HEADER LYASE 21-APR-11 2YGW
TITLE CRYSTAL STRUCTURE OF HUMAN MCD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALONYL-COA DECARBOXYLASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.1.1.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VOLLMAR,S.PURANIK,T.KROJER,P.SAVITSKY,C.ALLERSTON,W.W.YUE,
AUTHOR 2 A.CHAIKUAD,F.VON DELFT,O.GILEADI,K.KAVANAGH,C.BOUNTRA,
AUTHOR 3 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,U.OPPERMANN
REVDAT 4 24-JAN-18 2YGW 1 AUTHOR JRNL
REVDAT 3 17-JUL-13 2YGW 1 JRNL
REVDAT 2 10-JUL-13 2YGW 1 JRNL
REVDAT 1 15-FEB-12 2YGW 0
JRNL AUTH D.S.FROESE,F.FOROUHAR,T.H.TRAN,M.VOLLMAR,Y.S.KIM,S.LEW,
JRNL AUTH 2 H.NEELY,J.SEETHARAMAN,Y.SHEN,R.XIAO,T.B.ACTON,J.K.EVERETT,
JRNL AUTH 3 G.CANNONE,S.PURANIK,P.SAVITSKY,T.KROJER,E.S.PILKA,W.KIYANI,
JRNL AUTH 4 W.H.LEE,B.D.MARSDEN,F.VON DELFT,C.K.ALLERSTON,L.SPAGNOLO,
JRNL AUTH 5 O.GILEADI,G.T.MONTELIONE,U.OPPERMANN,W.W.YUE,L.TONG
JRNL TITL CRYSTAL STRUCTURES OF MALONYL-COENZYME A DECARBOXYLASE
JRNL TITL 2 PROVIDE INSIGHTS INTO ITS CATALYTIC MECHANISM AND
JRNL TITL 3 DISEASE-CAUSING MUTATIONS.
JRNL REF STRUCTURE V. 21 1182 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 23791943
JRNL DOI 10.1016/J.STR.2013.05.001
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 31694
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1607
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 : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2857
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2579
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2724
REMARK 3 BIN R VALUE (WORKING SET) : 0.2562
REMARK 3 BIN FREE R VALUE : 0.2953
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.66
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
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 : 6249
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 94.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97490
REMARK 3 B22 (A**2) : -2.66620
REMARK 3 B33 (A**2) : 3.64100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.453
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6418 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8738 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2868 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 117 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 979 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6418 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 822 ; 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 : 7133 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.94
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID -9 - 40 AND RESID 41 - 59 AND
REMARK 3 RESID 66 - 114 AND RESID 117 - 275 AND 282 - 343 AND
REMARK 3 RESID 372 - 488)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3018 57.4346 63.6730
REMARK 3 T TENSOR
REMARK 3 T11: -0.0630 T22: -0.3041
REMARK 3 T33: -0.2141 T12: -0.0483
REMARK 3 T13: 0.0696 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.7187 L22: 0.7315
REMARK 3 L33: 2.5983 L12: 0.1387
REMARK 3 L13: 0.2473 L23: -0.2203
REMARK 3 S TENSOR
REMARK 3 S11: -0.1232 S12: 0.1451 S13: -0.0085
REMARK 3 S21: -0.2194 S22: 0.1414 S23: -0.1943
REMARK 3 S31: 0.4789 S32: 0.0821 S33: -0.0182
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND (RESID -2 - 40 AND RESID 41 - 274 AND
REMARK 3 RESID 282 - 343 AND RESID 373 - 487)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0563 66.2527 98.0487
REMARK 3 T TENSOR
REMARK 3 T11: -0.1562 T22: -0.2230
REMARK 3 T33: -0.1764 T12: 0.0493
REMARK 3 T13: 0.0124 T23: 0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 1.2417 L22: 1.4201
REMARK 3 L33: 2.1129 L12: 0.2744
REMARK 3 L13: 0.8840 L23: 0.0532
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: -0.0671 S13: 0.0497
REMARK 3 S21: 0.0087 S22: -0.1083 S23: -0.2140
REMARK 3 S31: 0.1223 S32: 0.0701 S33: 0.0779
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=UNK. NUMBER OF
REMARK 3 ATOMS WITH PROPER CCP4 ATOM TYPE=6350. NUMBER WITH APPROX
REMARK 3 DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED
REMARK 3 CONTACTS=2.
