HEADER TRANSFERASE 05-APR-04 1SZK
TITLE THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE
TITLE 2 MUTANT: E211S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-AMINOBUTYRATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GAMMA-AMINO-N-BUTYRATE TRANSAMINASE, GABA
COMPND 5 TRANSAMINASE, GLUTAMATE:SUCCINIC SEMIALDEHYDE TRANSAMINASE,
COMPND 6 GABA AMINOTRANSFERASE, GABA-AT;
COMPND 7 EC: 2.6.1.19;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET23A(+)
KEYWDS GABA-AT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.LIU,P.E.PETERSON,J.A.LANGSTON,X.JIN,A.J.FISHER,M.D.TONEY
REVDAT 2 24-FEB-09 1SZK 1 VERSN
REVDAT 1 01-MAR-05 1SZK 0
JRNL AUTH W.LIU,P.E.PETERSON,J.A.LANGSTON,X.JIN,X.ZHOU,
JRNL AUTH 2 A.J.FISHER,M.D.TONEY
JRNL TITL KINETIC AND CRYSTALLOGRAPHIC ANALYSIS OF ACTIVE
JRNL TITL 2 SITE MUTANTS OF ESCHERICHIA
JRNL TITL 3 COLIGAMMA-AMINOBUTYRATE AMINOTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 44 2982 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15723541
JRNL DOI 10.1021/BI048657A
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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 : 69873
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) : 0.187
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3515
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 : 12824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 191
REMARK 3 SOLVENT ATOMS : 673
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) : -4.37400
REMARK 3 B22 (A**2) : -4.37400
REMARK 3 B33 (A**2) : 8.74800
REMARK 3 B12 (A**2) : -5.05900
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) : 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) : 1.31
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) : 1.215 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.027 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.780 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.641 ; 2.500
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PMP_SO4_EGL.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
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: NULL
REMARK 4
REMARK 4 1SZK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-04.
REMARK 100 THE RCSB ID CODE IS RCSB022126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
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) : 1.54
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69873
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1SF2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULFATE, PLP, PH
REMARK 280 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 200.55333
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 100.27667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 100.27667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 200.55333
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -265.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
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 ASN A 32 -99.36 55.26
REMARK 500 ILE A 50 63.76 78.01
REMARK 500 LYS A 72 -63.13 -98.60
REMARK 500 THR A 76 -24.85 -147.37
REMARK 500 CYS A 77 99.37 83.14
REMARK 500 VAL A 108 -150.18 -119.35
REMARK 500 LYS A 151 112.88 -169.63
REMARK 500 PRO A 163 140.72 -37.88
REMARK 500 CYS A 173 76.57 -150.07
REMARK 500 ALA A 267 -147.53 -170.33
REMARK 500 LYS A 268 -107.31 45.30
REMARK 500 PRO A 275 98.94 -56.68
REMARK 500 ALA A 299 126.44 -29.13
