HEADER OXIDOREDUCTASE 19-DEC-18 6QAP
TITLE STRUCTURE OF THE HUMAN ALDEHYDE DEHYDROGENASE 9A1 IN C2 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TMABADH,ALDEHYDE DEHYDROGENASE E3 ISOZYME,ALDEHYDE
COMPND 5 DEHYDROGENASE FAMILY 9 MEMBER A1,GAMMA-AMINOBUTYRALDEHYDE
COMPND 6 DEHYDROGENASE,R-AMINOBUTYRALDEHYDE DEHYDROGENASE;
COMPND 7 EC: 1.2.1.47,1.2.1.3,1.2.1.19;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDH9A1, ALDH4, ALDH7, ALDH9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MORERA,A.VIGOUROUX
REVDAT 3 24-JAN-24 6QAP 1 LINK
REVDAT 2 08-MAY-19 6QAP 1 JRNL
REVDAT 1 10-APR-19 6QAP 0
JRNL AUTH R.KONCITIKOVA,A.VIGOUROUX,M.KOPECNA,M.SEBELA,S.MORERA,
JRNL AUTH 2 D.KOPECNY
JRNL TITL KINETIC AND STRUCTURAL ANALYSIS OF HUMAN ALDH9A1.
JRNL REF BIOSCI.REP. V. 39 2019
JRNL REFN ISSN 0144-8463
JRNL PMID 30914451
JRNL DOI 10.1042/BSR20190558
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 96847
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 + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4843
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.69
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1937
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2953
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1840
REMARK 3 BIN R VALUE (WORKING SET) : 0.2926
REMARK 3 BIN FREE R VALUE : 0.3473
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
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 : 14408
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 358
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.21400
REMARK 3 B22 (A**2) : -3.36470
REMARK 3 B33 (A**2) : 8.57860
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.33950
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.350
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.305
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.220
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.318
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.226
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 14783 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 19958 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5123 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 2528 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 14783 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 5 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1914 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 17389 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.09
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.32
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -61.1061 15.1601 14.1702
REMARK 3 T TENSOR
REMARK 3 T11: -0.3162 T22: -0.2679
REMARK 3 T33: -0.2210 T12: -0.0059
REMARK 3 T13: -0.0407 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.9854 L22: 1.0311
REMARK 3 L33: 0.4935 L12: 0.6748
REMARK 3 L13: -0.1685 L23: -0.1133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0991 S12: 0.0342 S13: 0.5059
REMARK 3 S21: -0.0605 S22: 0.1436 S23: 0.2829
REMARK 3 S31: 0.0197 S32: -0.1731 S33: -0.0445
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6434 23.0106 14.8793
REMARK 3 T TENSOR
REMARK 3 T11: -0.3298 T22: -0.3033
REMARK 3 T33: -0.1865 T12: -0.0006
REMARK 3 T13: 0.0223 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 2.4870 L22: 1.2566
REMARK 3 L33: 0.5490 L12: 1.1063
REMARK 3 L13: 0.3346 L23: 0.3424
REMARK 3 S TENSOR
REMARK 3 S11: -0.0586 S12: 0.0269 S13: -0.7291
REMARK 3 S21: -0.0226 S22: 0.1763 S23: -0.4466
REMARK 3 S31: -0.0315 S32: 0.1901 S33: -0.1177
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -38.9768 39.1239 -23.9195
REMARK 3 T TENSOR
REMARK 3 T11: -0.2062 T22: -0.3183
REMARK 3 T33: -0.2430 T12: -0.0155
REMARK 3 T13: 0.0220 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.5670 L22: 2.5328
REMARK 3 L33: 0.7401 L12: 0.4628
REMARK 3 L13: -0.0802 L23: -0.7497
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: 0.0065 S13: 0.1451
REMARK 3 S21: 0.1380 S22: 0.0185 S23: 0.5529
REMARK 3 S31: -0.1092 S32: -0.0634 S33: -0.1308
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3680 -0.9216 -23.8999
REMARK 3 T TENSOR
