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HEADER HYDROLASE 09-MAR-20 6Y9E
TITLE CRYSTAL STRUCTURE OF PUTATIVE ANCESTRAL HALOALKANE DEHALOGENASE
TITLE 2 ANCHLD2 (NODE 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANCESTRAL HALOALKANE DEHALOGENASE ANCHLD2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHALOUPKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 18-NOV-20 6Y9E 0
JRNL AUTH P.BABKOVA,Z.DUNAJOVA,R.CHALOUPKOVA,J.DAMBORSKY,D.BEDNAR,
JRNL AUTH 2 M.MAREK
JRNL TITL STRUCTURES OF HYPERSTABLE ANCESTRAL HALOALKANE DEHALOGENASES
JRNL TITL 2 SHOW RESTRICTED CONFORMATIONAL DYNAMICS.
JRNL REF COMPUT STRUCT BIOTECHNOL J V. 18 1497 2020
JRNL REFN ISSN 2001-0370
JRNL PMID 32637047
JRNL DOI 10.1016/J.CSBJ.2020.06.021
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14-3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 201065
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 9946
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 67.6170 - 5.2815 1.00 6781 331 0.1679 0.1884
REMARK 3 2 5.2815 - 4.1923 1.00 6482 366 0.1357 0.1632
REMARK 3 3 4.1923 - 3.6624 1.00 6472 343 0.1340 0.1733
REMARK 3 4 3.6624 - 3.3275 1.00 6385 384 0.1502 0.1751
REMARK 3 5 3.3275 - 3.0890 1.00 6430 337 0.1572 0.1994
REMARK 3 6 3.0890 - 2.9069 1.00 6421 336 0.1629 0.1982
REMARK 3 7 2.9069 - 2.7613 1.00 6393 340 0.1699 0.2162
REMARK 3 8 2.7613 - 2.6411 1.00 6381 327 0.1782 0.2181
REMARK 3 9 2.6411 - 2.5394 1.00 6401 312 0.1716 0.2096
REMARK 3 10 2.5394 - 2.4518 1.00 6344 352 0.1695 0.2426
REMARK 3 11 2.4518 - 2.3751 1.00 6397 301 0.1720 0.2164
REMARK 3 12 2.3751 - 2.3072 1.00 6349 338 0.1733 0.2187
REMARK 3 13 2.3072 - 2.2465 1.00 6354 336 0.1843 0.2264
REMARK 3 14 2.2465 - 2.1917 1.00 6297 342 0.1824 0.2267
REMARK 3 15 2.1917 - 2.1419 1.00 6366 342 0.1984 0.2327
REMARK 3 16 2.1419 - 2.0963 1.00 6314 342 0.2169 0.2538
REMARK 3 17 2.0963 - 2.0543 1.00 6368 320 0.2319 0.2711
REMARK 3 18 2.0543 - 2.0156 1.00 6358 318 0.2286 0.2794
REMARK 3 19 2.0156 - 1.9796 1.00 6336 313 0.2296 0.2588
REMARK 3 20 1.9796 - 1.9460 1.00 6341 326 0.2404 0.2765
REMARK 3 21 1.9460 - 1.9146 1.00 6292 355 0.2474 0.2980
REMARK 3 22 1.9146 - 1.8852 1.00 6340 321 0.2506 0.3166
REMARK 3 23 1.8852 - 1.8574 1.00 6268 330 0.2752 0.3282
REMARK 3 24 1.8574 - 1.8313 1.00 6341 314 0.2852 0.3088
REMARK 3 25 1.8313 - 1.8065 1.00 6356 331 0.2935 0.3620
REMARK 3 26 1.8065 - 1.7831 1.00 6304 313 0.3110 0.3723
REMARK 3 27 1.7831 - 1.7608 1.00 6349 322 0.3281 0.3535
REMARK 3 28 1.7608 - 1.7395 1.00 6313 319 0.3359 0.3610
REMARK 3 29 1.7395 - 1.7193 1.00 6270 298 0.3522 0.3978
REMARK 3 30 1.7193 - 1.7000 1.00 6316 337 0.3694 0.3987
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6Y9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-20.