REMARK 500 HIS A 365 43.44 -56.08
REMARK 500 ASN A 366 10.12 -164.45
REMARK 500 PRO B 24 46.59 -77.54
REMARK 500 ASN B 32 -110.71 55.20
REMARK 500 ILE B 50 62.20 78.50
REMARK 500 LEU B 53 52.36 -117.02
REMARK 500 THR B 76 -25.45 -148.42
REMARK 500 CYS B 77 101.43 82.45
REMARK 500 VAL B 108 -152.78 -126.44
REMARK 500 LYS B 151 106.83 -169.26
REMARK 500 TYR B 155 -18.14 -42.08
REMARK 500 SER B 156 24.72 -154.61
REMARK 500 CYS B 173 80.95 -164.60
REMARK 500 LEU B 175 -19.33 -48.59
REMARK 500 ALA B 267 -141.96 -171.11
REMARK 500 LYS B 268 -110.91 38.52
REMARK 500 PRO B 275 101.49 -58.26
REMARK 500 ARG B 282 127.10 -38.88
REMARK 500 ALA B 299 123.66 -30.29
REMARK 500 HIS B 365 34.91 -65.32
REMARK 500 ASN B 366 -16.68 -144.79
REMARK 500 CYS B 390 -175.89 -174.63
REMARK 500 PRO C 24 47.83 -74.61
REMARK 500 GLU C 31 112.79 -162.64
REMARK 500 ASN C 32 -98.13 60.30
REMARK 500 ILE C 50 69.29 70.19
REMARK 500 LEU C 58 59.94 36.58
REMARK 500 LYS C 72 -61.12 -92.61
REMARK 500 THR C 76 -20.31 -142.10
REMARK 500 CYS C 77 99.84 77.75
REMARK 500 VAL C 108 -152.62 -115.57
REMARK 500 LYS C 151 114.96 -170.80
REMARK 500 CYS C 173 85.21 -169.46
REMARK 500 ALA C 267 -145.34 -169.97
REMARK 500 LYS C 268 -110.60 46.08
REMARK 500 PRO C 275 95.14 -52.22
REMARK 500 ALA C 299 127.93 -39.31
REMARK 500 HIS C 365 8.78 -63.52
REMARK 500 CYS C 390 -173.29 -175.78
REMARK 500 THR C 404 31.42 -90.18
REMARK 500 ASP D 28 -50.43 -120.12
REMARK 500 GLU D 31 112.97 -163.98
REMARK 500 ASN D 32 -101.78 59.22
REMARK 500 ILE D 50 56.50 81.52
REMARK 500 LEU D 53 55.15 -117.35
REMARK 500 LYS D 72 -64.81 -91.49
REMARK 500 THR D 76 -23.25 -147.34
REMARK 500 CYS D 77 98.08 79.20
REMARK 500 VAL D 80 -61.72 -105.50
REMARK 500 VAL D 108 -137.45 -124.31
REMARK 500 THR D 109 -41.14 -134.50
REMARK 500 LYS D 151 119.18 -171.31
REMARK 500 TYR D 155 -31.22 -38.74
REMARK 500 ALA D 157 125.15 -38.01
REMARK 500 CYS D 173 82.35 -166.95
REMARK 500 ALA D 267 -146.54 -172.35
REMARK 500 LYS D 268 -110.38 43.09
REMARK 500 ARG D 282 119.28 -34.42
REMARK 500 ALA D 299 127.21 -26.27
REMARK 500 HIS D 342 84.33 -155.86
REMARK 500 ASP D 364 116.63 -31.19
REMARK 500 CYS D 390 -159.01 -171.49
REMARK 500 TYR D 394 38.09 38.24
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 A 701
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 703
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 704
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 705
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 706
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 707
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 708
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 709
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 710
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 711
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 712
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 713
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 714
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 715
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 801
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 802
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 803
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 805
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 806
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 807
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 808
