GLU Y 121
REMARK 465 THR Y 122
REMARK 465 THR Y 123
REMARK 465 ILE Y 124
REMARK 465 GLN Y 125
REMARK 465 GLY Y 126
REMARK 465 LEU Y 127
REMARK 465 VAL Y 150
REMARK 465 LEU Y 151
REMARK 465 ARG Y 152
REMARK 465 ILE Y 153
REMARK 465 ALA Y 154
REMARK 465 ASP Y 155
REMARK 465 GLN Y 156
REMARK 465 CYS Y 157
REMARK 465 PRO Y 158
REMARK 465 GLY Y 194
REMARK 465 ASP Y 195
REMARK 465 HIS Y 196
REMARK 465 ALA Y 235
REMARK 465 GLY Y 236
REMARK 465 HIS Y 237
REMARK 465 ALA Y 238
REMARK 465 CYS Y 239
REMARK 465 THR Y 240
REMARK 465 GLY Y 346
REMARK 465 SER Y 347
REMARK 465 SER Y 348
REMARK 465 GLY Y 349
REMARK 465 ALA Y 350
REMARK 465 ALA Y 351
REMARK 465 SER Y 352
REMARK 465 THR Y 353
REMARK 465 GLN Y 354
REMARK 465 SER Y 355
REMARK 465 LEU Y 356
REMARK 465 PHE Y 357
REMARK 465 THR Y 358
REMARK 465 ALA Y 359
REMARK 465 CYS Y 360
REMARK 465 TYR Y 361
REMARK 465 THR Y 362
REMARK 465 TYR Y 363
REMARK 465 GLY Z -1
REMARK 465 SER Z 0
REMARK 465 ALA Z 1
REMARK 465 HIS Z 2
REMARK 465 ARG Z 3
REMARK 465 PHE Z 4
REMARK 465 GLN Z 110
REMARK 465 GLY Z 111
REMARK 465 GLY Z 112
REMARK 465 ALA Z 113
REMARK 465 PRO Z 114
REMARK 465 LEU Z 115
REMARK 465 ALA Z 116
REMARK 465 GLY Z 117
REMARK 465 THR Z 118
REMARK 465 ASN Z 119
REMARK 465 LYS Z 120
REMARK 465 GLU Z 121
REMARK 465 THR Z 122
REMARK 465 THR Z 123
REMARK 465 ILE Z 124
REMARK 465 GLN Z 125
REMARK 465 GLY Z 126
REMARK 465 LEU Z 127
REMARK 465 PRO Z 149
REMARK 465 VAL Z 150
REMARK 465 LEU Z 151
REMARK 465 ARG Z 152
REMARK 465 ILE Z 153
REMARK 465 ALA Z 154
REMARK 465 ASP Z 155
REMARK 465 GLN Z 156
REMARK 465 CYS Z 157
REMARK 465 PRO Z 158
REMARK 465 VAL Z 190
REMARK 465 ILE Z 191
REMARK 465 PRO Z 192
REMARK 465 ASP Z 193
REMARK 465 GLY Z 194
REMARK 465 ASP Z 195
REMARK 465 HIS Z 196
REMARK 465 ALA Z 235
REMARK 465 GLY Z 236
REMARK 465 HIS Z 237
REMARK 465 ALA Z 238
REMARK 465 CYS Z 239
REMARK 465 THR Z 240
REMARK 465 LYS Z 241
REMARK 465 LYS Z 242
REMARK 465 VAL Z 343
REMARK 465 HIS Z 344
REMARK 465 THR Z 345
REMARK 465 GLY Z 346
REMARK 465 SER Z 347
REMARK 465 SER Z 348
REMARK 465 GLY Z 349
REMARK 465 ALA Z 350
REMARK 465 ALA Z 351
REMARK 465 SER Z 352
REMARK 465 THR Z 353
REMARK 465 GLN Z 354
REMARK 465 SER Z 355
REMARK 465 LEU Z 356
REMARK 465 PHE Z 357
REMARK 465 THR Z 358
REMARK 465 ALA Z 359
REMARK 465 CYS Z 360
REMARK 465 TYR Z 361
REMARK 465 THR Z 362
REMARK 465 TYR Z 363
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS D 339 O HOH D 367 2.19