REMARK 3 T11: -0.2035 T22: -0.3129
REMARK 3 T33: -0.2457 T12: -0.0248
REMARK 3 T13: -0.0204 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.6158 L22: 2.3393
REMARK 3 L33: 0.5147 L12: 0.4500
REMARK 3 L13: 0.0520 L23: 0.5652
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: -0.0005 S13: -0.1189
REMARK 3 S21: 0.1159 S22: -0.0077 S23: -0.5000
REMARK 3 S31: 0.0946 S32: 0.0123 S33: -0.0982
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6QAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1200013572.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.15200
REMARK 200 R SYM (I) : 0.14100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
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: PHASER
REMARK 200 STARTING MODEL: 6QAK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4K, 0.1 M SODIUM CITRATE PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 82.14500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.01500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 82.14500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 80.01500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 22900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 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 -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 GLY A 232
REMARK 465 SER A 233
REMARK 465 VAL A 234
REMARK 465 PRO A 235
REMARK 465 THR A 236
REMARK 465 GLY A 237
REMARK 465 MET A 238
REMARK 465 LYS A 239
REMARK 465 ILE A 240
REMARK 465 MET A 241
REMARK 465 GLU A 242
REMARK 465 MET A 243
REMARK 465 SER A 244
REMARK 465 ALA A 245
REMARK 465 LYS A 246
REMARK 465 GLY A 247
REMARK 465 ILE A 248
REMARK 465 LYS A 249
REMARK 465 PRO A 250
REMARK 465 VAL A 251
REMARK 465 THR A 252
REMARK 465 LEU A 253
REMARK 465 GLU A 254
REMARK 465 LEU A 255
REMARK 465 GLY A 256
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 SER B -3
REMARK 465 GLN B -2
REMARK 465 ASP B -1
REMARK 465 GLY B 232
REMARK 465 SER B 233
REMARK 465 VAL B 234
REMARK 465 PRO B 235
REMARK 465 THR B 236
REMARK 465 GLY B 237
REMARK 465 MET B 238
REMARK 465 LYS B 239
REMARK 465 ILE B 240
REMARK 465 MET B 241
REMARK 465 GLU B 242
REMARK 465 MET B 243
REMARK 465 SER B 244
REMARK 465 ALA B 245
REMARK 465 LYS B 246
REMARK 465 GLY B 247
REMARK 465 ILE B 248
REMARK 465 LYS B 249
REMARK 465 PRO B 250
REMARK 465 VAL B 251
REMARK 465 THR B 252
REMARK 465 LEU B 253
REMARK 465 GLU B 254
REMARK 465 LEU B 255
REMARK 465 GLY B 256
REMARK 465 MET C -13
REMARK 465 GLY C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 SER C -3
REMARK 465 GLN C -2
REMARK 465 ASP C -1
REMARK 465 GLY C 232
REMARK 465 SER C 233
REMARK 465 VAL C 234
REMARK 465 PRO C 235
REMARK 465 THR C 236
REMARK 465 GLY C 237
REMARK 465 MET C 238
REMARK 465 LYS C 239
REMARK 465 ILE C 240
REMARK 465 MET C 241
REMARK 465 GLU C 242
REMARK 465 MET C 243
REMARK 465 SER C 244
REMARK 465 ALA C 245
REMARK 465 LYS C 246
REMARK 465 GLY C 247
REMARK 465 ILE C 248
REMARK 465 LYS C 249
REMARK 465 PRO C 250
REMARK 465 VAL C 251
REMARK 465 THR C 252
REMARK 465 LEU C 253
REMARK 465 GLU C 254
REMARK 465 LEU C 255
REMARK 465 MET D -13
REMARK 465 GLY D -12
REMARK 465 SER D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 SER D -3
REMARK 465 GLN D -2
REMARK 465 ASP D -1
REMARK 465 GLY D 232
REMARK 465 SER D 233
REMARK 465 VAL D 234
REMARK 465 PRO D 235
REMARK 465 THR D 236
REMARK 465 GLY D 237
REMARK 465 MET D 238
REMARK 465 LYS D 239
REMARK 465 ILE D 240
REMARK 465 MET D 241
REMARK 465 GLU D 242
REMARK 465 MET D 243
REMARK 465 SER D 244
REMARK 465 ALA D 245
REMARK 465 LYS D 246
REMARK 465 GLY D 247
REMARK 465 ILE D 248
REMARK 465 LYS D 249
REMARK 465 PRO D 250
REMARK 465 VAL D 251
REMARK 465 THR D 252
REMARK 465 LEU D 253
REMARK 465 GLU D 254
REMARK 465 LEU D 255
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 SER A 259 112.64 -37.53
REMARK 500 ASN A 290 132.76 -27.32
REMARK 500 LYS A 461 -72.80 -58.50
REMARK 500 LYS A 462 49.04 -93.03
REMARK 500 SER B 259 113.52 -38.66
REMARK 500 ASN B 290 133.81 -36.71
REMARK 500 ASP B 414 12.66 -160.80
REMARK 500 LYS B 461 -73.99 -57.84
REMARK 500 LYS B 462 50.57 -93.23
REMARK 500 SER C 259 113.53 -34.86
REMARK 500 GLN C 286 56.22 -93.37