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 809
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 810
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 811
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 812
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 813
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 750
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 751
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 752
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 753
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SF2 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE
REMARK 900 RELATED ID: 1SFF RELATED DB: PDB
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE
REMARK 900 COMPLEX WITH AMINOOXYACETATE
DBREF 1SZK A 1 426 UNP P22256 GABT_ECOLI 1 426
DBREF 1SZK B 1 426 UNP P22256 GABT_ECOLI 1 426
DBREF 1SZK C 1 426 UNP P22256 GABT_ECOLI 1 426
DBREF 1SZK D 1 426 UNP P22256 GABT_ECOLI 1 426
SEQADV 1SZK SER A 211 UNP P22256 GLU 211 ENGINEERED
SEQADV 1SZK SER B 211 UNP P22256 GLU 211 ENGINEERED
SEQADV 1SZK SER C 211 UNP P22256 GLU 211 ENGINEERED
SEQADV 1SZK SER D 211 UNP P22256 GLU 211 ENGINEERED
SEQRES 1 A 426 MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN
SEQRES 2 A 426 ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE
SEQRES 3 A 426 ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU
SEQRES 4 A 426 GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL
SEQRES 5 A 426 LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA
SEQRES 6 A 426 VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE
SEQRES 7 A 426 GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU
SEQRES 8 A 426 ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS
SEQRES 9 A 426 THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN
SEQRES 10 A 426 ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY
SEQRES 11 A 426 THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS
SEQRES 12 A 426 TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER
SEQRES 13 A 426 ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA
SEQRES 14 A 426 LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP
SEQRES 15 A 426 ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA
SEQRES 16 A 426 ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL
SEQRES 17 A 426 GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE
SEQRES 18 A 426 MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE
SEQRES 19 A 426 MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG
SEQRES 20 A 426 THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA
SEQRES 21 A 426 PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY
SEQRES 22 A 426 PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET
SEQRES 23 A 426 ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA
SEQRES 24 A 426 GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU
SEQRES 25 A 426 LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN
SEQRES 26 A 426 ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE
SEQRES 27 A 426 ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU
SEQRES 28 A 426 GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP
SEQRES 29 A 426 HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL
SEQRES 30 A 426 ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS
SEQRES 31 A 426 GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU