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 C 94 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG C 94 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG C 94 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 PRO D 261 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO W 261 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG X 94 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG X 94 NE - CZ - NH1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG X 94 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ILE X 191 N - CA - C ANGL. DEV. = 25.9 DEGREES
REMARK 500 PRO X 192 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 24 -45.37 -18.97
REMARK 500 ALA A 31 58.84 -93.06
REMARK 500 ALA A 32 71.67 -100.01
REMARK 500 ASP A 33 14.08 -153.33
REMARK 500 GLU A 34 150.99 -46.15
REMARK 500 ILE A 46 18.76 -69.99
REMARK 500 ASN A 54 -2.63 -53.89
REMARK 500 VAL A 65 153.17 -44.17
REMARK 500 ASP A 66 150.94 -32.94
REMARK 500 ASN A 70 22.09 -65.99
REMARK 500 GLU A 81 -74.64 -34.94
REMARK 500 LEU A 83 -8.52 -56.26
REMARK 500 SER A 88 -61.60 -18.06
REMARK 500 GLN A 89 30.64 -77.79
REMARK 500 LYS A 100 6.53 -62.72
REMARK 500 ASP A 140 23.42 -76.44
REMARK 500 ASN A 180 52.66 -108.76
REMARK 500 HIS A 196 -177.81 -69.17
REMARK 500 TYR A 222 99.84 -59.59
REMARK 500 VAL A 233 91.09 -53.57
REMARK 500 PRO A 245 -39.47 -38.49
REMARK 500 ALA A 263 -8.51 -59.24
REMARK 500 PRO A 290 66.23 -69.87
REMARK 500 LYS A 293 38.70 -145.03
REMARK 500 PRO A 294 0.64 -38.70
REMARK 500 ALA A 307 -73.49 -18.46
REMARK 500 ALA A 312 12.90 -57.85
REMARK 500 TRP A 313 -70.74 -125.91
REMARK 500 ASN A 319 31.51 -90.25
REMARK 500 LEU B 7 133.36 -33.50
REMARK 500 GLN B 9 -9.66 -55.73
REMARK 500 ALA B 24 -88.39 -58.94
REMARK 500 VAL B 36 -77.51 -21.65
REMARK 500 LEU B 62 -71.83 -54.22
REMARK 500 HIS B 80 -76.67 -24.59
REMARK 500 LYS B 100 30.41 -81.14
REMARK 500 LEU B 130 -70.26 -55.80
REMARK 500 PHE B 144 142.90 -176.65
REMARK 500 TRP B 147 113.43 -169.98
REMARK 500 PRO B 188 -160.24 -77.00
REMARK 500 VAL B 190 160.85 172.55
REMARK 500 PRO B 192 -17.15 -49.97
REMARK 500 TYR B 222 86.14 -62.16
REMARK 500 LYS B 229 71.95 -112.91
REMARK 500 THR B 254 -73.71 -51.30
REMARK 500 PRO B 261 152.83 -46.35
REMARK 500 PRO B 290 57.42 -65.65
REMARK 500 LYS B 293 79.11 -151.36
REMARK 500 SER B 298 -156.04 -106.13
REMARK 500 ALA B 307 -74.30 -36.83
REMARK 500
REMARK 500 THIS ENTRY HAS 222 RAMACHANDRAN OUTLIERS.