REMARK 100 THE DEPOSITION ID IS D_1292107176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 201162
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 67.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.51400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: 4K2A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MAGNESIUM CHLORIDE, TRIS
REMARK 280 BASE, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 54.79000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.31000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 513 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 297
REMARK 465 THR A 298
REMARK 465 ALA A 299
REMARK 465 LYS A 300
REMARK 465 ALA A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 297
REMARK 465 THR B 298
REMARK 465 ALA B 299
REMARK 465 LYS B 300
REMARK 465 ALA B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 297
REMARK 465 THR C 298
REMARK 465 ALA C 299
REMARK 465 LYS C 300
REMARK 465 ALA C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 HIS C 304
REMARK 465 HIS C 305
REMARK 465 HIS C 306
REMARK 465 HIS C 307
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 THR D 3
REMARK 465 SER D 4
REMARK 465 ALA D 5
REMARK 465 ASP D 6
REMARK 465 THR D 298
REMARK 465 ALA D 299
REMARK 465 LYS D 300
REMARK 465 ALA D 301
REMARK 465 HIS D 302
REMARK 465 HIS D 303
REMARK 465 HIS D 304
REMARK 465 HIS D 305
REMARK 465 HIS D 306
REMARK 465 HIS D 307
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 THR E 3
REMARK 465 SER E 4
REMARK 465 ALA E 5
REMARK 465 ASP E 6
REMARK 465 ILE E 7
REMARK 465 SER E 8
REMARK 465 SER E 296
REMARK 465 ALA E 297
REMARK 465 THR E 298
REMARK 465 ALA E 299
REMARK 465 LYS E 300
REMARK 465 ALA E 301
REMARK 465 HIS E 302
REMARK 465 HIS E 303
REMARK 465 HIS E 304
REMARK 465 HIS E 305
REMARK 465 HIS E 306
REMARK 465 HIS E 307
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 THR F 3
REMARK 465 SER F 4
REMARK 465 ALA F 5
REMARK 465 SER F 296
REMARK 465 ALA F 297
REMARK 465 THR F 298
REMARK 465 ALA F 299
REMARK 465 LYS F 300
REMARK 465 ALA F 301
REMARK 465 HIS F 302
REMARK 465 HIS F 303
REMARK 465 HIS F 304
REMARK 465 HIS F 305
REMARK 465 HIS F 306
REMARK 465 HIS F 307
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 PHE B 204 N CA C O CB CG CD1
REMARK 480 PHE B 204 CD2 CE1 CE2 CZ
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 LEU A 15 -123.81 48.42
REMARK 500 SER A 17 -159.97 -149.48
REMARK 500 ASP A 103 -133.90 60.41
REMARK 500 HIS A 139 -160.39 64.06
REMARK 500 ARG A 170 -59.24 -127.49
REMARK 500 ALA A 244 -78.06 -139.27
REMARK 500 LEU A 270 -107.88 -125.21
REMARK 500 LEU B 15 -116.44 53.76
REMARK 500 SER B 17 -156.76 -149.03
REMARK 500 PRO B 39 50.72 -111.40
REMARK 500 THR B 40 -158.21 -100.70
REMARK 500 ASP B 103 -134.40 60.53
REMARK 500 HIS B 139 -159.33 64.07
REMARK 500 ARG B 170 -55.26 -126.76
REMARK 500 ALA B 244 -78.76 -141.01
REMARK 500 LEU B 270 -110.37 -121.56
REMARK 500 LEU C 15 -125.36 49.62
REMARK 500 SER C 17 -156.53 -131.26
REMARK 500 PRO C 39 51.17 -110.48
REMARK 500 ASP C 103 -132.95 63.16
REMARK 500 HIS C 139 -159.82 63.85
REMARK 500 ARG C 170 -47.82 -130.76
REMARK 500 ALA C 244 -78.27 -142.22
REMARK 500 LEU C 270 -111.57 -116.62
REMARK 500 LEU D 15 -125.43 49.91
REMARK 500 PRO D 39 52.15 -111.68
REMARK 500 THR D 40 -156.38 -99.89
REMARK 500 ASP D 103 -133.01 59.17
REMARK 500 HIS D 139 -157.94 64.23
REMARK 500 ALA D 244 -81.31 -145.18
REMARK 500 LEU D 270 -105.39 -120.82
REMARK 500 LEU E 15 -118.90 47.31
REMARK 500 SER E 17 -158.28 -156.82
