HEADER TRANSFERASE 14-JUN-02 1IX7
TITLE ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT V39F MALEATE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.6.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACTIVE SITE MUTANT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HAYASHI,H.MIZUGUCHI,I.MIYAHARA,Y.NAKAJIMA,K.HIROTSU,H.KAGAMIYAMA
REVDAT 6 27-DEC-23 1IX7 1 REMARK
REVDAT 5 10-NOV-21 1IX7 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1IX7 1 VERSN
REVDAT 3 24-FEB-09 1IX7 1 VERSN
REVDAT 2 07-OCT-03 1IX7 1 JRNL
REVDAT 1 03-JUL-02 1IX7 0
JRNL AUTH H.HAYASHI,H.MIZUGUCHI,I.MIYAHARA,Y.NAKAJIMA,K.HIROTSU,
JRNL AUTH 2 H.KAGAMIYAMA
JRNL TITL CONFORMATIONAL CHANGE IN ASPARTATE AMINOTRANSFERASE ON
JRNL TITL 2 SUBSTRATE BINDING INDUCES STRAIN IN THE CATALYTIC GROUP AND
JRNL TITL 3 ENHANCES CATALYSIS
JRNL REF J.BIOL.CHEM. V. 278 9481 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12488449
JRNL DOI 10.1074/JBC.M209235200
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 25797
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.247
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 : 3073
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 76
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
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 1IX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000005367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27153
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 60.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 39.81650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.81650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 79.22250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.91650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 79.22250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.91650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.81650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 79.22250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.91650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.81650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 79.22250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.91650
REMARK 290 SMTRY3 8 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 SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS: X, -Y, -Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 ILE A 17 -60.19 -95.21
REMARK 500 GLU A 28 5.81 -60.11
REMARK 500 LYS A 32 144.38 -38.53
REMARK 500 TYR A 160 -55.00 -157.43
REMARK 500 GLU A 164 -63.47 -97.51
REMARK 500 LEU A 177 -9.88 -58.72
REMARK 500 ALA A 229 -68.39 -93.52
REMARK 500 LEU A 262 32.21 -98.66
REMARK 500 ARG A 266 73.12 58.95
REMARK 500 ASN A 294 -72.99 -105.94
REMARK 500 SER A 296 -64.03 82.37
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 PLP A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAE A 414
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IX6 RELATED DB: PDB
REMARK 900 1IX6 CONTAINS THE SAME PROTEIN WITH ACTIVE SITE MUTANT V39F WITHOUT
REMARK 900 MALEATE
REMARK 900 RELATED ID: 1IX8 RELATED DB: PDB
REMARK 900 1IX8 CONTAINS THE SAME PROTEIN WITH ACTIVE SITE MUTANT V39F/N194A
DBREF 1IX7 A 5 409 UNP P00509 AAT_ECOLI 1 396
SEQADV 1IX7 PHE A 39 UNP P00509 VAL 35 ENGINEERED MUTATION
SEQRES 1 A 396 MET PHE GLU ASN ILE THR ALA ALA PRO ALA ASP PRO ILE
SEQRES 2 A 396 LEU GLY LEU ALA ASP LEU PHE ARG ALA ASP GLU ARG PRO
SEQRES 3 A 396 GLY LYS ILE ASN LEU GLY ILE GLY PHE TYR LYS ASP GLU
SEQRES 4 A 396 THR GLY LYS THR PRO VAL LEU THR SER VAL LYS LYS ALA
SEQRES 5 A 396 GLU GLN TYR LEU LEU GLU ASN GLU THR THR LYS ASN TYR
SEQRES 6 A 396 LEU GLY ILE ASP GLY ILE PRO GLU PHE GLY ARG CYS THR
SEQRES 7 A 396 GLN GLU LEU LEU PHE GLY LYS GLY SER ALA LEU ILE ASN