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 X 213 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 W 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 Y 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 Z 364
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XDL RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTALLIZED AT 277K
DBREF 1XDM A 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM B 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM C 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM D 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM W 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM X 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM Y 1 363 UNP P05062 ALDOB_HUMAN 1 363
DBREF 1XDM Z 1 363 UNP P05062 ALDOB_HUMAN 1 363
SEQADV 1XDM GLY A -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER A 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO A 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY B -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER B 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO B 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY C -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER C 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO C 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY D -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER D 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO D 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY W -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER W 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO W 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY X -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER X 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO X 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY Y -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER Y 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO Y 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQADV 1XDM GLY Z -1 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM SER Z 0 UNP P05062 CLONING ARTIFACT
SEQADV 1XDM PRO Z 149 UNP P05062 ALA 149 ENGINEERED MUTATION
SEQRES 1 A 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 A 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 A 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 A 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 A 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 A 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 A 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 A 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 A 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 A 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 A 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 A 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 A 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 A 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 A 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 A 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 A 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 A 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 A 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 A 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 A 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 A 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 A 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 A 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 A 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 A 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 A 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 A 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 A 365 TYR
SEQRES 1 B 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 B 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 B 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 B 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 B 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 B 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 B 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 B 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 B 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 B 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 B 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 B 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 B 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 B 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 B 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 B 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 B 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 B 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 B 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 B 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 B 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 B 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 B 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 B 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 B 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 B 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 B 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 B 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 B 365 TYR