REMARK 500 PRO E 39 50.36 -111.77
REMARK 500 THR E 40 -158.27 -100.78
REMARK 500 ASP E 103 -132.98 59.12
REMARK 500 MET E 126 148.21 -171.15
REMARK 500 HIS E 139 -165.87 60.59
REMARK 500 ARG E 170 -53.96 -127.18
REMARK 500 ALA E 244 -80.00 -136.58
REMARK 500 LEU E 270 -106.84 -118.80
REMARK 500 LEU F 15 -126.45 53.52
REMARK 500 SER F 17 -149.72 -139.36
REMARK 500 PRO F 39 51.65 -110.03
REMARK 500 THR F 40 -157.08 -102.58
REMARK 500 ASP F 103 -132.92 59.45
REMARK 500 HIS F 139 -160.81 59.74
REMARK 500 ARG F 170 -52.96 -123.85
REMARK 500 ALA F 244 -75.55 -138.35
REMARK 500 LEU F 270 -107.65 -110.72
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 407
DBREF 6Y9E A 1 307 PDB 6Y9E 6Y9E 1 307
DBREF 6Y9E B 1 307 PDB 6Y9E 6Y9E 1 307
DBREF 6Y9E C 1 307 PDB 6Y9E 6Y9E 1 307
DBREF 6Y9E D 1 307 PDB 6Y9E 6Y9E 1 307
DBREF 6Y9E E 1 307 PDB 6Y9E 6Y9E 1 307
DBREF 6Y9E F 1 307 PDB 6Y9E 6Y9E 1 307
SEQRES 1 A 307 MET THR THR SER ALA ASP ILE SER LEU ARG HIS VAL SER
SEQRES 2 A 307 VAL LEU ASP SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 A 307 SER ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO LEU VAL
SEQRES 5 A 307 ALA PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 A 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP LYS
SEQRES 8 A 307 LEU GLY ILE GLU SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 A 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 A 307 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN THR PRO GLN
SEQRES 12 A 307 ALA ARG GLU MET PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 A 307 GLY GLU GLN MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 A 307 ARG VAL LEU PRO GLY SER ILE VAL ARG LYS LEU SER GLU
SEQRES 15 A 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 A 307 GLU SER ARG ARG PRO THR LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 A 307 PRO ILE ALA GLY GLU PRO ALA ASP VAL TYR SER THR LEU
SEQRES 18 A 307 GLU SER ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 A 307 LYS LEU LEU PHE THR GLY ASP PRO GLY ALA LEU VAL SER
SEQRES 20 A 307 PRO ALA PHE ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 A 307 CYS ARG LEU ILE ARG LEU GLY ALA GLY LEU HIS TYR LEU
SEQRES 22 A 307 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG THR VAL ALA
SEQRES 23 A 307 GLY TRP ILE ALA GLU ILE GLU ALA ALA SER ALA THR ALA
SEQRES 24 A 307 LYS ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 307 MET THR THR SER ALA ASP ILE SER LEU ARG HIS VAL SER
SEQRES 2 B 307 VAL LEU ASP SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 B 307 SER ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO LEU VAL
SEQRES 5 B 307 ALA PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 B 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 B 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP LYS
SEQRES 8 B 307 LEU GLY ILE GLU SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 B 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 B 307 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 B 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN THR PRO GLN
SEQRES 12 B 307 ALA ARG GLU MET PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 B 307 GLY GLU GLN MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 B 307 ARG VAL LEU PRO GLY SER ILE VAL ARG LYS LEU SER GLU
SEQRES 15 B 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 B 307 GLU SER ARG ARG PRO THR LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 B 307 PRO ILE ALA GLY GLU PRO ALA ASP VAL TYR SER THR LEU