REMARK 4
REMARK 4 2YGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1290048089.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-AUG-10
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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31699
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 1.06000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000,0.1M MES (PH 6.5)
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 75.87800
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 75.87800
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 47.81350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 87.67100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.81350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 87.67100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.87800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.81350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 87.67100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.87800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.81350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 87.67100
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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 58 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LYS 59 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 278 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 289 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LYS 280 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 58 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LYS 59 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 278 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 279 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LYS 280 TO ALA
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 THR A 60
REMARK 465 PRO A 61
REMARK 465 ALA A 62
REMARK 465 PRO A 63
REMARK 465 ALA A 64
REMARK 465 GLU A 65
REMARK 465 GLN A 115
REMARK 465 GLN A 116
REMARK 465 GLU A 276
REMARK 465 THR A 277
REMARK 465 ALA A 278
REMARK 465 ALA A 279
REMARK 465 ALA A 280
REMARK 465 ASN A 281
REMARK 465 SER A 344
REMARK 465 GLN A 345
REMARK 465 THR A 346
REMARK 465 LYS A 347
REMARK 465 GLU A 348
REMARK 465 HIS A 349
REMARK 465 GLY A 350
REMARK 465 ARG A 351
REMARK 465 ASN A 352
REMARK 465 GLU A 353
REMARK 465 LEU A 354
REMARK 465 PHE A 355
REMARK 465 THR A 356
REMARK 465 ASP A 357
REMARK 465 SER A 358
REMARK 465 GLU A 359
REMARK 465 CYS A 360
REMARK 465 LYS A 361
REMARK 465 GLU A 362
REMARK 465 ILE A 363
REMARK 465 SER A 364
REMARK 465 GLU A 365
REMARK 465 ILE A 366
REMARK 465 THR A 367
REMARK 465 GLY A 368
REMARK 465 GLY A 369
REMARK 465 PRO A 370
REMARK 465 ILE A 371
REMARK 465 LYS A 489
REMARK 465 ASN A 490
REMARK 465 GLY B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 SER B 275
REMARK 465 GLU B 276
REMARK 465 THR B 277
REMARK 465 ALA B 278
REMARK 465 ALA B 279