SEQRES 1 C 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 C 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 C 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 C 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 C 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 C 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 C 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 C 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 C 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 C 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 C 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 C 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 C 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 C 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 C 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 C 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 C 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 C 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 C 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 C 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 C 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 C 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 C 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 C 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 C 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 C 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 C 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 C 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 C 365 TYR
SEQRES 1 D 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 D 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 D 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 D 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 D 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 D 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 D 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 D 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 D 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 D 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 D 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 D 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 D 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 D 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 D 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 D 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 D 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 D 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 D 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 D 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 D 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 D 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 D 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 D 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 D 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 D 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 D 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 D 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 D 365 TYR
SEQRES 1 W 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 W 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 W 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 W 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 W 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 W 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 W 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 W 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 W 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 W 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 W 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 W 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 W 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 W 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 W 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 W 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 W 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 W 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 W 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 W 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 W 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 W 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 W 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 W 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 W 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 W 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 W 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 W 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 W 365 TYR
SEQRES 1 X 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 X 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 X 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 X 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 X 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 X 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 X 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 X 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 X 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 X 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 X 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 X 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 X 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 X 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 X 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 X 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 X 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 X 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 X 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 X 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 X 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 X 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 X 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 X 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 X 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 X 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 X 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 X 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 X 365 TYR
SEQRES 1 Y 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 Y 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 Y 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 Y 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 Y 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 Y 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 Y 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 Y 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 Y 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 Y 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 Y 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 Y 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 Y 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 Y 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 Y 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 Y 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 Y 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 Y 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 Y 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 Y 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 Y 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 Y 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 Y 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 Y 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 Y 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 Y 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 Y 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 Y 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 Y 365 TYR
SEQRES 1 Z 365 GLY SER ALA HIS ARG PHE PRO ALA LEU THR GLN GLU GLN
SEQRES 2 Z 365 LYS LYS GLU LEU SER GLU ILE ALA GLN SER ILE VAL ALA
SEQRES 3 Z 365 ASN GLY LYS GLY ILE LEU ALA ALA ASP GLU SER VAL GLY
SEQRES 4 Z 365 THR MET GLY ASN ARG LEU GLN ARG ILE LYS VAL GLU ASN
SEQRES 5 Z 365 THR GLU GLU ASN ARG ARG GLN PHE ARG GLU ILE LEU PHE
SEQRES 6 Z 365 SER VAL ASP SER SER ILE ASN GLN SER ILE GLY GLY VAL
SEQRES 7 Z 365 ILE LEU PHE HIS GLU THR LEU TYR GLN LYS ASP SER GLN
SEQRES 8 Z 365 GLY LYS LEU PHE ARG ASN ILE LEU LYS GLU LYS GLY ILE
SEQRES 9 Z 365 VAL VAL GLY ILE LYS LEU ASP GLN GLY GLY ALA PRO LEU
SEQRES 10 Z 365 ALA GLY THR ASN LYS GLU THR THR ILE GLN GLY LEU ASP
SEQRES 11 Z 365 GLY LEU SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY
SEQRES 12 Z 365 VAL ASP PHE GLY LYS TRP ARG PRO VAL LEU ARG ILE ALA
SEQRES 13 Z 365 ASP GLN CYS PRO SER SER LEU ALA ILE GLN GLU ASN ALA