SEQRES 18 B 307 GLU SER ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 B 307 LYS LEU LEU PHE THR GLY ASP PRO GLY ALA LEU VAL SER
SEQRES 20 B 307 PRO ALA PHE ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 B 307 CYS ARG LEU ILE ARG LEU GLY ALA GLY LEU HIS TYR LEU
SEQRES 22 B 307 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG THR VAL ALA
SEQRES 23 B 307 GLY TRP ILE ALA GLU ILE GLU ALA ALA SER ALA THR ALA
SEQRES 24 B 307 LYS ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 C 307 MET THR THR SER ALA ASP ILE SER LEU ARG HIS VAL SER
SEQRES 2 C 307 VAL LEU ASP SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 C 307 SER ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 C 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO LEU VAL
SEQRES 5 C 307 ALA PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 C 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 C 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP LYS
SEQRES 8 C 307 LEU GLY ILE GLU SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 C 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 C 307 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 C 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN THR PRO GLN
SEQRES 12 C 307 ALA ARG GLU MET PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 C 307 GLY GLU GLN MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 C 307 ARG VAL LEU PRO GLY SER ILE VAL ARG LYS LEU SER GLU
SEQRES 15 C 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 C 307 GLU SER ARG ARG PRO THR LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 C 307 PRO ILE ALA GLY GLU PRO ALA ASP VAL TYR SER THR LEU
SEQRES 18 C 307 GLU SER ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 C 307 LYS LEU LEU PHE THR GLY ASP PRO GLY ALA LEU VAL SER
SEQRES 20 C 307 PRO ALA PHE ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 C 307 CYS ARG LEU ILE ARG LEU GLY ALA GLY LEU HIS TYR LEU
SEQRES 22 C 307 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG THR VAL ALA
SEQRES 23 C 307 GLY TRP ILE ALA GLU ILE GLU ALA ALA SER ALA THR ALA
SEQRES 24 C 307 LYS ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 D 307 MET THR THR SER ALA ASP ILE SER LEU ARG HIS VAL SER
SEQRES 2 D 307 VAL LEU ASP SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 D 307 SER ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 D 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO LEU VAL
SEQRES 5 D 307 ALA PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 D 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 D 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP LYS
SEQRES 8 D 307 LEU GLY ILE GLU SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 D 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 D 307 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 D 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN THR PRO GLN
SEQRES 12 D 307 ALA ARG GLU MET PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 D 307 GLY GLU GLN MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 D 307 ARG VAL LEU PRO GLY SER ILE VAL ARG LYS LEU SER GLU
SEQRES 15 D 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 D 307 GLU SER ARG ARG PRO THR LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 D 307 PRO ILE ALA GLY GLU PRO ALA ASP VAL TYR SER THR LEU
SEQRES 18 D 307 GLU SER ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 D 307 LYS LEU LEU PHE THR GLY ASP PRO GLY ALA LEU VAL SER