REMARK 465 ALA B 280
REMARK 465 ASN B 281
REMARK 465 SER B 344
REMARK 465 GLN B 345
REMARK 465 THR B 346
REMARK 465 LYS B 347
REMARK 465 GLU B 348
REMARK 465 HIS B 349
REMARK 465 GLY B 350
REMARK 465 ARG B 351
REMARK 465 ASN B 352
REMARK 465 GLU B 353
REMARK 465 LEU B 354
REMARK 465 PHE B 355
REMARK 465 THR B 356
REMARK 465 ASP B 357
REMARK 465 SER B 358
REMARK 465 GLU B 359
REMARK 465 CYS B 360
REMARK 465 LYS B 361
REMARK 465 GLU B 362
REMARK 465 ILE B 363
REMARK 465 SER B 364
REMARK 465 GLU B 365
REMARK 465 ILE B 366
REMARK 465 THR B 367
REMARK 465 GLY B 368
REMARK 465 GLY B 369
REMARK 465 PRO B 370
REMARK 465 ILE B 371
REMARK 465 ASN B 372
REMARK 465 GLN B 488
REMARK 465 LYS B 489
REMARK 465 ASN B 490
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A -4 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 SER A 73 OG
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 THR A 81 OG1 CG2
REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 101 CG CD OE1 NE2
REMARK 470 GLU A 104 CG CD OE1 OE2
REMARK 470 ARG A 113 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 GLU A 118 CG CD OE1 OE2
REMARK 470 VAL A 121 CG1 CG2
REMARK 470 GLU A 171 CG CD OE1 OE2
REMARK 470 SER A 187 OG
REMARK 470 SER A 213 OG
REMARK 470 VAL A 218 CG1 CG2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 MET A 227 CG SD CE
REMARK 470 LYS A 228 CG CD CE NZ
REMARK 470 VAL A 269 CG1 CG2
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 SER A 275 OG
REMARK 470 LYS A 282 CG CD CE NZ
REMARK 470 ILE A 283 CG1 CG2 CD1
REMARK 470 GLN A 299 CG CD OE1 NE2
REMARK 470 VAL A 301 CG1 CG2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 LYS A 313 CG CD CE NZ
REMARK 470 ILE A 331 O
REMARK 470 LEU A 338 CG CD1 CD2
REMARK 470 ASN A 343 CG OD1 ND2
REMARK 470 ASN A 372 CG OD1 ND2
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 THR A 374 OG1 CG2
REMARK 470 LEU A 375 CG CD1 CD2
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 LEU A 378 CG CD1 CD2
REMARK 470 LEU A 379 CG CD1 CD2
REMARK 470 SER A 382 OG
REMARK 470 GLU A 383 CG CD OE1 OE2
REMARK 470 VAL A 385 CG1 CG2
REMARK 470 GLN A 386 CG CD OE1 NE2
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 ARG A 392 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 441 CG CD1 CD2
REMARK 470 ARG A 442 CG CD NE CZ NH1 NH2
REMARK 470 SER A 471 OG
REMARK 470 GLU A 478 CG CD OE1 OE2
REMARK 470 GLN B -2 CG CD OE1 NE2
REMARK 470 GLU B 42 CG CD OE1 OE2
REMARK 470 GLU B 80 CG CD OE1 OE2
REMARK 470 HIS B 111 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 114 CG CD OE1 NE2
REMARK 470 GLN B 116 CG CD OE1 NE2
REMARK 470 GLU B 118 CG CD OE1 OE2
REMARK 470 VAL B 121 CG1 CG2
REMARK 470 LYS B 146 NZ
REMARK 470 LYS B 228 CG CD CE NZ
REMARK 470 VAL B 269 CG1 CG2
REMARK 470 LYS B 270 CG CD CE NZ
REMARK 470 GLU B 271 CG CD OE1 OE2
REMARK 470 LYS B 282 CG CD CE NZ
REMARK 470 ILE B 283 CG1 CG2 CD1
REMARK 470 ILE B 291 CG1 CG2 CD1