SEQRES 14 Z 365 ASN ALA LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN
SEQRES 15 Z 365 GLY LEU VAL PRO ILE VAL GLU PRO GLU VAL ILE PRO ASP
SEQRES 16 Z 365 GLY ASP HIS ASP LEU GLU HIS CYS GLN TYR VAL THR GLU
SEQRES 17 Z 365 LYS VAL LEU ALA ALA VAL TYR LYS ALA LEU ASN ASP HIS
SEQRES 18 Z 365 HIS VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET
SEQRES 19 Z 365 VAL THR ALA GLY HIS ALA CYS THR LYS LYS TYR THR PRO
SEQRES 20 Z 365 GLU GLN VAL ALA MET ALA THR VAL THR ALA LEU HIS ARG
SEQRES 21 Z 365 THR VAL PRO ALA ALA VAL PRO GLY ILE CYS PHE LEU SER
SEQRES 22 Z 365 GLY GLY MET SER GLU GLU ASP ALA THR LEU ASN LEU ASN
SEQRES 23 Z 365 ALA ILE ASN LEU CYS PRO LEU PRO LYS PRO TRP LYS LEU
SEQRES 24 Z 365 SER PHE SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU
SEQRES 25 Z 365 ALA ALA TRP GLY GLY LYS ALA ALA ASN LYS GLU ALA THR
SEQRES 26 Z 365 GLN GLU ALA PHE MET LYS ARG ALA MET ALA ASN CYS GLN
SEQRES 27 Z 365 ALA ALA LYS GLY GLN TYR VAL HIS THR GLY SER SER GLY
SEQRES 28 Z 365 ALA ALA SER THR GLN SER LEU PHE THR ALA CYS TYR THR
SEQRES 29 Z 365 TYR
HET SO4 A 364 5
HET SO4 B 364 5
HET SO4 C 364 5
HET SO4 C 365 5
HET SO4 W 364 5
HET SO4 X 364 5
HET SO4 Y 364 5
HET SO4 Z 364 5
HETNAM SO4 SULFATE ION
FORMUL 9 SO4 8(O4 S 2-)
FORMUL 17 HOH *35(H2 O)
HELIX 1 1 THR A 8 ILE A 22 1 15
HELIX 2 2 SER A 35 ILE A 46 1 12
HELIX 3 3 THR A 51 VAL A 65 1 15
HELIX 4 4 ASP A 66 GLN A 71 5 6
HELIX 5 5 HIS A 80 TYR A 84 5 5
HELIX 6 6 PHE A 93 LYS A 100 1 8
HELIX 7 7 GLY A 129 ASP A 140 1 12
HELIX 8 8 SER A 159 GLN A 178 1 20
HELIX 9 9 GLN A 179 GLY A 181 5 3
HELIX 10 10 ASP A 197 HIS A 219 1 23
HELIX 11 11 THR A 244 ARG A 258 1 15
HELIX 12 12 GLU A 277 ASN A 287 1 11
HELIX 13 13 GLY A 302 ALA A 312 1 11
HELIX 14 14 ASN A 319 ALA A 338 1 20
HELIX 15 15 THR B 8 VAL B 23 1 16
HELIX 16 16 SER B 35 ILE B 46 1 12
HELIX 17 17 THR B 51 VAL B 65 1 15
HELIX 18 18 ASP B 66 GLN B 71 5 6
HELIX 19 19 HIS B 80 GLN B 85 5 6
HELIX 20 20 LEU B 92 LYS B 100 1 9
HELIX 21 21 GLY B 129 ASP B 140 1 12
HELIX 22 22 SER B 159 ASN B 180 1 22
HELIX 23 23 ASP B 197 HIS B 219 1 23
HELIX 24 24 TYR B 222 THR B 226 5 5
HELIX 25 25 THR B 244 VAL B 260 1 17
HELIX 26 26 SER B 275 CYS B 289 1 15
HELIX 27 27 GLY B 302 ALA B 312 1 11
HELIX 28 28 LYS B 316 ALA B 318 5 3
HELIX 29 29 ASN B 319 LYS B 339 1 21
HELIX 30 30 THR C 8 VAL C 23 1 16
HELIX 31 31 SER C 35 ILE C 46 1 12
HELIX 32 32 GLU C 53 VAL C 65 1 13
HELIX 33 33 ASP C 66 GLN C 71 5 6
HELIX 34 34 GLU C 81 GLN C 85 5 5
HELIX 35 35 LEU C 92 LYS C 100 1 9
HELIX 36 36 LEU C 130 GLY C 141 1 12
HELIX 37 37 SER C 159 GLY C 181 1 23
HELIX 38 38 ASP C 197 HIS C 219 1 23
HELIX 39 39 TYR C 222 THR C 226 5 5
HELIX 40 40 THR C 244 VAL C 260 1 17
HELIX 41 41 GLU C 277 LEU C 288 1 12
HELIX 42 42 GLY C 302 ALA C 312 1 11
HELIX 43 43 ASN C 319 GLY C 340 1 22
HELIX 44 44 THR D 8 SER D 21 1 14
HELIX 45 45 SER D 35 ILE D 46 1 12
HELIX 46 46 THR D 51 SER D 64 1 14
HELIX 47 47 SER D 68 SER D 72 1 5
HELIX 48 48 GLU D 81 GLN D 85 5 5
HELIX 49 49 LEU D 92 LYS D 100 1 9
HELIX 50 50 GLY D 129 ASP D 140 1 12
HELIX 51 51 LEU D 161 ASN D 180 1 20
HELIX 52 52 ASP D 197 HIS D 219 1 23
HELIX 53 53 TYR D 222 THR D 226 5 5
HELIX 54 54 THR D 244 VAL D 260 1 17
HELIX 55 55 SER D 275 CYS D 289 1 15
HELIX 56 56 GLY D 302 ALA D 312 1 11
HELIX 57 57 LYS D 316 ALA D 318 5 3
HELIX 58 58 ASN D 319 GLY D 340 1 22
HELIX 59 59 THR W 8 SER W 21 1 14
HELIX 60 60 SER W 35 ILE W 46 1 12
HELIX 61 61 THR W 51 SER W 64 1 14
HELIX 62 62 SER W 68 SER W 72 1 5
HELIX 63 63 GLU W 81 GLN W 85 5 5
HELIX 64 64 LEU W 92 LYS W 100 1 9
HELIX 65 65 GLY W 129 ASP W 140 1 12
HELIX 66 66 LEU W 161 ASN W 180 1 20
HELIX 67 67 ASP W 197 HIS W 219 1 23
HELIX 68 68 TYR W 222 THR W 226 5 5
HELIX 69 69 THR W 244 VAL W 260 1 17
HELIX 70 70 SER W 275 CYS W 289 1 15
HELIX 71 71 GLY W 302 ALA W 312 1 11
HELIX 72 72 LYS W 316 ALA W 318 5 3
HELIX 73 73 ASN W 319 GLY W 340 1 22
HELIX 74 74 THR X 8 VAL X 23 1 16
HELIX 75 75 SER X 35 ILE X 46 1 12
HELIX 76 76 GLU X 53 VAL X 65 1 13
HELIX 77 77 ASP X 66 GLN X 71 5 6
HELIX 78 78 GLU X 81 GLN X 85 5 5
HELIX 79 79 LEU X 92 LYS X 100 1 9
HELIX 80 80 LEU X 130 GLY X 141 1 12
HELIX 81 81 LEU X 161 GLY X 181 1 21
HELIX 82 82 ASP X 197 HIS X 219 1 23
HELIX 83 83 TYR X 222 THR X 226 5 5
HELIX 84 84 THR X 244 VAL X 260 1 17
HELIX 85 85 SER X 275 LEU X 288 1 14
HELIX 86 86 GLY X 302 ALA X 312 1 11
HELIX 87 87 ASN X 319 GLY X 340 1 22
HELIX 88 88 THR Y 8 VAL Y 23 1 16
HELIX 89 89 SER Y 35 ILE Y 46 1 12
HELIX 90 90 THR Y 51 VAL Y 65 1 15
HELIX 91 91 ASP Y 66 GLN Y 71 5 6
HELIX 92 92 HIS Y 80 GLN Y 85 5 6
HELIX 93 93 LEU Y 92 LYS Y 100 1 9
HELIX 94 94 GLY Y 129 ASP Y 140 1 12
HELIX 95 95 SER Y 159 ASN Y 180 1 22
HELIX 96 96 ASP Y 197 HIS Y 219 1 23
HELIX 97 97 TYR Y 222 THR Y 226 5 5