SEQRES 32 A 426 THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE
SEQRES 33 A 426 ILE SER GLN CYS PHE ASP GLU ALA LYS GLN
SEQRES 1 B 426 MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN
SEQRES 2 B 426 ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE
SEQRES 3 B 426 ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU
SEQRES 4 B 426 GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL
SEQRES 5 B 426 LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA
SEQRES 6 B 426 VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE
SEQRES 7 B 426 GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU
SEQRES 8 B 426 ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS
SEQRES 9 B 426 THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN
SEQRES 10 B 426 ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY
SEQRES 11 B 426 THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS
SEQRES 12 B 426 TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER
SEQRES 13 B 426 ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA
SEQRES 14 B 426 LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP
SEQRES 15 B 426 ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA
SEQRES 16 B 426 ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL
SEQRES 17 B 426 GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE
SEQRES 18 B 426 MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE
SEQRES 19 B 426 MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG
SEQRES 20 B 426 THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA
SEQRES 21 B 426 PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY
SEQRES 22 B 426 PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET
SEQRES 23 B 426 ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA
SEQRES 24 B 426 GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU
SEQRES 25 B 426 LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN
SEQRES 26 B 426 ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE
SEQRES 27 B 426 ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU
SEQRES 28 B 426 GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP
SEQRES 29 B 426 HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL
SEQRES 30 B 426 ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS
SEQRES 31 B 426 GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU
SEQRES 32 B 426 THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE
SEQRES 33 B 426 ILE SER GLN CYS PHE ASP GLU ALA LYS GLN
SEQRES 1 C 426 MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN
SEQRES 2 C 426 ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE
SEQRES 3 C 426 ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU
SEQRES 4 C 426 GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL
SEQRES 5 C 426 LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA
SEQRES 6 C 426 VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE
SEQRES 7 C 426 GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU
SEQRES 8 C 426 ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS
SEQRES 9 C 426 THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN
SEQRES 10 C 426 ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY
SEQRES 11 C 426 THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS
SEQRES 12 C 426 TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER
SEQRES 13 C 426 ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA
SEQRES 14 C 426 LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP
SEQRES 15 C 426 ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA
SEQRES 16 C 426 ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL
SEQRES 17 C 426 GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE
SEQRES 18 C 426 MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE
SEQRES 19 C 426 MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG
SEQRES 20 C 426 THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA
SEQRES 21 C 426 PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY
SEQRES 22 C 426 PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET
SEQRES 23 C 426 ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA
SEQRES 24 C 426 GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU
SEQRES 25 C 426 LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN
SEQRES 26 C 426 ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE
SEQRES 27 C 426 ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU
SEQRES 28 C 426 GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP
SEQRES 29 C 426 HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL
SEQRES 30 C 426 ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS
SEQRES 31 C 426 GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU
SEQRES 32 C 426 THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE
SEQRES 33 C 426 ILE SER GLN CYS PHE ASP GLU ALA LYS GLN
SEQRES 1 D 426 MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN
SEQRES 2 D 426 ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE
SEQRES 3 D 426 ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU
SEQRES 4 D 426 GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL
SEQRES 5 D 426 LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA
SEQRES 6 D 426 VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE
SEQRES 7 D 426 GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU
SEQRES 8 D 426 ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS
SEQRES 9 D 426 THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN
SEQRES 10 D 426 ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY
SEQRES 11 D 426 THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS
SEQRES 12 D 426 TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER
SEQRES 13 D 426 ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA
SEQRES 14 D 426 LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP
SEQRES 15 D 426 ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA
SEQRES 16 D 426 ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL
SEQRES 17 D 426 GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE
SEQRES 18 D 426 MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE
SEQRES 19 D 426 MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG
SEQRES 20 D 426 THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA
SEQRES 21 D 426 PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY
SEQRES 22 D 426 PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET
SEQRES 23 D 426 ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA
SEQRES 24 D 426 GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU
SEQRES 25 D 426 LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN
SEQRES 26 D 426 ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE
SEQRES 27 D 426 ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU
SEQRES 28 D 426 GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP
SEQRES 29 D 426 HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL
SEQRES 30 D 426 ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS
SEQRES 31 D 426 GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU
SEQRES 32 D 426 THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE
SEQRES 33 D 426 ILE SER GLN CYS PHE ASP GLU ALA LYS GLN
HET SO4 A 701 5
HET SO4 B 702 5
HET SO4 B 703 5
HET SO4 C 704 5
HET SO4 D 705 5
HET SO4 D 706 5
HET SO4 A 707 5
HET SO4 B 708 5
HET SO4 D 709 5
HET SO4 C 710 5
HET SO4 D 711 5
HET SO4 A 712 5
HET SO4 B 713 5
HET SO4 C 714 5
HET SO4 D 715 5
HET EDO B 801 4
HET EDO B 802 4
HET EDO C 803 4
HET EDO B 804 4
HET EDO D 805 4
HET EDO D 806 4
HET EDO D 807 4
HET EDO A 808 4
HET EDO C 809 4
HET EDO A 810 4
HET EDO C 811 4
HET EDO D 812 4
HET EDO A 813 4
HET PMP A 750 16
HET PMP B 751 16
HET PMP C 752 16
HET PMP D 753 16
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
HETSYN PMP PYRIDOXAMINE-5'-PHOSPHATE
FORMUL 5 SO4 15(O4 S 2-)
FORMUL 20 EDO 13(C2 H6 O2)
FORMUL 33 PMP 4(C8 H13 N2 O5 P)
FORMUL 37 HOH *673(H2 O)
HELIX 1 1 SER A 3 ILE A 15 1 13
HELIX 2 2 ALA A 47 VAL A 52 1 6
HELIX 3 3 HIS A 59 LYS A 71 1 13
HELIX 4 4 TYR A 83 VAL A 97 1 15
HELIX 5 5 THR A 110 LYS A 127 1 18
HELIX 6 6 THR A 142 THR A 149 1 8
HELIX 7 7 CYS A 173 GLY A 177 5 5
HELIX 8 8 SER A 179 ASP A 194 1 16
HELIX 9 9 ALA A 196 GLU A 198 5 3
HELIX 10 10 SER A 218 GLY A 233 1 16
HELIX 11 11 PHE A 252 MET A 257 5 6
HELIX 12 12 ALA A 267 GLY A 272 5 6
HELIX 13 13 ALA A 283 ASP A 287 1 5
HELIX 14 14 ASN A 301 GLU A 318 1 18
HELIX 15 15 ASN A 319 GLU A 340 1 22
HELIX 16 16 GLU A 361 ASP A 364 5 4
HELIX 17 17 ASP A 369 LYS A 383 1 15
HELIX 18 18 GLU A 406 GLN A 426 1 21
HELIX 19 19 SER B 3 ILE B 15 1 13
HELIX 20 20 ALA B 47 VAL B 52 1 6
HELIX 21 21 HIS B 59 LEU B 73 1 15
HELIX 22 22 TYR B 83 VAL B 97 1 15
HELIX 23 23 THR B 110 LYS B 127 1 18
HELIX 24 24 THR B 142 THR B 149 1 8
HELIX 25 25 CYS B 173 GLY B 177 5 5
HELIX 26 26 SER B 179 ASP B 194 1 16
HELIX 27 27 ALA B 196 GLU B 198 5 3
HELIX 28 28 SER B 218 GLY B 233 1 16
HELIX 29 29 PHE B 252 MET B 257 5 6
HELIX 30 30 ALA B 267 ALA B 271 5 5
HELIX 31 31 ALA B 283 ASP B 287 1 5
HELIX 32 32 ASN B 301 GLU B 318 1 18
HELIX 33 33 ASN B 319 ALA B 339 1 21
HELIX 34 34 ASP B 369 LYS B 383 1 15
HELIX 35 35 GLU B 406 ALA B 424 1 19
HELIX 36 36 SER C 3 ILE C 15 1 13
HELIX 37 37 ALA C 47 VAL C 52 1 6
HELIX 38 38 HIS C 59 LYS C 71 1 13
HELIX 39 39 GLU C 84 VAL C 97 1 14
HELIX 40 40 THR C 110 LYS C 127 1 18
HELIX 41 41 THR C 142 THR C 149 1 8
HELIX 42 42 CYS C 173 GLY C 177 5 5
HELIX 43 43 SER C 179 ASP C 194 1 16
HELIX 44 44 ALA C 196 GLU C 198 5 3
HELIX 45 45 SER C 218 GLY C 233 1 16
HELIX 46 46 PHE C 252 GLY C 258 5 7
HELIX 47 47 ALA C 267 GLY C 272 5 6
HELIX 48 48 ALA C 283 ASP C 287 1 5
HELIX 49 49 ASN C 301 GLU C 318 1 18
HELIX 50 50 ASN C 319 ALA C 339 1 21
HELIX 51 51 ASP C 369 LYS C 383 1 15
HELIX 52 52 GLU C 406 ALA C 424 1 19
HELIX 53 53 SER D 3 ILE D 15 1 13
HELIX 54 54 ALA D 47 VAL D 52 1 6
HELIX 55 55 HIS D 59 LEU D 73 1 15
HELIX 56 56 TYR D 83 VAL D 97 1 15
HELIX 57 57 THR D 110 LYS D 127 1 18
HELIX 58 58 THR D 142 THR D 149 1 8
HELIX 59 59 CYS D 173 GLY D 177 5 5
HELIX 60 60 SER D 179 ASP D 194 1 16
HELIX 61 61 ALA D 196 GLU D 198 5 3
HELIX 62 62 SER D 218 GLY D 233 1 16
HELIX 63 63 PHE D 252 GLY D 258 5 7
HELIX 64 64 ALA D 267 GLY D 272 5 6
HELIX 65 65 ALA D 283 ASP D 287 1 5