SEQRES 20 D 307 PRO ALA PHE ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 D 307 CYS ARG LEU ILE ARG LEU GLY ALA GLY LEU HIS TYR LEU
SEQRES 22 D 307 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG THR VAL ALA
SEQRES 23 D 307 GLY TRP ILE ALA GLU ILE GLU ALA ALA SER ALA THR ALA
SEQRES 24 D 307 LYS ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 E 307 MET THR THR SER ALA ASP ILE SER LEU ARG HIS VAL SER
SEQRES 2 E 307 VAL LEU ASP SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 E 307 SER ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 E 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO LEU VAL
SEQRES 5 E 307 ALA PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 E 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 E 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP LYS
SEQRES 8 E 307 LEU GLY ILE GLU SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 E 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 E 307 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 E 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN THR PRO GLN
SEQRES 12 E 307 ALA ARG GLU MET PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 E 307 GLY GLU GLN MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 E 307 ARG VAL LEU PRO GLY SER ILE VAL ARG LYS LEU SER GLU
SEQRES 15 E 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 E 307 GLU SER ARG ARG PRO THR LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 E 307 PRO ILE ALA GLY GLU PRO ALA ASP VAL TYR SER THR LEU
SEQRES 18 E 307 GLU SER ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 E 307 LYS LEU LEU PHE THR GLY ASP PRO GLY ALA LEU VAL SER
SEQRES 20 E 307 PRO ALA PHE ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 E 307 CYS ARG LEU ILE ARG LEU GLY ALA GLY LEU HIS TYR LEU
SEQRES 22 E 307 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG THR VAL ALA
SEQRES 23 E 307 GLY TRP ILE ALA GLU ILE GLU ALA ALA SER ALA THR ALA
SEQRES 24 E 307 LYS ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 F 307 MET THR THR SER ALA ASP ILE SER LEU ARG HIS VAL SER
SEQRES 2 F 307 VAL LEU ASP SER THR MET ALA TYR ARG GLU THR GLY ARG
SEQRES 3 F 307 SER ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 F 307 THR SER SER TYR ILE TRP ARG ASN ILE ILE PRO LEU VAL
SEQRES 5 F 307 ALA PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 F 307 PHE GLY GLN SER GLY LYS PRO ASP ILE ASP TYR ARG PHE
SEQRES 7 F 307 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE ASP LYS
SEQRES 8 F 307 LEU GLY ILE GLU SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 F 307 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 F 307 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 F 307 PRO MET PRO THR TRP ASP ASP PHE HIS GLN THR PRO GLN
SEQRES 12 F 307 ALA ARG GLU MET PHE ARG LYS PHE ARG THR PRO GLY VAL
SEQRES 13 F 307 GLY GLU GLN MET ILE LEU GLU ASP ASN VAL PHE VAL GLU
SEQRES 14 F 307 ARG VAL LEU PRO GLY SER ILE VAL ARG LYS LEU SER GLU
SEQRES 15 F 307 GLU GLU MET ALA VAL TYR ARG ALA PRO PHE PRO THR PRO
SEQRES 16 F 307 GLU SER ARG ARG PRO THR LEU ARG PHE PRO ARG GLU LEU
SEQRES 17 F 307 PRO ILE ALA GLY GLU PRO ALA ASP VAL TYR SER THR LEU
SEQRES 18 F 307 GLU SER ALA HIS ALA ALA LEU ALA ALA SER THR TYR PRO
SEQRES 19 F 307 LYS LEU LEU PHE THR GLY ASP PRO GLY ALA LEU VAL SER
SEQRES 20 F 307 PRO ALA PHE ALA GLU ARG PHE ALA ALA ASN LEU LYS ASN
SEQRES 21 F 307 CYS ARG LEU ILE ARG LEU GLY ALA GLY LEU HIS TYR LEU
SEQRES 22 F 307 GLN GLU ASP HIS PRO GLU ALA ILE GLY ARG THR VAL ALA
SEQRES 23 F 307 GLY TRP ILE ALA GLU ILE GLU ALA ALA SER ALA THR ALA