REMARK 470 GLN B 296 CG CD OE1 NE2
REMARK 470 GLU B 302 CG CD OE1 OE2
REMARK 470 LYS B 309 CG CD CE NZ
REMARK 470 LYS B 313 CG CD CE NZ
REMARK 470 ILE B 331 O
REMARK 470 LYS B 336 CG CD CE NZ
REMARK 470 GLU B 373 CG CD OE1 OE2
REMARK 470 THR B 374 OG1 CG2
REMARK 470 LEU B 375 CG CD1 CD2
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 LEU B 378 CG CD1 CD2
REMARK 470 LEU B 379 CG CD1 CD2
REMARK 470 SER B 382 OG
REMARK 470 VAL B 385 CG1 CG2
REMARK 470 GLN B 386 CG CD OE1 NE2
REMARK 470 SER B 387 OG
REMARK 470 GLU B 388 CG CD OE1 OE2
REMARK 470 LYS B 389 CG CD CE NZ
REMARK 470 LEU B 390 CG CD1 CD2
REMARK 470 ARG B 392 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 394 CG CD1 CD2
REMARK 470 ARG B 412 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 430 CG CD1 CD2
REMARK 470 LEU B 441 CG CD1 CD2
REMARK 470 SER B 447 OG
REMARK 470 SER B 471 OG
REMARK 470 LYS B 475 CG CD CE NZ
REMARK 470 SER B 477 OG
REMARK 470 GLU B 478 CG CD OE1 OE2
REMARK 470 SER B 482 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 79 -75.62 -74.08
REMARK 500 VAL A 218 -70.19 -53.79
REMARK 500 LYS A 270 73.90 -104.46
REMARK 500 PRO A 320 -4.27 -59.01
REMARK 500 ILE A 331 71.73 -111.18
REMARK 500 LEU A 342 34.97 -67.23
REMARK 500 SER A 380 78.62 -67.27
REMARK 500 SER A 381 73.46 -171.54
REMARK 500 SER A 382 -54.26 62.54
REMARK 500 GLN A 395 -70.66 -66.52
REMARK 500 ALA B 79 -75.80 -71.02
REMARK 500 GLN B 116 92.95 -66.54
REMARK 500 VAL B 218 -67.97 -140.18
REMARK 500 ILE B 268 -64.32 -90.16
REMARK 500 LYS B 270 74.04 -105.03
REMARK 500 LEU B 342 34.25 -67.30
REMARK 500 SER B 380 78.33 -67.67
REMARK 500 SER B 381 73.36 -170.71
REMARK 500 SER B 382 -54.64 62.87
REMARK 500 LEU B 430 88.62 -64.68
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 EDO B 1489
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N TERMINAL GTENLYFQSM SEQUENCE DUE TO CLONING AND
REMARK 999 UNCLEAVED TAG AND MUTATIONS E58A K59A E278A E279A K280A
DBREF 2YGW A 40 490 UNP O95822 DCMC_HUMAN 40 490
DBREF 2YGW B 40 490 UNP O95822 DCMC_HUMAN 40 490
SEQADV 2YGW GLY A -9 UNP O95822 EXPRESSION TAG
SEQADV 2YGW THR A -8 UNP O95822 EXPRESSION TAG
SEQADV 2YGW GLU A -7 UNP O95822 EXPRESSION TAG
SEQADV 2YGW ASN A -6 UNP O95822 EXPRESSION TAG
SEQADV 2YGW LEU A -5 UNP O95822 EXPRESSION TAG
SEQADV 2YGW TYR A -4 UNP O95822 EXPRESSION TAG
SEQADV 2YGW PHE A -3 UNP O95822 EXPRESSION TAG
SEQADV 2YGW GLN A -2 UNP O95822 EXPRESSION TAG
SEQADV 2YGW SER A -1 UNP O95822 EXPRESSION TAG
SEQADV 2YGW ALA A 58 UNP O95822 GLU 58 ENGINEERED MUTATION
SEQADV 2YGW ALA A 59 UNP O95822 LYS 59 ENGINEERED MUTATION
SEQADV 2YGW ALA A 278 UNP O95822 GLU 278 ENGINEERED MUTATION
SEQADV 2YGW ALA A 279 UNP O95822 GLU 279 ENGINEERED MUTATION
SEQADV 2YGW ALA A 280 UNP O95822 LYS 280 ENGINEERED MUTATION
SEQADV 2YGW GLY B -9 UNP O95822 EXPRESSION TAG
SEQADV 2YGW THR B -8 UNP O95822 EXPRESSION TAG
SEQADV 2YGW GLU B -7 UNP O95822 EXPRESSION TAG