HELIX 98 98 THR Y 244 VAL Y 260 1 17
HELIX 99 99 SER Y 275 CYS Y 289 1 15
HELIX 100 100 GLY Y 302 ALA Y 312 1 11
HELIX 101 101 LYS Y 316 ALA Y 318 5 3
HELIX 102 102 ASN Y 319 LYS Y 339 1 21
HELIX 103 103 THR Z 8 ILE Z 22 1 15
HELIX 104 104 SER Z 35 ILE Z 46 1 12
HELIX 105 105 THR Z 51 VAL Z 65 1 15
HELIX 106 106 ASP Z 66 GLN Z 71 5 6
HELIX 107 107 HIS Z 80 TYR Z 84 5 5
HELIX 108 108 PHE Z 93 LYS Z 100 1 8
HELIX 109 109 GLY Z 129 ASP Z 140 1 12
HELIX 110 110 SER Z 159 GLN Z 178 1 20
HELIX 111 111 GLN Z 179 GLY Z 181 5 3
HELIX 112 112 ASP Z 197 HIS Z 219 1 23
HELIX 113 113 THR Z 244 ARG Z 258 1 15
HELIX 114 114 GLU Z 277 ASN Z 287 1 11
HELIX 115 115 GLY Z 302 ALA Z 312 1 11
HELIX 116 116 ASN Z 319 ALA Z 338 1 20
SHEET 1 A 7 LEU A 227 LEU A 228 0
SHEET 2 A 7 ILE A 185 VAL A 186 1 N VAL A 186 O LEU A 227
SHEET 3 A 7 PHE A 144 TRP A 147 1 N GLY A 145 O ILE A 185
SHEET 4 A 7 VAL A 104 LYS A 107 1 N ILE A 106 O PHE A 144
SHEET 5 A 7 ILE A 73 LEU A 78 1 N LEU A 78 O LYS A 107
SHEET 6 A 7 GLY A 28 ALA A 31 1 N GLY A 28 O GLY A 74
SHEET 7 A 7 SER A 300 TYR A 301 1 O TYR A 301 N ALA A 31
SHEET 1 B 2 LYS A 86 ASP A 87 0
SHEET 2 B 2 LYS A 91 LEU A 92 -1 O LYS A 91 N ASP A 87
SHEET 1 C 9 GLY B 28 ALA B 32 0
SHEET 2 C 9 ILE B 73 LEU B 78 1 O ILE B 77 N LEU B 30
SHEET 3 C 9 VAL B 103 LYS B 107 1 O GLY B 105 N VAL B 76
SHEET 4 C 9 VAL B 142 TRP B 147 1 O ASP B 143 N VAL B 104
SHEET 5 C 9 ILE B 185 VAL B 186 1 O ILE B 185 N GLY B 145
SHEET 6 C 9 LEU B 227 LEU B 228 1 N LEU B 227 O VAL B 186
SHEET 7 C 9 GLY B 266 PHE B 269 1 O CYS B 268 N LEU B 228
SHEET 8 C 9 LYS B 296 TYR B 301 1 O LYS B 296 N ILE B 267
SHEET 9 C 9 GLY B 28 ALA B 32 1 N ILE B 29 O PHE B 299
SHEET 1 D 6 VAL C 183 PRO C 184 0
SHEET 2 D 6 PHE C 144 LYS C 146 1 N GLY C 145 O VAL C 183
SHEET 3 D 6 VAL C 104 LYS C 107 1 N ILE C 106 O PHE C 144
SHEET 4 D 6 ILE C 73 LEU C 78 1 N LEU C 78 O GLY C 105
SHEET 5 D 6 GLY C 28 ALA C 32 1 N LEU C 30 O ILE C 77
SHEET 6 D 6 SER C 300 TYR C 301 1 O TYR C 301 N ALA C 31
SHEET 1 E 6 GLY D 28 ALA D 31 0
SHEET 2 E 6 ILE D 73 LEU D 78 1 O GLY D 74 N GLY D 28
SHEET 3 E 6 VAL D 103 LYS D 107 1 O GLY D 105 N VAL D 76
SHEET 4 E 6 PHE D 144 TRP D 147 1 O PHE D 144 N ILE D 106
SHEET 5 E 6 VAL D 183 VAL D 186 1 O ILE D 185 N GLY D 145
SHEET 6 E 6 LEU D 227 LEU D 228 1 O LEU D 227 N VAL D 186
SHEET 1 F 2 GLY D 266 PHE D 269 0
SHEET 2 F 2 LYS D 296 PHE D 299 1 O LYS D 296 N ILE D 267
SHEET 1 G 6 GLY W 28 ALA W 31 0
SHEET 2 G 6 ILE W 73 LEU W 78 1 O GLY W 74 N GLY W 28
SHEET 3 G 6 VAL W 103 LYS W 107 1 O GLY W 105 N VAL W 76
SHEET 4 G 6 PHE W 144 LYS W 146 1 O PHE W 144 N ILE W 106
SHEET 5 G 6 VAL W 183 VAL W 186 1 O ILE W 185 N GLY W 145
SHEET 6 G 6 LEU W 227 LEU W 228 1 O LEU W 227 N PRO W 184
SHEET 1 H 2 GLY W 266 PHE W 269 0
SHEET 2 H 2 LYS W 296 PHE W 299 1 O LYS W 296 N ILE W 267
SHEET 1 I 5 PHE X 144 LYS X 146 0
SHEET 2 I 5 VAL X 104 LYS X 107 1 N ILE X 106 O PHE X 144
SHEET 3 I 5 ILE X 73 LEU X 78 1 N LEU X 78 O GLY X 105
SHEET 4 I 5 GLY X 28 ALA X 32 1 N LEU X 30 O ILE X 77
SHEET 5 I 5 SER X 300 TYR X 301 1 O TYR X 301 N ALA X 31
SHEET 1 J 9 GLY Y 28 ALA Y 32 0
SHEET 2 J 9 ILE Y 73 LEU Y 78 1 O ILE Y 77 N LEU Y 30
SHEET 3 J 9 VAL Y 103 LYS Y 107 1 O GLY Y 105 N VAL Y 76
SHEET 4 J 9 VAL Y 142 TRP Y 147 1 O ASP Y 143 N VAL Y 104
SHEET 5 J 9 VAL Y 183 VAL Y 186 1 O ILE Y 185 N GLY Y 145
SHEET 6 J 9 LEU Y 227 LEU Y 228 1 N LEU Y 227 O VAL Y 186
SHEET 7 J 9 GLY Y 266 PHE Y 269 1 O CYS Y 268 N LEU Y 228
SHEET 8 J 9 LYS Y 296 TYR Y 301 1 O LYS Y 296 N ILE Y 267
SHEET 9 J 9 GLY Y 28 ALA Y 32 1 N ILE Y 29 O PHE Y 299
SHEET 1 K 5 PHE Z 144 LYS Z 146 0
SHEET 2 K 5 VAL Z 103 LYS Z 107 1 N ILE Z 106 O PHE Z 144
SHEET 3 K 5 ILE Z 73 LEU Z 78 1 N VAL Z 76 O VAL Z 103
SHEET 4 K 5 GLY Z 28 ALA Z 31 1 N GLY Z 28 O GLY Z 74
SHEET 5 K 5 SER Z 300 TYR Z 301 1 O TYR Z 301 N ALA Z 31
SHEET 1 L 2 LYS Z 86 ASP Z 87 0
SHEET 2 L 2 LYS Z 91 LEU Z 92 -1 O LYS Z 91 N ASP Z 87
SHEET 1 M 2 ILE Z 185 VAL Z 186 0
SHEET 2 M 2 LEU Z 227 LEU Z 228 1 O LEU Z 227 N VAL Z 186
SITE 1 AC1 5 GLN W 202 THR W 254 ARG W 258 GLN X 9
SITE 2 AC1 5 LYS X 12
SITE 1 AC2 4 LYS A 12 GLN B 202 THR B 254 ARG B 258
SITE 1 AC3 3 LYS W 12 GLN X 202 ARG X 258
SITE 1 AC4 3 GLN Y 202 ARG Y 258 LYS Z 12
SITE 1 AC5 3 GLN C 202 ARG C 258 LYS D 12
SITE 1 AC6 6 GLN A 202 THR A 254 ARG A 258 HOH A 368
SITE 2 AC6 6 GLN B 9 LYS B 12
SITE 1 AC7 6 GLN C 9 LYS C 12 HOH C 368 GLN D 202
SITE 2 AC7 6 THR D 254 ARG D 258
SITE 1 AC8 5 GLN Y 9 LYS Y 12 GLN Z 202 ARG Z 258
SITE 2 AC8 5 HOH Z 367
CRYST1 153.421 153.475 185.553 90.00 90.00 90.00 P 21 21 2 32
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 0.006518 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005389 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