SEQRES 24 F 307 LYS ALA HIS HIS HIS HIS HIS HIS
HET CL A 401 1
HET CL A 402 1
HET MPD A 403 8
HET TRS A 404 8
HET TRS A 405 8
HET TRS A 406 8
HET TRS A 407 8
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET EDO A 412 4
HET EDO A 413 4
HET EDO A 414 4
HET CL B 401 1
HET CL B 402 1
HET MPD B 403 8
HET TRS B 404 8
HET EDO B 405 4
HET EDO B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET EDO B 409 4
HET EDO B 410 4
HET EDO B 411 4
HET CL C 401 1
HET CL C 402 1
HET MPD C 403 8
HET MPD C 404 8
HET EDO C 405 4
HET EDO C 406 4
HET EDO C 407 4
HET EDO C 408 4
HET EDO C 409 4
HET EDO C 410 4
HET EDO C 411 4
HET CL D 401 1
HET CL D 402 1
HET MPD D 403 8
HET EDO D 404 4
HET EDO D 405 4
HET EDO D 406 4
HET CL E 401 1
HET CL E 402 1
HET EDO E 403 4
HET CL F 401 1
HET CL F 402 1
HET EDO F 403 4
HET EDO F 404 4
HET EDO F 405 4
HET EDO F 406 4
HET EDO F 407 4
HETNAM CL CHLORIDE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN TRS TRIS BUFFER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 CL 12(CL 1-)
FORMUL 9 MPD 5(C6 H14 O2)
FORMUL 10 TRS 5(C4 H12 N O3 1+)
FORMUL 14 EDO 30(C2 H6 O2)
FORMUL 59 HOH *1044(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 1 6
HELIX 3 AA3 PRO A 54 ALA A 56 5 3
HELIX 4 AA4 ARG A 77 LEU A 92 1 16
HELIX 5 AA5 ASP A 103 ARG A 116 1 14
HELIX 6 AA6 THR A 134 PHE A 138 5 5
HELIX 7 AA7 THR A 141 ARG A 152 1 12
HELIX 8 AA8 GLY A 155 LEU A 162 1 8
HELIX 9 AA9 ASN A 165 ARG A 170 1 6
HELIX 10 AB1 ARG A 170 SER A 175 1 6
HELIX 11 AB2 SER A 181 ALA A 190 1 10
HELIX 12 AB3 PRO A 195 SER A 197 5 3
HELIX 13 AB4 ARG A 198 LEU A 208 1 11
HELIX 14 AB5 PRO A 214 SER A 231 1 18
HELIX 15 AB6 SER A 247 LEU A 258 1 12
HELIX 16 AB7 TYR A 272 ASP A 276 5 5
HELIX 17 AB8 HIS A 277 ALA A 295 1 19
HELIX 18 AB9 SER B 41 ARG B 46 5 6
HELIX 19 AC1 ILE B 48 ALA B 53 1 6
HELIX 20 AC2 PRO B 54 ALA B 56 5 3
HELIX 21 AC3 ARG B 77 LEU B 92 1 16
HELIX 22 AC4 ASP B 103 ARG B 116 1 14
HELIX 23 AC5 THR B 134 PHE B 138 5 5
HELIX 24 AC6 THR B 141 ARG B 152 1 12
HELIX 25 AC7 GLY B 155 LEU B 162 1 8
HELIX 26 AC8 ASN B 165 ARG B 170 1 6
HELIX 27 AC9 ARG B 170 SER B 175 1 6
HELIX 28 AD1 SER B 181 ALA B 190 1 10
HELIX 29 AD2 PRO B 195 SER B 197 5 3
HELIX 30 AD3 ARG B 198 LEU B 208 1 11
HELIX 31 AD4 PRO B 214 SER B 231 1 18
HELIX 32 AD5 SER B 247 LEU B 258 1 12
HELIX 33 AD6 TYR B 272 ASP B 276 5 5
HELIX 34 AD7 HIS B 277 SER B 296 1 20
HELIX 35 AD8 SER C 41 ARG C 46 5 6
HELIX 36 AD9 ILE C 48 ALA C 53 1 6
HELIX 37 AE1 PRO C 54 ALA C 56 5 3
HELIX 38 AE2 ARG C 77 LEU C 92 1 16
HELIX 39 AE3 ASP C 103 ARG C 116 1 14
HELIX 40 AE4 THR C 134 PHE C 138 5 5
HELIX 41 AE5 THR C 141 ARG C 152 1 12
HELIX 42 AE6 GLY C 155 LEU C 162 1 8
HELIX 43 AE7 ASN C 165 ARG C 170 1 6
HELIX 44 AE8 ARG C 170 SER C 175 1 6
HELIX 45 AE9 SER C 181 ALA C 190 1 10
HELIX 46 AF1 PRO C 195 SER C 197 5 3
HELIX 47 AF2 ARG C 198 LEU C 208 1 11
HELIX 48 AF3 PRO C 214 SER C 231 1 18
HELIX 49 AF4 SER C 247 LEU C 258 1 12
HELIX 50 AF5 TYR C 272 ASP C 276 5 5
HELIX 51 AF6 HIS C 277 ALA C 295 1 19
HELIX 52 AF7 SER D 41 ARG D 46 5 6
HELIX 53 AF8 ILE D 48 ALA D 53 1 6
HELIX 54 AF9 ARG D 77 LEU D 92 1 16
HELIX 55 AG1 ASP D 103 ARG D 116 1 14
HELIX 56 AG2 THR D 134 PHE D 138 5 5
HELIX 57 AG3 THR D 141 ARG D 152 1 12
HELIX 58 AG4 GLY D 155 LEU D 162 1 8
HELIX 59 AG5 ASN D 165 ARG D 170 1 6
HELIX 60 AG6 ARG D 170 SER D 175 1 6
HELIX 61 AG7 SER D 181 ALA D 190 1 10
HELIX 62 AG8 PRO D 195 SER D 197 5 3
HELIX 63 AG9 ARG D 198 LEU D 208 1 11
HELIX 64 AH1 PRO D 214 SER D 231 1 18