SEQADV 2YGW ASN B -6 UNP O95822 EXPRESSION TAG
SEQADV 2YGW LEU B -5 UNP O95822 EXPRESSION TAG
SEQADV 2YGW TYR B -4 UNP O95822 EXPRESSION TAG
SEQADV 2YGW PHE B -3 UNP O95822 EXPRESSION TAG
SEQADV 2YGW GLN B -2 UNP O95822 EXPRESSION TAG
SEQADV 2YGW SER B -1 UNP O95822 EXPRESSION TAG
SEQADV 2YGW ALA B 58 UNP O95822 GLU 58 ENGINEERED MUTATION
SEQADV 2YGW ALA B 59 UNP O95822 LYS 59 ENGINEERED MUTATION
SEQADV 2YGW ALA B 278 UNP O95822 GLU 278 ENGINEERED MUTATION
SEQADV 2YGW ALA B 279 UNP O95822 GLU 279 ENGINEERED MUTATION
SEQADV 2YGW ALA B 280 UNP O95822 LYS 280 ENGINEERED MUTATION
SEQRES 1 A 460 GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP GLU LEU
SEQRES 2 A 460 LEU ARG ARG ALA VAL PRO PRO THR PRO ALA TYR GLU LEU
SEQRES 3 A 460 ARG ALA ALA THR PRO ALA PRO ALA GLU GLY GLN CYS ALA
SEQRES 4 A 460 ASP PHE VAL SER PHE TYR GLY GLY LEU ALA GLU THR ALA
SEQRES 5 A 460 GLN ARG ALA GLU LEU LEU GLY ARG LEU ALA ARG GLY PHE
SEQRES 6 A 460 GLY VAL ASP HIS GLY GLN VAL ALA GLU GLN SER ALA GLY
SEQRES 7 A 460 VAL LEU HIS LEU ARG GLN GLN GLN ARG GLU ALA ALA VAL
SEQRES 8 A 460 LEU LEU GLN ALA GLU ASP ARG LEU ARG TYR ALA LEU VAL
SEQRES 9 A 460 PRO ARG TYR ARG GLY LEU PHE HIS HIS ILE SER LYS LEU
SEQRES 10 A 460 ASP GLY GLY VAL ARG PHE LEU VAL GLN LEU ARG ALA ASP
SEQRES 11 A 460 LEU LEU GLU ALA GLN ALA LEU LYS LEU VAL GLU GLY PRO
SEQRES 12 A 460 ASP VAL ARG GLU MET ASN GLY VAL LEU LYS GLY MET LEU
SEQRES 13 A 460 SER GLU TRP PHE SER SER GLY PHE LEU ASN LEU GLU ARG
SEQRES 14 A 460 VAL THR TRP HIS SER PRO CYS GLU VAL LEU GLN LYS ILE
SEQRES 15 A 460 SER GLU ALA GLU ALA VAL HIS PRO VAL LYS ASN TRP MET
SEQRES 16 A 460 ASP MET LYS ARG ARG VAL GLY PRO TYR ARG ARG CYS TYR
SEQRES 17 A 460 PHE PHE SER HIS CYS SER THR PRO GLY GLU PRO LEU VAL
SEQRES 18 A 460 VAL LEU HIS VAL ALA LEU THR GLY ASP ILE SER SER ASN
SEQRES 19 A 460 ILE GLN ALA ILE VAL LYS GLU HIS PRO PRO SER GLU THR
SEQRES 20 A 460 ALA ALA ALA ASN LYS ILE THR ALA ALA ILE PHE TYR SER
SEQRES 21 A 460 ILE SER LEU THR GLN GLN GLY LEU GLN GLY VAL GLU LEU
SEQRES 22 A 460 GLY THR PHE LEU ILE LYS ARG VAL VAL LYS GLU LEU GLN
SEQRES 23 A 460 ARG GLU PHE PRO HIS LEU GLY VAL PHE SER SER LEU SER
SEQRES 24 A 460 PRO ILE PRO GLY PHE THR LYS TRP LEU LEU GLY LEU LEU
SEQRES 25 A 460 ASN SER GLN THR LYS GLU HIS GLY ARG ASN GLU LEU PHE
SEQRES 26 A 460 THR ASP SER GLU CYS LYS GLU ILE SER GLU ILE THR GLY
SEQRES 27 A 460 GLY PRO ILE ASN GLU THR LEU LYS LEU LEU LEU SER SER
SEQRES 28 A 460 SER GLU TRP VAL GLN SER GLU LYS LEU VAL ARG ALA LEU
SEQRES 29 A 460 GLN THR PRO LEU MET ARG LEU CYS ALA TRP TYR LEU TYR
SEQRES 30 A 460 GLY GLU LYS HIS ARG GLY TYR ALA LEU ASN PRO VAL ALA
SEQRES 31 A 460 ASN PHE HIS LEU GLN ASN GLY ALA VAL LEU TRP ARG ILE
SEQRES 32 A 460 ASN TRP MET ALA ASP VAL SER LEU ARG GLY ILE THR GLY
SEQRES 33 A 460 SER CYS GLY LEU MET ALA ASN TYR ARG TYR PHE LEU GLU
SEQRES 34 A 460 GLU THR GLY PRO ASN SER THR SER TYR LEU GLY SER LYS