REMARK 500 ASN C 290 127.25 -26.77
REMARK 500 PHE C 393 40.66 71.48
REMARK 500 ASP C 414 11.76 -145.63
REMARK 500 LYS C 461 -73.52 -58.67
REMARK 500 LYS C 462 51.69 -92.77
REMARK 500 SER D 259 112.57 -36.52
REMARK 500 GLN D 286 58.09 -95.99
REMARK 500 LYS D 461 -73.62 -59.16
REMARK 500 LYS D 462 49.68 -92.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 691 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A 692 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 693 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A 694 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH B 682 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH B 683 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH B 684 DISTANCE = 8.50 ANGSTROMS
REMARK 525 HOH B 685 DISTANCE = 9.01 ANGSTROMS
REMARK 525 HOH C 695 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH C 696 DISTANCE = 7.99 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 207 OD1
REMARK 620 2 EDO D 507 O2 105.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 511
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6QAK RELATED DB: PDB
DBREF 6QAP A 1 494 UNP P49189 AL9A1_HUMAN 1 494
DBREF 6QAP B 1 494 UNP P49189 AL9A1_HUMAN 1 494
DBREF 6QAP C 1 494 UNP P49189 AL9A1_HUMAN 1 494
DBREF 6QAP D 1 494 UNP P49189 AL9A1_HUMAN 1 494
SEQADV 6QAP MET A -13 UNP P49189 INITIATING METHIONINE
SEQADV 6QAP GLY A -12 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER A -11 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER A -10 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS A -9 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS A -8 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS A -7 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS A -6 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS A -5 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS A -4 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER A -3 UNP P49189 EXPRESSION TAG
SEQADV 6QAP GLN A -2 UNP P49189 EXPRESSION TAG
SEQADV 6QAP ASP A -1 UNP P49189 EXPRESSION TAG
SEQADV 6QAP PRO A 0 UNP P49189 EXPRESSION TAG
SEQADV 6QAP MET B -13 UNP P49189 INITIATING METHIONINE
SEQADV 6QAP GLY B -12 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER B -11 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER B -10 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS B -9 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS B -8 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS B -7 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS B -6 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS B -5 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS B -4 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER B -3 UNP P49189 EXPRESSION TAG
SEQADV 6QAP GLN B -2 UNP P49189 EXPRESSION TAG
SEQADV 6QAP ASP B -1 UNP P49189 EXPRESSION TAG
SEQADV 6QAP PRO B 0 UNP P49189 EXPRESSION TAG
SEQADV 6QAP MET C -13 UNP P49189 INITIATING METHIONINE
SEQADV 6QAP GLY C -12 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER C -11 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER C -10 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS C -9 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS C -8 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS C -7 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS C -6 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS C -5 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS C -4 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER C -3 UNP P49189 EXPRESSION TAG
SEQADV 6QAP GLN C -2 UNP P49189 EXPRESSION TAG
SEQADV 6QAP ASP C -1 UNP P49189 EXPRESSION TAG
SEQADV 6QAP PRO C 0 UNP P49189 EXPRESSION TAG
SEQADV 6QAP MET D -13 UNP P49189 INITIATING METHIONINE
SEQADV 6QAP GLY D -12 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER D -11 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER D -10 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS D -9 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS D -8 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS D -7 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS D -6 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS D -5 UNP P49189 EXPRESSION TAG