SEQRES 8 A 396 ASP LYS ARG ALA ARG THR ALA GLN THR PRO GLY GLY THR
SEQRES 9 A 396 GLY ALA LEU ARG VAL ALA ALA ASP PHE LEU ALA LYS ASN
SEQRES 10 A 396 THR SER VAL LYS ARG VAL TRP VAL SER ASN PRO SER TRP
SEQRES 11 A 396 PRO ASN HIS LYS SER VAL PHE ASN SER ALA GLY LEU GLU
SEQRES 12 A 396 VAL ARG GLU TYR ALA TYR TYR ASP ALA GLU ASN HIS THR
SEQRES 13 A 396 LEU ASP PHE ASP ALA LEU ILE ASN SER LEU ASN GLU ALA
SEQRES 14 A 396 GLN ALA GLY ASP VAL VAL LEU PHE HIS GLY CYS CYS HIS
SEQRES 15 A 396 ASN PRO THR GLY ILE ASP PRO THR LEU GLU GLN TRP GLN
SEQRES 16 A 396 THR LEU ALA GLN LEU SER VAL GLU LYS GLY TRP LEU PRO
SEQRES 17 A 396 LEU PHE ASP PHE ALA TYR GLN GLY PHE ALA ARG GLY LEU
SEQRES 18 A 396 GLU GLU ASP ALA GLU GLY LEU ARG ALA PHE ALA ALA MET
SEQRES 19 A 396 HIS LYS GLU LEU ILE VAL ALA SER SER TYR SER LYS ASN
SEQRES 20 A 396 PHE GLY LEU TYR ASN GLU ARG VAL GLY ALA CYS THR LEU
SEQRES 21 A 396 VAL ALA ALA ASP SER GLU THR VAL ASP ARG ALA PHE SER
SEQRES 22 A 396 GLN MET LYS ALA ALA ILE ARG ALA ASN TYR SER ASN PRO
SEQRES 23 A 396 PRO ALA HIS GLY ALA SER VAL VAL ALA THR ILE LEU SER
SEQRES 24 A 396 ASN ASP ALA LEU ARG ALA ILE TRP GLU GLN GLU LEU THR
SEQRES 25 A 396 ASP MET ARG GLN ARG ILE GLN ARG MET ARG GLN LEU PHE
SEQRES 26 A 396 VAL ASN THR LEU GLN GLU LYS GLY ALA ASN ARG ASP PHE
SEQRES 27 A 396 SER PHE ILE ILE LYS GLN ASN GLY MET PHE SER PHE SER
SEQRES 28 A 396 GLY LEU THR LYS GLU GLN VAL LEU ARG LEU ARG GLU GLU
SEQRES 29 A 396 PHE GLY VAL TYR ALA VAL ALA SER GLY ARG VAL ASN VAL
SEQRES 30 A 396 ALA GLY MET THR PRO ASP ASN MET ALA PRO LEU CYS GLU
SEQRES 31 A 396 ALA ILE VAL ALA VAL LEU
HET PLP A 413 15
HET MAE A 414 8
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM MAE MALEIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 PLP C8 H10 N O6 P
FORMUL 3 MAE C4 H4 O4
FORMUL 4 HOH *76(H2 O)
HELIX 1 1 MET A 5 ILE A 9 5 5
HELIX 2 2 ILE A 17 ASP A 27 1 11
HELIX 3 3 LEU A 50 GLU A 62 1 13
HELIX 4 4 ILE A 76 GLY A 89 1 14
HELIX 5 5 SER A 92 ASP A 97 1 6
HELIX 6 6 GLY A 107 THR A 123 1 17
HELIX 7 7 PRO A 141 ALA A 150 1 10
HELIX 8 8 ASP A 169 ASN A 178 1 10
HELIX 9 9 THR A 201 GLY A 216 1 16
HELIX 10 10 GLU A 234 ASP A 236 5 3
HELIX 11 11 ALA A 237 HIS A 247 1 11
HELIX 12 12 LEU A 262 GLU A 265 5 4
HELIX 13 13 ASP A 276 ALA A 293 1 18
HELIX 14 14 PRO A 299 ASN A 312 1 14
HELIX 15 15 ASN A 312 LYS A 344 1 33
HELIX 16 16 SER A 351 GLN A 356 1 6
HELIX 17 17 THR A 366 GLY A 378 1 13
HELIX 18 18 ALA A 390 MET A 392 5 3
HELIX 19 19 ASN A 396 VAL A 408 1 12
SHEET 1 A 2 ILE A 33 ASN A 34 0
SHEET 2 A 2 VAL A 379 TYR A 380 1 O TYR A 380 N ILE A 33
SHEET 1 B 7 ALA A 100 PRO A 106 0
SHEET 2 B 7 VAL A 267 VAL A 273 -1 O LEU A 272 N ARG A 101
SHEET 3 B 7 LEU A 250 SER A 255 -1 N VAL A 252 O THR A 271
SHEET 4 B 7 LEU A 218 PHE A 223 1 N PHE A 223 O ALA A 253
SHEET 5 B 7 VAL A 185 HIS A 189 1 N PHE A 188 O ASP A 222
SHEET 6 B 7 ARG A 129 ASN A 137 1 N TRP A 134 O VAL A 185
SHEET 7 B 7 GLU A 154 ALA A 159 1 O ARG A 156 N VAL A 135
SHEET 1 C 2 TYR A 161 ASP A 162 0
SHEET 2 C 2 THR A 167 LEU A 168 -1 O THR A 167 N ASP A 162
SHEET 1 D 2 PHE A 360 PHE A 362 0
SHEET 2 D 2 ARG A 386 ASN A 388 -1 O VAL A 387 N SER A 361
LINK NZ LYS A 258 C4A PLP A 413 1555 1555 1.36
CISPEP 1 ASN A 137 PRO A 138 0 -0.40
CISPEP 2 ASN A 194 PRO A 195 0 -0.67
SITE 1 AC1 13 TYR A 70 GLY A 108 THR A 109 TRP A 140
SITE 2 AC1 13 ASN A 194 ASP A 222 TYR A 225 SER A 255
SITE 3 AC1 13 SER A 257 LYS A 258 ARG A 266 MAE A 414
SITE 4 AC1 13 HOH A 523
SITE 1 AC2 10 ILE A 17 GLY A 38 TRP A 140 ASN A 194
SITE 2 AC2 10 ARG A 292 ARG A 386 PLP A 413 HOH A 523
SITE 3 AC2 10 HOH A 527 HOH A 552
CRYST1 158.445 85.833 79.633 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006311 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011651 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