HELIX 66 66 ASN D 301 GLU D 318 1 18
HELIX 67 67 ASN D 319 ALA D 339 1 21
HELIX 68 68 ASP D 369 ASP D 382 1 14
HELIX 69 69 GLU D 406 GLN D 426 1 21
SHEET 1 A 5 LEU A 385 ILE A 386 0
SHEET 2 A 5 GLU A 42 ASP A 45 1 N LEU A 44 O ILE A 386
SHEET 3 A 5 ARG A 34 ASP A 37 -1 N VAL A 35 O TYR A 43
SHEET 4 A 5 HIS A 23 GLU A 31 -1 N ASP A 28 O TRP A 36
SHEET 5 A 5 LEU B 81 ALA B 82 1 O ALA B 82 N ALA A 27
SHEET 1 B 5 LEU A 81 ALA A 82 0
SHEET 2 B 5 HIS B 23 GLU B 31 1 O ALA B 27 N ALA A 82
SHEET 3 B 5 ARG B 34 ASP B 37 -1 O TRP B 36 N ASP B 28
SHEET 4 B 5 GLU B 42 ASP B 45 -1 O TYR B 43 N VAL B 35
SHEET 5 B 5 LEU B 385 ILE B 386 1 O ILE B 386 N LEU B 44
SHEET 1 C 7 LYS A 103 VAL A 108 0
SHEET 2 C 7 ALA A 277 ARG A 282 -1 O VAL A 279 N LEU A 106
SHEET 3 C 7 LEU A 263 PHE A 266 -1 N PHE A 266 O GLY A 278
SHEET 4 C 7 MET A 235 ASP A 239 1 N ALA A 238 O LEU A 263
SHEET 5 C 7 ILE A 200 ILE A 205 1 N ALA A 201 O MET A 235
SHEET 6 C 7 GLY A 130 PHE A 134 1 N GLY A 130 O ALA A 201
SHEET 7 C 7 VAL A 166 ALA A 169 1 O TYR A 167 N THR A 131
SHEET 1 D 4 ILE A 345 ARG A 349 0
SHEET 2 D 4 ILE A 355 LEU A 359 -1 O ALA A 356 N ARG A 349
SHEET 3 D 4 VAL A 396 ILE A 399 -1 O ILE A 399 N ILE A 355
SHEET 4 D 4 LEU A 388 CYS A 390 -1 N CYS A 390 O VAL A 396
SHEET 1 E 7 LYS B 103 VAL B 108 0
SHEET 2 E 7 ALA B 277 ARG B 282 -1 O VAL B 279 N LEU B 106
SHEET 3 E 7 LEU B 263 PHE B 266 -1 N THR B 264 O THR B 280
SHEET 4 E 7 MET B 235 ASP B 239 1 N ALA B 238 O LEU B 263
SHEET 5 E 7 ILE B 200 ILE B 205 1 N ILE B 203 O ILE B 237
SHEET 6 E 7 GLY B 130 PHE B 134 1 N ILE B 132 O VAL B 204
SHEET 7 E 7 VAL B 166 ALA B 169 1 O ALA B 169 N ALA B 133
SHEET 1 F 4 ILE B 345 LEU B 351 0
SHEET 2 F 4 MET B 354 LEU B 359 -1 O MET B 354 N LEU B 351
SHEET 3 F 4 VAL B 396 ILE B 399 -1 O ILE B 399 N ILE B 355
SHEET 4 F 4 LEU B 388 CYS B 390 -1 N CYS B 390 O VAL B 396
SHEET 1 G 4 ALA C 27 GLU C 31 0
SHEET 2 G 4 ARG C 34 ASP C 37 -1 O TRP C 36 N ASP C 28
SHEET 3 G 4 GLU C 42 ASP C 45 -1 O TYR C 43 N VAL C 35
SHEET 4 G 4 LEU C 385 ILE C 386 1 O ILE C 386 N LEU C 44
SHEET 1 H 5 LEU C 81 TYR C 83 0
SHEET 2 H 5 HIS D 23 GLU D 31 1 O ALA D 27 N ALA C 82
SHEET 3 H 5 ARG D 34 ASP D 37 -1 O TRP D 36 N ASP D 28
SHEET 4 H 5 GLU D 42 ASP D 45 -1 O TYR D 43 N VAL D 35
SHEET 5 H 5 LEU D 385 ILE D 386 1 O ILE D 386 N LEU D 44
SHEET 1 I 7 LYS C 103 VAL C 108 0
SHEET 2 I 7 ALA C 277 ARG C 282 -1 O VAL C 279 N LEU C 106
SHEET 3 I 7 LEU C 263 PHE C 266 -1 N PHE C 266 O GLY C 278
SHEET 4 I 7 MET C 235 ASP C 239 1 N ALA C 238 O LEU C 263
SHEET 5 I 7 ILE C 200 ILE C 205 1 N ILE C 203 O ILE C 237
SHEET 6 I 7 GLY C 130 PHE C 134 1 N ILE C 132 O VAL C 204
SHEET 7 I 7 VAL C 166 ALA C 169 1 O ALA C 169 N ALA C 133
SHEET 1 J 3 ILE C 345 LEU C 351 0
SHEET 2 J 3 MET C 354 GLU C 361 -1 O ALA C 356 N ARG C 349
SHEET 3 J 3 ASP C 364 PRO C 368 -1 O LYS C 367 N GLU C 361
SHEET 1 K 4 ILE C 345 LEU C 351 0
SHEET 2 K 4 MET C 354 GLU C 361 -1 O ALA C 356 N ARG C 349
SHEET 3 K 4 VAL C 396 ILE C 399 -1 O LEU C 397 N ILE C 357
SHEET 4 K 4 LEU C 388 CYS C 390 -1 N LEU C 388 O ARG C 398
SHEET 1 L 7 LYS D 103 VAL D 108 0
SHEET 2 L 7 ALA D 277 ARG D 282 -1 O VAL D 279 N LEU D 106
SHEET 3 L 7 LEU D 263 PHE D 266 -1 N PHE D 266 O GLY D 278
SHEET 4 L 7 MET D 235 ASP D 239 1 N ALA D 238 O LEU D 263
SHEET 5 L 7 ILE D 200 ILE D 205 1 N ILE D 203 O ILE D 237
SHEET 6 L 7 GLY D 130 PHE D 134 1 N ILE D 132 O VAL D 204
SHEET 7 L 7 VAL D 166 ALA D 169 1 O ALA D 169 N ALA D 133