SEQADV 6QAP HIS D -4 UNP P49189 EXPRESSION TAG
SEQADV 6QAP SER D -3 UNP P49189 EXPRESSION TAG
SEQADV 6QAP GLN D -2 UNP P49189 EXPRESSION TAG
SEQADV 6QAP ASP D -1 UNP P49189 EXPRESSION TAG
SEQADV 6QAP PRO D 0 UNP P49189 EXPRESSION TAG
SEQRES 1 A 508 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 508 PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU
SEQRES 3 A 508 ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA
SEQRES 4 A 508 SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG
SEQRES 5 A 508 VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL
SEQRES 6 A 508 ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE
SEQRES 7 A 508 TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU
SEQRES 8 A 508 LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU
SEQRES 9 A 508 ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE
SEQRES 10 A 508 PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS
SEQRES 11 A 508 LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY
SEQRES 12 A 508 GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR
SEQRES 13 A 508 ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA
SEQRES 14 A 508 TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA
SEQRES 15 A 508 PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO
SEQRES 16 A 508 SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU
SEQRES 17 A 508 ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN
SEQRES 18 A 508 VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS
SEQRES 19 A 508 GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER
SEQRES 20 A 508 VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS
SEQRES 21 A 508 GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 A 508 PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA
SEQRES 23 A 508 VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY
SEQRES 24 A 508 GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS
SEQRES 25 A 508 GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN
SEQRES 26 A 508 THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP
SEQRES 27 A 508 THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU
SEQRES 28 A 508 ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY
SEQRES 29 A 508 ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU
SEQRES 30 A 508 ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS
SEQRES 31 A 508 VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS
SEQRES 32 A 508 GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE
SEQRES 33 A 508 ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR
SEQRES 34 A 508 THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE
SEQRES 35 A 508 GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY
SEQRES 36 A 508 THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU
SEQRES 37 A 508 LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG
SEQRES 38 A 508 GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU
SEQRES 39 A 508 LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA
SEQRES 40 A 508 PHE
SEQRES 1 B 508 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 508 PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU
SEQRES 3 B 508 ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA
SEQRES 4 B 508 SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG
SEQRES 5 B 508 VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL
SEQRES 6 B 508 ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE
SEQRES 7 B 508 TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU
SEQRES 8 B 508 LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU
SEQRES 9 B 508 ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE
SEQRES 10 B 508 PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS
SEQRES 11 B 508 LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY
SEQRES 12 B 508 GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR
SEQRES 13 B 508 ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA
SEQRES 14 B 508 TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA
SEQRES 15 B 508 PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO
SEQRES 16 B 508 SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU
SEQRES 17 B 508 ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN
SEQRES 18 B 508 VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS
SEQRES 19 B 508 GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER
SEQRES 20 B 508 VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS
SEQRES 21 B 508 GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 B 508 PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA
SEQRES 23 B 508 VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY
SEQRES 24 B 508 GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS
SEQRES 25 B 508 GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN
SEQRES 26 B 508 THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP
SEQRES 27 B 508 THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU
SEQRES 28 B 508 ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY
SEQRES 29 B 508 ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU
SEQRES 30 B 508 ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS
SEQRES 31 B 508 VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS
SEQRES 32 B 508 GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE
SEQRES 33 B 508 ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR
SEQRES 34 B 508 THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE
SEQRES 35 B 508 GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY
SEQRES 36 B 508 THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU
SEQRES 37 B 508 LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG
SEQRES 38 B 508 GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU
SEQRES 39 B 508 LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA
SEQRES 40 B 508 PHE
SEQRES 1 C 508 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 C 508 PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU
SEQRES 3 C 508 ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA
SEQRES 4 C 508 SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG
SEQRES 5 C 508 VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL
SEQRES 6 C 508 ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE
SEQRES 7 C 508 TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU
SEQRES 8 C 508 LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU
SEQRES 9 C 508 ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE
SEQRES 10 C 508 PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS
SEQRES 11 C 508 LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY
SEQRES 12 C 508 GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR
SEQRES 13 C 508 ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA
SEQRES 14 C 508 TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA
SEQRES 15 C 508 PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO
SEQRES 16 C 508 SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU
SEQRES 17 C 508 ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN
SEQRES 18 C 508 VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS
SEQRES 19 C 508 GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER
SEQRES 20 C 508 VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS
SEQRES 21 C 508 GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 C 508 PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA
SEQRES 23 C 508 VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY
SEQRES 24 C 508 GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS
SEQRES 25 C 508 GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN
SEQRES 26 C 508 THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP
SEQRES 27 C 508 THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU
SEQRES 28 C 508 ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY
SEQRES 29 C 508 ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU
SEQRES 30 C 508 ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS
SEQRES 31 C 508 VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS
SEQRES 32 C 508 GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE
SEQRES 33 C 508 ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR
SEQRES 34 C 508 THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE
SEQRES 35 C 508 GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY
SEQRES 36 C 508 THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU
SEQRES 37 C 508 LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG
SEQRES 38 C 508 GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU
SEQRES 39 C 508 LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA
SEQRES 40 C 508 PHE
SEQRES 1 D 508 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 D 508 PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU
SEQRES 3 D 508 ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA
SEQRES 4 D 508 SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG
SEQRES 5 D 508 VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL
SEQRES 6 D 508 ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE
SEQRES 7 D 508 TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU
SEQRES 8 D 508 LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU
SEQRES 9 D 508 ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE
SEQRES 10 D 508 PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS
SEQRES 11 D 508 LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY
SEQRES 12 D 508 GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR
SEQRES 13 D 508 ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA
SEQRES 14 D 508 TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA
SEQRES 15 D 508 PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO
SEQRES 16 D 508 SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU
SEQRES 17 D 508 ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN
SEQRES 18 D 508 VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS
SEQRES 19 D 508 GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER
SEQRES 20 D 508 VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS
SEQRES 21 D 508 GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 D 508 PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA
SEQRES 23 D 508 VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY
SEQRES 24 D 508 GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS
SEQRES 25 D 508 GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN
SEQRES 26 D 508 THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP
SEQRES 27 D 508 THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU
SEQRES 28 D 508 ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY
SEQRES 29 D 508 ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU
SEQRES 30 D 508 ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS
SEQRES 31 D 508 VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS
SEQRES 32 D 508 GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE
SEQRES 33 D 508 ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR
SEQRES 34 D 508 THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE
SEQRES 35 D 508 GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY
SEQRES 36 D 508 THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU
SEQRES 37 D 508 LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG
SEQRES 38 D 508 GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU
SEQRES 39 D 508 LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA
SEQRES 40 D 508 PHE
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET EDO B 501 4
HET EDO B 502 4
HET EDO B 503 4
HET PEG B 504 7
HET NA C 501 1
HET NA C 502 1
HET NA C 503 1
HET EDO C 504 4
HET PEG C 505 7
HET PEG C 506 7
HET PEG C 507 7
HET NA D 501 1
HET NA D 502 1
HET NA D 503 1
HET NA D 504 1
HET NA D 505 1
HET EDO D 506 4
HET EDO D 507 4
HET EDO D 508 4
HET EDO D 509 4
HET EDO D 510 4
HET EDO D 511 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 15(C2 H6 O2)
FORMUL 13 PEG 4(C4 H10 O3)
FORMUL 14 NA 8(NA 1+)
FORMUL 32 HOH *358(H2 O)
HELIX 1 AA1 GLY A 47 SER A 66 1 20
HELIX 2 AA2 SER A 69 ARG A 87 1 19
HELIX 3 AA3 ARG A 87 GLY A 100 1 14
HELIX 4 AA4 SER A 102 MET A 127 1 26
HELIX 5 AA5 PRO A 135 GLY A 137 5 3
HELIX 6 AA6 TYR A 158 CYS A 173 1 16
HELIX 7 AA7 VAL A 187 GLY A 200 1 14
HELIX 8 AA8 GLY A 212 HIS A 222 1 11
HELIX 9 AA9 ASP A 268 LEU A 282 1 15
HELIX 10 AB1 THR A 283 GLN A 286 5 4
HELIX 11 AB2 ILE A 300 GLN A 313 1 14
HELIX 12 AB3 ASN A 332 GLN A 349 1 18
HELIX 13 AB4 ASP A 364 LYS A 368 5 5