HELIX 65 AH2 SER D 247 LEU D 258 1 12
HELIX 66 AH3 TYR D 272 ASP D 276 5 5
HELIX 67 AH4 HIS D 277 SER D 296 1 20
HELIX 68 AH5 SER E 41 ARG E 46 5 6
HELIX 69 AH6 ILE E 48 ALA E 53 1 6
HELIX 70 AH7 PRO E 54 ALA E 56 5 3
HELIX 71 AH8 ARG E 77 LEU E 92 1 16
HELIX 72 AH9 ASP E 103 ARG E 116 1 14
HELIX 73 AI1 THR E 134 PHE E 138 5 5
HELIX 74 AI2 THR E 141 ARG E 152 1 12
HELIX 75 AI3 GLY E 155 LEU E 162 1 8
HELIX 76 AI4 ASN E 165 ARG E 170 1 6
HELIX 77 AI5 ARG E 170 SER E 175 1 6
HELIX 78 AI6 SER E 181 ALA E 190 1 10
HELIX 79 AI7 PRO E 195 SER E 197 5 3
HELIX 80 AI8 ARG E 198 LEU E 208 1 11
HELIX 81 AI9 PRO E 214 SER E 231 1 18
HELIX 82 AJ1 SER E 247 LEU E 258 1 12
HELIX 83 AJ2 TYR E 272 HIS E 277 1 6
HELIX 84 AJ3 HIS E 277 ALA E 295 1 19
HELIX 85 AJ4 SER F 41 ARG F 46 5 6
HELIX 86 AJ5 ILE F 48 ALA F 53 1 6
HELIX 87 AJ6 PRO F 54 ALA F 56 5 3
HELIX 88 AJ7 ARG F 77 LEU F 92 1 16
HELIX 89 AJ8 ASP F 103 ARG F 116 1 14
HELIX 90 AJ9 THR F 134 PHE F 138 5 5
HELIX 91 AK1 THR F 141 ARG F 152 1 12
HELIX 92 AK2 GLY F 155 LEU F 162 1 8
HELIX 93 AK3 ASN F 165 ARG F 170 1 6
HELIX 94 AK4 ARG F 170 SER F 175 1 6
HELIX 95 AK5 SER F 181 ALA F 190 1 10
HELIX 96 AK6 PRO F 195 SER F 197 5 3
HELIX 97 AK7 ARG F 198 LEU F 208 1 11
HELIX 98 AK8 PRO F 214 SER F 231 1 18
HELIX 99 AK9 SER F 247 ASN F 257 1 11
HELIX 100 AL1 TYR F 272 ASP F 276 5 5
HELIX 101 AL2 HIS F 277 ALA F 294 1 18
SHEET 1 AA1 8 SER A 8 VAL A 14 0
SHEET 2 AA1 8 SER A 17 THR A 24 -1 O SER A 17 N VAL A 14
SHEET 3 AA1 8 HIS A 57 PRO A 61 -1 O ALA A 60 N ARG A 22
SHEET 4 AA1 8 VAL A 31 LEU A 35 1 N VAL A 32 O ILE A 59
SHEET 5 AA1 8 ALA A 97 GLN A 102 1 O TYR A 98 N LEU A 33
SHEET 6 AA1 8 VAL A 120 MET A 126 1 O ALA A 124 N LEU A 99
SHEET 7 AA1 8 LYS A 235 PRO A 242 1 O LEU A 236 N PHE A 125
SHEET 8 AA1 8 CYS A 261 GLY A 269 1 O ILE A 264 N LEU A 237
SHEET 1 AA2 8 SER B 8 VAL B 14 0
SHEET 2 AA2 8 SER B 17 THR B 24 -1 O TYR B 21 N ARG B 10
SHEET 3 AA2 8 HIS B 57 PRO B 61 -1 O ALA B 60 N ARG B 22
SHEET 4 AA2 8 VAL B 31 LEU B 35 1 N VAL B 32 O ILE B 59
SHEET 5 AA2 8 ALA B 97 GLN B 102 1 O TYR B 98 N LEU B 33
SHEET 6 AA2 8 VAL B 120 MET B 126 1 O ALA B 124 N LEU B 99
SHEET 7 AA2 8 LYS B 235 PRO B 242 1 O LEU B 236 N PHE B 125
SHEET 8 AA2 8 CYS B 261 GLY B 269 1 O LEU B 266 N THR B 239
SHEET 1 AA3 8 SER C 8 VAL C 14 0
SHEET 2 AA3 8 SER C 17 THR C 24 -1 O TYR C 21 N ARG C 10
SHEET 3 AA3 8 HIS C 57 PRO C 61 -1 O ALA C 60 N ARG C 22
SHEET 4 AA3 8 VAL C 31 LEU C 35 1 N VAL C 32 O ILE C 59
SHEET 5 AA3 8 ALA C 97 GLN C 102 1 O TYR C 98 N LEU C 33
SHEET 6 AA3 8 VAL C 120 MET C 126 1 O ALA C 124 N LEU C 99
SHEET 7 AA3 8 LYS C 235 PRO C 242 1 O LEU C 236 N PHE C 125
SHEET 8 AA3 8 CYS C 261 GLY C 269 1 O ARG C 262 N LEU C 237
SHEET 1 AA4 8 SER D 8 VAL D 14 0
SHEET 2 AA4 8 SER D 17 THR D 24 -1 O TYR D 21 N ARG D 10
SHEET 3 AA4 8 HIS D 57 PRO D 61 -1 O ALA D 60 N ARG D 22
SHEET 4 AA4 8 VAL D 31 LEU D 35 1 N VAL D 32 O ILE D 59
SHEET 5 AA4 8 ALA D 97 GLN D 102 1 O TYR D 98 N LEU D 33
SHEET 6 AA4 8 VAL D 120 MET D 126 1 O ALA D 124 N LEU D 99
SHEET 7 AA4 8 LYS D 235 PRO D 242 1 O LEU D 236 N PHE D 125
SHEET 8 AA4 8 CYS D 261 GLY D 269 1 O LEU D 266 N THR D 239
SHEET 1 AA5 8 ARG E 10 VAL E 14 0
SHEET 2 AA5 8 SER E 17 THR E 24 -1 O TYR E 21 N ARG E 10
SHEET 3 AA5 8 HIS E 57 PRO E 61 -1 O ALA E 60 N ARG E 22
SHEET 4 AA5 8 VAL E 31 LEU E 35 1 N VAL E 32 O ILE E 59
SHEET 5 AA5 8 ALA E 97 GLN E 102 1 O TYR E 98 N LEU E 33
SHEET 6 AA5 8 VAL E 120 MET E 126 1 O ALA E 124 N LEU E 99
SHEET 7 AA5 8 LYS E 235 PRO E 242 1 O LEU E 236 N PHE E 125