SHEET 1 M 4 ARG D 349 LEU D 351 0
SHEET 2 M 4 MET D 354 GLU D 358 -1 O MET D 354 N LEU D 351
SHEET 3 M 4 VAL D 396 ILE D 399 -1 O ILE D 399 N ILE D 355
SHEET 4 M 4 LEU D 388 CYS D 390 -1 N LEU D 388 O ARG D 398
CISPEP 1 ASN A 153 PRO A 154 0 0.68
CISPEP 2 ASN B 153 PRO B 154 0 0.17
CISPEP 3 ASN C 153 PRO C 154 0 0.08
CISPEP 4 ASN D 153 PRO D 154 0 -0.04
SITE 1 AC1 3 ILE A 184 ARG A 224 HOH A 950
SITE 1 AC2 3 LYS B 5 ARG B 381 HOH B 926
SITE 1 AC3 3 HIS B 188 ARG B 224 HOH B 925
SITE 1 AC4 2 HIS C 188 ARG C 224
SITE 1 AC5 1 ARG D 224
SITE 1 AC6 3 LYS D 5 ARG D 381 HOH D 881
SITE 1 AC7 4 ASN A 153 TYR A 394 LYS C 192 HOH C 852
SITE 1 AC8 3 ASN B 153 TYR B 394 LYS D 192
SITE 1 AC9 3 LYS B 192 ASN D 153 TYR D 394
SITE 1 BC1 3 LYS A 192 ASN C 153 TYR C 394
SITE 1 BC2 3 GLN A 419 ARG D 29 HOH D 978
SITE 1 BC3 6 ILE A 50 TYR A 138 SER A 211 ARG A 398
SITE 2 BC3 6 PMP A 750 HOH A 991
SITE 1 BC4 7 ILE B 50 TYR B 138 SER B 211 GLN B 242
SITE 2 BC4 7 LYS B 268 ARG B 398 PMP B 751
SITE 1 BC5 7 ILE C 50 TYR C 138 SER C 211 GLN C 242
SITE 2 BC5 7 ARG C 398 PMP C 752 HOH C 952
SITE 1 BC6 7 ILE D 50 TYR D 138 SER D 211 GLN D 242
SITE 2 BC6 7 ARG D 398 PMP D 753 HOH D 987
SITE 1 BC7 8 THR A 76 VAL A 80 LEU A 81 ASP B 45
SITE 2 BC7 8 ALA B 47 GLY B 48 GLY B 49 HIS B 57
SITE 1 BC8 2 HIS B 23 ARG B 381
SITE 1 BC9 6 GLY A 164 HIS A 165 GLY C 164 HIS C 165
SITE 2 BC9 6 VAL C 166 TYR C 167
SITE 1 CC1 6 GLY B 164 HIS B 165 VAL B 166 HIS D 165
SITE 2 CC1 6 VAL D 166 HOH D 968
SITE 1 CC2 8 THR C 76 VAL C 80 LEU C 81 ASP D 45
SITE 2 CC2 8 ALA D 47 GLY D 48 GLY D 49 HIS D 57
SITE 1 CC3 4 PRO C 275 ASN C 301 PRO D 275 ASN D 301
SITE 1 CC4 4 HIS D 23 PRO D 24 ARG D 381 HOH D 959
SITE 1 CC5 8 ASP A 45 ALA A 47 GLY A 48 GLY A 49
SITE 2 CC5 8 HIS A 57 THR B 76 VAL B 80 LEU B 81
SITE 1 CC6 7 ASP C 45 ALA C 47 GLY C 48 GLY C 49
SITE 2 CC6 7 HIS C 57 THR D 76 LEU D 81
SITE 1 CC7 5 GLN A 69 LYS A 72 PRO A 85 ASP B 28
SITE 2 CC7 5 HOH B 936
SITE 1 CC8 5 GLN C 69 LYS C 72 LEU C 73 PRO C 85
SITE 2 CC8 5 ASP D 28
SITE 1 CC9 6 TYR B 167 VAL D 166 TYR D 167 HOH D 923
SITE 2 CC9 6 HOH D 956 HOH D 968
SITE 1 DC1 5 GLN A 9 GLN D 95 LYS D 96 PRO D 98
SITE 2 DC1 5 GLU D 255
SITE 1 DC2 18 GLY A 111 SER A 112 TYR A 138 HIS A 139
SITE 2 DC2 18 GLU A 206 ASP A 239 VAL A 241 GLN A 242
SITE 3 DC2 18 LYS A 268 SO4 A 712 HOH A 815 HOH A 823
SITE 4 DC2 18 HOH A 890 HOH A 912 HOH A 987 HOH A 989
SITE 5 DC2 18 GLY B 296 THR B 297
SITE 1 DC3 16 THR A 297 HOH A 859 THR B 110 GLY B 111
SITE 2 DC3 16 SER B 112 TYR B 138 HIS B 139 GLU B 206
SITE 3 DC3 16 ASP B 239 VAL B 241 GLN B 242 LYS B 268
SITE 4 DC3 16 SO4 B 713 HOH B 805 HOH B 811 HOH B 818
SITE 1 DC4 17 THR C 110 GLY C 111 SER C 112 TYR C 138
SITE 2 DC4 17 HIS C 139 GLU C 206 ASP C 239 VAL C 241
SITE 3 DC4 17 GLN C 242 LYS C 268 SO4 C 714 HOH C 825
SITE 4 DC4 17 HOH C 828 HOH C 867 THR D 297 HOH D 838
SITE 5 DC4 17 HOH D 984
SITE 1 DC5 16 THR C 297 GLY D 111 SER D 112 TYR D 138
SITE 2 DC5 16 HIS D 139 GLU D 206 ASP D 239 VAL D 241
SITE 3 DC5 16 GLN D 242 LYS D 268 SO4 D 715 HOH D 813
SITE 4 DC5 16 HOH D 823 HOH D 826 HOH D 836 HOH D 845
CRYST1 108.260 108.260 300.830 90.00 90.00 120.00 P 32 2 1 24
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 0.009237 0.005333 0.000000 0.00000
SCALE2 0.000000 0.010666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003324 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