HELIX 14 AB5 MET A 385 GLU A 390 1 6
HELIX 15 AB6 THR A 404 ASN A 413 1 10
HELIX 16 AB7 ASP A 427 LEU A 438 1 12
HELIX 17 AB8 PRO A 456 TYR A 460 5 5
HELIX 18 AB9 ARG A 467 TYR A 477 1 11
HELIX 19 AC1 GLY B 47 SER B 66 1 20
HELIX 20 AC2 SER B 69 ARG B 87 1 19
HELIX 21 AC3 ARG B 87 GLY B 100 1 14
HELIX 22 AC4 SER B 102 MET B 127 1 26
HELIX 23 AC5 PRO B 135 GLY B 137 5 3
HELIX 24 AC6 TYR B 158 CYS B 173 1 16
HELIX 25 AC7 VAL B 187 GLY B 200 1 14
HELIX 26 AC8 GLY B 212 HIS B 222 1 11
HELIX 27 AC9 ASP B 268 LEU B 282 1 15
HELIX 28 AD1 THR B 283 GLN B 286 5 4
HELIX 29 AD2 ILE B 300 GLN B 313 1 14
HELIX 30 AD3 ASN B 332 GLN B 349 1 18
HELIX 31 AD4 ASP B 364 LYS B 368 5 5
HELIX 32 AD5 MET B 385 GLU B 390 1 6
HELIX 33 AD6 THR B 404 ASN B 413 1 10
HELIX 34 AD7 ASP B 427 LEU B 438 1 12
HELIX 35 AD8 PRO B 456 TYR B 460 5 5
HELIX 36 AD9 ARG B 467 TYR B 477 1 11
HELIX 37 AE1 GLY C 47 SER C 66 1 20
HELIX 38 AE2 SER C 69 ARG C 87 1 19
HELIX 39 AE3 ARG C 87 GLY C 100 1 14
HELIX 40 AE4 SER C 102 MET C 127 1 26
HELIX 41 AE5 PRO C 135 GLY C 137 5 3
HELIX 42 AE6 TYR C 158 CYS C 173 1 16
HELIX 43 AE7 VAL C 187 GLY C 200 1 14
HELIX 44 AE8 GLY C 212 HIS C 222 1 11
HELIX 45 AE9 ASP C 268 LEU C 282 1 15
HELIX 46 AF1 THR C 283 GLN C 286 5 4
HELIX 47 AF2 ILE C 300 GLN C 313 1 14
HELIX 48 AF3 ASN C 332 GLY C 350 1 19
HELIX 49 AF4 ASP C 364 LYS C 368 5 5
HELIX 50 AF5 MET C 385 GLU C 390 1 6
HELIX 51 AF6 THR C 404 ASN C 413 1 10
HELIX 52 AF7 ASP C 427 LEU C 438 1 12
HELIX 53 AF8 PRO C 456 TYR C 460 5 5
HELIX 54 AF9 ARG C 467 TYR C 477 1 11
HELIX 55 AG1 GLY D 47 SER D 66 1 20
HELIX 56 AG2 SER D 69 ARG D 87 1 19
HELIX 57 AG3 ARG D 87 GLY D 100 1 14
HELIX 58 AG4 SER D 102 MET D 127 1 26
HELIX 59 AG5 PRO D 135 GLY D 137 5 3
HELIX 60 AG6 TYR D 158 CYS D 173 1 16
HELIX 61 AG7 VAL D 187 GLY D 200 1 14
HELIX 62 AG8 GLY D 212 HIS D 222 1 11
HELIX 63 AG9 ASP D 268 LEU D 282 1 15
HELIX 64 AH1 THR D 283 GLN D 286 5 4
HELIX 65 AH2 ILE D 300 GLN D 313 1 14
HELIX 66 AH3 ASN D 332 GLY D 350 1 19
HELIX 67 AH4 ASP D 364 LYS D 368 5 5
HELIX 68 AH5 MET D 385 GLU D 390 1 6
HELIX 69 AH6 THR D 404 ASN D 413 1 10
HELIX 70 AH7 ASP D 427 LEU D 438 1 12
HELIX 71 AH8 PRO D 456 TYR D 460 5 5
HELIX 72 AH9 ARG D 467 TYR D 477 1 11
SHEET 1 AA1 2 ASN A 13 ARG A 15 0
SHEET 2 AA1 2 ALA A 18 VAL A 20 -1 O ALA A 18 N ARG A 15
SHEET 1 AA2 2 ALA A 25 PHE A 32 0
SHEET 2 AA2 2 VAL A 39 SER A 46 -1 O PHE A 43 N GLU A 29
SHEET 1 AA320 LYS B 352 CYS B 355 0
SHEET 2 AA320 CYS B 376 THR B 379 -1 O VAL B 377 N LEU B 354
SHEET 3 AA320 VAL B 396 PHE B 402 1 O MET B 397 N LEU B 378
SHEET 4 AA320 ARG B 293 GLN B 297 1 N VAL B 294 O SER B 398
SHEET 5 AA320 PRO B 260 ILE B 263 1 N ILE B 263 O PHE B 295
SHEET 6 AA320 ALA B 420 PHE B 424 1 O PHE B 424 N ILE B 262
SHEET 7 AA320 THR B 442 ILE B 445 1 O PHE B 444 N VAL B 423
SHEET 8 AA320 SER A 478 VAL A 485 1 N THR A 482 O CYS B 443
SHEET 9 AA320 PHE A 139 PRO A 146 -1 N ARG A 143 O LYS A 481
SHEET 10 AA320 GLY A 129 GLN A 133 -1 N ILE A 132 O GLY A 140
SHEET 11 AA320 GLY C 129 GLN C 133 -1 O GLY C 129 N HIS A 131
SHEET 12 AA320 PHE C 139 PRO C 146 -1 O THR C 142 N GLU C 130
SHEET 13 AA320 SER C 478 VAL C 485 -1 O LYS C 481 N ARG C 143
SHEET 14 AA320 THR D 442 ILE D 445 1 O CYS D 443 N THR C 482
SHEET 15 AA320 ALA D 420 PHE D 424 1 N VAL D 423 O PHE D 444
SHEET 16 AA320 PRO D 260 ILE D 263 1 N ILE D 262 O GLY D 422
SHEET 17 AA320 ARG D 293 GLN D 297 1 O GLN D 297 N ILE D 263
SHEET 18 AA320 VAL D 396 PHE D 402 1 O SER D 398 N VAL D 294
SHEET 19 AA320 CYS D 376 THR D 379 1 N LEU D 378 O MET D 397
SHEET 20 AA320 LYS D 352 CYS D 355 -1 N LEU D 354 O VAL D 377
SHEET 1 AA4 4 PHE A 206 VAL A 208 0
SHEET 2 AA4 4 ALA A 176 LYS A 180 1 N MET A 177 O ASN A 207
SHEET 3 AA4 4 VAL A 149 ILE A 153 1 N GLY A 152 O LYS A 180
SHEET 4 AA4 4 VAL A 225 SER A 229 1 O SER A 229 N VAL A 151
SHEET 1 AA520 LYS A 352 CYS A 355 0
SHEET 2 AA520 CYS A 376 THR A 379 -1 O VAL A 377 N LEU A 354
SHEET 3 AA520 VAL A 396 PHE A 402 1 O MET A 397 N LEU A 378
SHEET 4 AA520 ARG A 293 GLN A 297 1 N VAL A 294 O SER A 398
SHEET 5 AA520 PRO A 260 ILE A 263 1 N ILE A 263 O PHE A 295
SHEET 6 AA520 ALA A 420 PHE A 424 1 O PHE A 424 N ILE A 262