SEQRES 35 A 460 ILE ILE LYS ALA SER GLU GLN VAL LEU SER LEU VAL ALA
SEQRES 36 A 460 GLN PHE GLN LYS ASN
SEQRES 1 B 460 GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP GLU LEU
SEQRES 2 B 460 LEU ARG ARG ALA VAL PRO PRO THR PRO ALA TYR GLU LEU
SEQRES 3 B 460 ARG ALA ALA THR PRO ALA PRO ALA GLU GLY GLN CYS ALA
SEQRES 4 B 460 ASP PHE VAL SER PHE TYR GLY GLY LEU ALA GLU THR ALA
SEQRES 5 B 460 GLN ARG ALA GLU LEU LEU GLY ARG LEU ALA ARG GLY PHE
SEQRES 6 B 460 GLY VAL ASP HIS GLY GLN VAL ALA GLU GLN SER ALA GLY
SEQRES 7 B 460 VAL LEU HIS LEU ARG GLN GLN GLN ARG GLU ALA ALA VAL
SEQRES 8 B 460 LEU LEU GLN ALA GLU ASP ARG LEU ARG TYR ALA LEU VAL
SEQRES 9 B 460 PRO ARG TYR ARG GLY LEU PHE HIS HIS ILE SER LYS LEU
SEQRES 10 B 460 ASP GLY GLY VAL ARG PHE LEU VAL GLN LEU ARG ALA ASP
SEQRES 11 B 460 LEU LEU GLU ALA GLN ALA LEU LYS LEU VAL GLU GLY PRO
SEQRES 12 B 460 ASP VAL ARG GLU MET ASN GLY VAL LEU LYS GLY MET LEU
SEQRES 13 B 460 SER GLU TRP PHE SER SER GLY PHE LEU ASN LEU GLU ARG
SEQRES 14 B 460 VAL THR TRP HIS SER PRO CYS GLU VAL LEU GLN LYS ILE
SEQRES 15 B 460 SER GLU ALA GLU ALA VAL HIS PRO VAL LYS ASN TRP MET
SEQRES 16 B 460 ASP MET LYS ARG ARG VAL GLY PRO TYR ARG ARG CYS TYR
SEQRES 17 B 460 PHE PHE SER HIS CYS SER THR PRO GLY GLU PRO LEU VAL
SEQRES 18 B 460 VAL LEU HIS VAL ALA LEU THR GLY ASP ILE SER SER ASN
SEQRES 19 B 460 ILE GLN ALA ILE VAL LYS GLU HIS PRO PRO SER GLU THR
SEQRES 20 B 460 ALA ALA ALA ASN LYS ILE THR ALA ALA ILE PHE TYR SER
SEQRES 21 B 460 ILE SER LEU THR GLN GLN GLY LEU GLN GLY VAL GLU LEU
SEQRES 22 B 460 GLY THR PHE LEU ILE LYS ARG VAL VAL LYS GLU LEU GLN
SEQRES 23 B 460 ARG GLU PHE PRO HIS LEU GLY VAL PHE SER SER LEU SER
SEQRES 24 B 460 PRO ILE PRO GLY PHE THR LYS TRP LEU LEU GLY LEU LEU
SEQRES 25 B 460 ASN SER GLN THR LYS GLU HIS GLY ARG ASN GLU LEU PHE
SEQRES 26 B 460 THR ASP SER GLU CYS LYS GLU ILE SER GLU ILE THR GLY
SEQRES 27 B 460 GLY PRO ILE ASN GLU THR LEU LYS LEU LEU LEU SER SER
SEQRES 28 B 460 SER GLU TRP VAL GLN SER GLU LYS LEU VAL ARG ALA LEU
SEQRES 29 B 460 GLN THR PRO LEU MET ARG LEU CYS ALA TRP TYR LEU TYR
SEQRES 30 B 460 GLY GLU LYS HIS ARG GLY TYR ALA LEU ASN PRO VAL ALA
SEQRES 31 B 460 ASN PHE HIS LEU GLN ASN GLY ALA VAL LEU TRP ARG ILE
SEQRES 32 B 460 ASN TRP MET ALA ASP VAL SER LEU ARG GLY ILE THR GLY
SEQRES 33 B 460 SER CYS GLY LEU MET ALA ASN TYR ARG TYR PHE LEU GLU
SEQRES 34 B 460 GLU THR GLY PRO ASN SER THR SER TYR LEU GLY SER LYS
SEQRES 35 B 460 ILE ILE LYS ALA SER GLU GLN VAL LEU SER LEU VAL ALA
SEQRES 36 B 460 GLN PHE GLN LYS ASN
HET UNX A1490 1
HET UNX B1490 1
HET EDO B1489 4
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 UNX 2(X)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 HOH *82(H2 O)
HELIX 1 1 THR A -8 VAL A 48 1 17
HELIX 2 2 ALA A 53 ARG A 57 5 5
HELIX 3 3 GLY A 66 GLY A 77 1 12
HELIX 4 4 GLU A 80 PHE A 95 1 16
HELIX 5 5 ASP A 98 ARG A 113 1 16
HELIX 6 6 GLU A 118 LEU A 133 1 16
HELIX 7 7 TYR A 137 LYS A 146 1 10
HELIX 8 8 GLY A 149 LEU A 167 1 19
HELIX 9 9 GLY A 172 PHE A 190 1 19
HELIX 10 10 SER A 191 GLY A 193 5 3
HELIX 11 11 PRO A 205 ALA A 215 1 11
HELIX 12 12 ASN A 223 VAL A 231 1 9
HELIX 13 13 ILE A 265 LYS A 270 1 6
HELIX 14 14 GLN A 295 GLN A 299 5 5
HELIX 15 15 GLU A 302 PHE A 319 1 18
HELIX 16 16 GLY A 333 LEU A 342 1 10
HELIX 17 17 GLU A 373 SER A 380 1 8
HELIX 18 18 SER A 382 GLN A 386 5 5
HELIX 19 19 SER A 387 LEU A 394 1 8
HELIX 20 20 LEU A 394 GLY A 408 1 15
HELIX 21 21 ASN A 417 ASN A 426 1 10
HELIX 22 22 SER A 440 CYS A 448 1 9
HELIX 23 23 PHE A 457 GLU A 459 5 3
HELIX 24 24 GLU A 460 LYS A 472 1 13
HELIX 25 25 SER A 477 PHE A 487 1 11
HELIX 26 26 GLN B -2 VAL B 48 1 11
HELIX 27 27 ALA B 53 ARG B 57 5 5
HELIX 28 28 ALA B 62 GLY B 77 1 16
HELIX 29 29 GLU B 80 PHE B 95 1 16
HELIX 30 30 ASP B 98 GLN B 115 1 18
HELIX 31 31 GLU B 118 LEU B 133 1 16
HELIX 32 32 TYR B 137 LYS B 146 1 10
HELIX 33 33 GLY B 149 LEU B 167 1 19
HELIX 34 34 GLY B 172 PHE B 190 1 19
HELIX 35 35 SER B 191 GLY B 193 5 3
HELIX 36 36 PRO B 205 ALA B 215 1 11
HELIX 37 37 ASN B 223 GLY B 232 1 10
HELIX 38 38 ILE B 265 LYS B 270 1 6
HELIX 39 39 GLN B 295 GLN B 299 5 5
HELIX 40 40 GLU B 302 PHE B 319 1 18
HELIX 41 41 GLY B 333 LEU B 342 1 10
HELIX 42 42 THR B 374 SER B 380 1 7
HELIX 43 43 SER B 382 GLN B 386 5 5
HELIX 44 44 SER B 387 LEU B 394 1 8
HELIX 45 45 LEU B 394 GLY B 408 1 15
HELIX 46 46 ASN B 417 ASN B 426 1 10
HELIX 47 47 SER B 440 CYS B 448 1 9
HELIX 48 48 PHE B 457 GLU B 459 5 3
HELIX 49 49 GLU B 460 LYS B 472 1 13
HELIX 50 50 SER B 477 PHE B 487 1 11
SHEET 1 AA 5 LEU A 195 VAL A 200 0
SHEET 2 AA 5 ARG A 235 HIS A 242 -1 O CYS A 237 N VAL A 200
SHEET 3 AA 5 VAL A 251 THR A 258 -1 O VAL A 251 N PHE A 240
SHEET 4 AA 5 ALA A 285 LEU A 293 -1 O ALA A 285 N THR A 258
SHEET 5 AA 5 VAL A 324 SER A 327 1 O VAL A 324 N ALA A 286
SHEET 1 AB 2 LYS A 410 HIS A 411 0
SHEET 2 AB 2 TYR A 414 ALA A 415 -1 O TYR A 414 N HIS A 411
SHEET 1 AC 2 VAL A 429 ASN A 434 0
SHEET 2 AC 2 MET A 451 ARG A 455 -1 O MET A 451 N ASN A 434
SHEET 1 BA 7 LEU B 195 VAL B 200 0
SHEET 2 BA 7 ARG B 235 HIS B 242 -1 O CYS B 237 N VAL B 200
SHEET 3 BA 7 VAL B 251 THR B 258 -1 O VAL B 251 N PHE B 240
SHEET 4 BA 7 ALA B 285 LEU B 293 -1 O ALA B 285 N THR B 258
SHEET 5 BA 7 VAL B 324 SER B 327 1 O VAL B 324 N ALA B 286
SHEET 6 BA 7 MET B 451 TYR B 456 -1 O TYR B 454 N SER B 327
SHEET 7 BA 7 VAL B 429 ASN B 434 -1 O VAL B 429 N ARG B 455
SHEET 1 BB 2 LYS B 410 HIS B 411 0
SHEET 2 BB 2 TYR B 414 ALA B 415 -1 O TYR B 414 N HIS B 411
SSBOND 1 CYS A 243 CYS B 243 1555 1555 2.97
SITE 1 AC1 4 THR B 51 PRO B 135 ARG B 136 GLY B 139
CRYST1 95.627 175.342 151.756 90.00 90.00 90.00 C 2 2 21 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 0.010457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006590 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