SHEET 7 AA520 THR A 442 ILE A 445 1 O PHE A 444 N VAL A 423
SHEET 8 AA520 SER B 478 VAL B 485 1 O THR B 482 N CYS A 443
SHEET 9 AA520 PHE B 139 PRO B 146 -1 N ARG B 143 O LYS B 481
SHEET 10 AA520 GLY B 129 GLN B 133 -1 N ILE B 132 O GLY B 140
SHEET 11 AA520 GLY D 129 GLN D 133 -1 O GLY D 129 N HIS B 131
SHEET 12 AA520 PHE D 139 PRO D 146 -1 O GLY D 140 N ILE D 132
SHEET 13 AA520 SER D 478 VAL D 485 -1 O LYS D 481 N ARG D 143
SHEET 14 AA520 THR C 442 ILE C 445 1 N CYS C 443 O THR D 482
SHEET 15 AA520 ALA C 420 PHE C 424 1 N VAL C 423 O PHE C 444
SHEET 16 AA520 PRO C 260 ILE C 263 1 N ILE C 262 O GLY C 422
SHEET 17 AA520 ARG C 293 GLN C 297 1 O PHE C 295 N ILE C 263
SHEET 18 AA520 VAL C 396 PHE C 402 1 O SER C 398 N VAL C 294
SHEET 19 AA520 CYS C 376 THR C 379 1 N LEU C 378 O MET C 397
SHEET 20 AA520 LYS C 352 CYS C 355 -1 N LEU C 354 O VAL C 377
SHEET 1 AA6 2 ASN B 13 ARG B 15 0
SHEET 2 AA6 2 ALA B 18 VAL B 20 -1 O ALA B 18 N ARG B 15
SHEET 1 AA7 2 ALA B 25 PHE B 32 0
SHEET 2 AA7 2 VAL B 39 SER B 46 -1 O PHE B 43 N GLU B 29
SHEET 1 AA8 4 PHE B 206 VAL B 208 0
SHEET 2 AA8 4 ALA B 176 LYS B 180 1 N PHE B 179 O ASN B 207
SHEET 3 AA8 4 VAL B 149 ILE B 153 1 N GLY B 152 O LYS B 180
SHEET 4 AA8 4 VAL B 225 SER B 229 1 O SER B 229 N VAL B 151
SHEET 1 AA9 2 ASN C 13 ARG C 15 0
SHEET 2 AA9 2 ALA C 18 VAL C 20 -1 O ALA C 18 N ARG C 15
SHEET 1 AB1 2 ALA C 25 PHE C 32 0
SHEET 2 AB1 2 VAL C 39 SER C 46 -1 O PHE C 43 N GLU C 29
SHEET 1 AB2 4 PHE C 206 VAL C 208 0
SHEET 2 AB2 4 ALA C 176 LYS C 180 1 N PHE C 179 O ASN C 207
SHEET 3 AB2 4 VAL C 149 ILE C 153 1 N CYS C 150 O ALA C 176
SHEET 4 AB2 4 VAL C 225 SER C 229 1 O SER C 229 N VAL C 151
SHEET 1 AB3 2 ASN D 13 ARG D 15 0
SHEET 2 AB3 2 ALA D 18 VAL D 20 -1 O ALA D 18 N ARG D 15
SHEET 1 AB4 2 ALA D 25 PHE D 32 0
SHEET 2 AB4 2 VAL D 39 SER D 46 -1 O PHE D 43 N GLU D 29
SHEET 1 AB5 4 PHE D 206 VAL D 208 0
SHEET 2 AB5 4 ALA D 176 LYS D 180 1 N PHE D 179 O ASN D 207
SHEET 3 AB5 4 VAL D 149 ILE D 153 1 N CYS D 150 O ALA D 176
SHEET 4 AB5 4 VAL D 225 SER D 229 1 O LYS D 227 N VAL D 151
LINK NA NA C 501 O HOH C 677 1555 1555 2.86
LINK OE1 GLU D 118 NA NA D 502 1555 1555 3.20
LINK O ALA D 155 NA NA D 503 1555 1555 2.85
LINK OD1 ASN D 207 NA NA D 501 1555 1555 2.69
LINK NA NA D 501 O2 EDO D 507 1555 1555 2.49
SITE 1 AC1 1 SER A 229
SITE 1 AC2 2 LYS A 227 VAL A 228
SITE 1 AC3 8 PRO A 11 LEU A 12 ASN A 13 GLU A 21
SITE 2 AC3 8 PRO A 22 PHE A 43 THR A 44 GLN A 210
SITE 1 AC4 6 GLU A 118 TYR A 119 HOH A 610 CYS D 74
SITE 2 AC4 6 GLY D 122 HOH D 617
SITE 1 AC5 8 GLY A 154 ALA A 155 PRO A 159 PHE A 179
SITE 2 AC5 8 PRO A 181 SER A 182 THR A 185 HOH A 603
SITE 1 AC6 5 GLU B 118 TYR B 119 GLY B 122 GLY C 122
SITE 2 AC6 5 PEG C 506
SITE 1 AC7 4 ARG B 467 ARG B 471 HOH B 636 ARG C 467
SITE 1 AC8 1 SER B 229
SITE 1 AC9 5 ASP B 24 ALA B 25 LYS B 49 THR C 28
SITE 2 AC9 5 GLU C 29
SITE 1 AD1 1 HOH C 677
SITE 1 AD2 2 GLN C 10 GLU C 194
SITE 1 AD3 2 SER C 9 GLN C 10
SITE 1 AD4 1 SER C 9
SITE 1 AD5 4 SER C 229 VAL C 472 THR C 473 TYR C 476
SITE 1 AD6 7 MET B 71 CYS B 74 GLY B 122 EDO B 501
SITE 2 AD6 7 HOH B 610 GLN C 115 GLU C 118
SITE 1 AD7 8 ILE C 153 GLY C 154 LYS C 180 SER C 182
SITE 2 AD7 8 PRO C 183 GLY C 212 ALA C 213 HOH C 621
SITE 1 AD8 8 TYR D 14 ARG D 15 GLY D 16 GLY D 17
SITE 2 AD8 8 GLY D 204 PHE D 206 ASN D 207 EDO D 507
SITE 1 AD9 2 GLU D 118 EDO D 506
SITE 1 AE1 4 ALA D 155 PRO D 181 SER D 182 THR D 185
SITE 1 AE2 2 SER D 9 GLN D 10
SITE 1 AE3 2 GLN D 10 GLU D 194
SITE 1 AE4 5 GLY A 122 GLU D 118 TYR D 119 GLY D 122
SITE 2 AE4 5 NA D 502
SITE 1 AE5 10 GLY D 17 SER D 197 VAL D 201 PRO D 202
SITE 2 AE5 10 PRO D 203 GLY D 204 LEU D 205 PHE D 206
SITE 3 AE5 10 NA D 501 HOH D 603
SITE 1 AE6 7 LEU D 12 ASN D 13 GLU D 21 PRO D 22
SITE 2 AE6 7 PHE D 43 THR D 44 GLN D 210
SITE 1 AE7 2 GLU D 198 GLY D 200
SITE 1 AE8 3 PHE D 104 ARG D 107 LEU D 108
SITE 1 AE9 4 GLU C 468 ALA D 128 GLY D 129 ARG D 144
CRYST1 164.290 160.030 84.600 90.00 91.09 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006087 0.000000 0.000116 0.00000
SCALE2 0.000000 0.006249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011822 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