SHEET 8 AA5 8 CYS E 261 GLY E 269 1 O LEU E 266 N THR E 239
SHEET 1 AA6 8 SER F 8 VAL F 14 0
SHEET 2 AA6 8 SER F 17 THR F 24 -1 O TYR F 21 N ARG F 10
SHEET 3 AA6 8 HIS F 57 PRO F 61 -1 O ALA F 60 N ARG F 22
SHEET 4 AA6 8 VAL F 31 LEU F 35 1 N VAL F 32 O ILE F 59
SHEET 5 AA6 8 ALA F 97 GLN F 102 1 O TYR F 98 N LEU F 33
SHEET 6 AA6 8 VAL F 120 MET F 126 1 O ALA F 124 N LEU F 99
SHEET 7 AA6 8 LYS F 235 PRO F 242 1 O LEU F 236 N PHE F 125
SHEET 8 AA6 8 CYS F 261 GLY F 269 1 O ILE F 264 N LEU F 237
CISPEP 1 ASN A 38 PRO A 39 0 -1.24
CISPEP 2 GLU A 213 PRO A 214 0 -7.33
CISPEP 3 ASP A 241 PRO A 242 0 7.01
CISPEP 4 ASN B 38 PRO B 39 0 -1.68
CISPEP 5 GLU B 213 PRO B 214 0 -6.84
CISPEP 6 ASP B 241 PRO B 242 0 6.45
CISPEP 7 ASN C 38 PRO C 39 0 -6.93
CISPEP 8 GLU C 213 PRO C 214 0 -4.07
CISPEP 9 ASP C 241 PRO C 242 0 7.89
CISPEP 10 ASN D 38 PRO D 39 0 -4.83
CISPEP 11 GLU D 213 PRO D 214 0 -6.14
CISPEP 12 ASP D 241 PRO D 242 0 7.31
CISPEP 13 ASN E 38 PRO E 39 0 -1.57
CISPEP 14 GLU E 213 PRO E 214 0 -8.63
CISPEP 15 ASP E 241 PRO E 242 0 5.68
CISPEP 16 ASN F 38 PRO F 39 0 -3.62
CISPEP 17 GLU F 213 PRO F 214 0 -6.63
CISPEP 18 ASP F 241 PRO F 242 0 4.97
SITE 1 AC1 6 ASN A 38 TRP A 104 PHE A 167 PHE A 204
SITE 2 AC1 6 PRO A 205 HOH A 565
SITE 1 AC2 4 GLY A 37 THR A 40 GLN A 102 GLN A 274
SITE 1 AC3 6 ARG A 130 ASP A 137 HIS A 139 GLN A 140
SITE 2 AC3 6 LEU A 245 SER A 247
SITE 1 AC4 3 GLU A 183 PRO B 195 GLU B 196
SITE 1 AC5 3 ASP A 86 ASP A 90 ARG A 116
SITE 1 AC6 7 PRO A 117 ASP A 118 VAL A 120 THR A 232
SITE 2 AC6 7 TYR A 233 HOH A 503 GLU B 95
SITE 1 AC7 3 PRO A 195 GLU A 196 GLU B 183
SITE 1 AC8 3 ASP A 16 PRO A 72 ASP A 73
SITE 1 AC9 4 LYS A 71 PRO A 72 GLU A 196 HOH A 505
SITE 1 AD1 3 MET A 147 SER A 175 HOH A 571
SITE 1 AD2 1 ARG A 170
SITE 1 AD3 3 HOH A 506 HOH A 637 ARG C 262
SITE 1 AD4 2 ILE A 7 ARG A 22
SITE 1 AD5 1 ARG A 262
SITE 1 AD6 4 GLY B 37 THR B 40 GLN B 102 GLN B 274
SITE 1 AD7 5 ASN B 38 TRP B 104 PHE B 167 PHE B 204
SITE 2 AD7 5 PRO B 205
SITE 1 AD8 3 ARG B 152 ARG B 206 GLU B 213
SITE 1 AD9 8 ARG B 130 ASP B 137 HIS B 139 GLN B 140
SITE 2 AD9 8 ALA B 244 LEU B 245 PHE B 250 HOH B 512
SITE 1 AE1 1 HOH B 549
SITE 1 AE2 5 THR A 194 HOH A 501 ARG B 22 GLN B 68
SITE 2 AE2 5 HOH B 521
SITE 1 AE3 1 PHE B 250
SITE 1 AE4 3 GLU B 291 HOH B 537 HOH B 552
SITE 1 AE5 5 PRO B 117 VAL B 120 THR B 232 TYR B 233
SITE 2 AE5 5 HOH B 590
SITE 1 AE6 2 LEU B 92 HOH B 525
SITE 1 AE7 7 ARG A 189 GLU B 182 ALA B 186 HOH B 502
SITE 2 AE7 7 HOH B 516 HOH B 518 HOH B 667
SITE 1 AE8 4 ASN C 38 TRP C 104 PRO C 205 HOH C 538
SITE 1 AE9 4 GLY C 37 THR C 40 GLN C 102 GLN C 274
SITE 1 AF1 6 GLY B 212 SER B 219 ILE C 74 ASP C 80
SITE 2 AF1 6 ARG C 83 TYR C 84
SITE 1 AF2 4 ALA C 144 MET C 147 HOH C 524 HOH C 627
SITE 1 AF3 3 ARG C 152 ARG C 206 HOH C 637
SITE 1 AF4 2 LEU C 92 HOH C 543
SITE 1 AF5 3 ALA C 114 SER C 223 HOH C 502
SITE 1 AF6 4 THR B 134 ASP B 137 HOH B 526 ASP C 90
SITE 1 AF7 3 GLU C 196 GLU E 183 HOH E 512
SITE 1 AF8 4 LEU C 162 ARG C 199 HOH C 510 HOH C 600
SITE 1 AF9 5 HIS C 277 PRO C 278 GLU C 279 ALA C 280
SITE 2 AF9 5 HOH C 523
SITE 1 AG1 6 ASN D 38 TRP D 104 PHE D 167 PHE D 204
SITE 2 AG1 6 PRO D 205 HOH D 535
SITE 1 AG2 4 GLY D 37 THR D 40 GLN D 102 GLN D 274
SITE 1 AG3 8 GLY A 212 ALA A 215 SER A 219 ASP D 16
SITE 2 AG3 8 ILE D 74 ASP D 80 ARG D 83 TYR D 84
SITE 1 AG4 6 LEU D 9 HIS D 11 GLN D 68 GLY F 70
SITE 2 AG4 6 LYS F 71 HOH F 549
SITE 1 AG5 4 ARG D 22 GLN D 68 HOH D 637 LYS F 71
SITE 1 AG6 1 ALA D 144
SITE 1 AG7 5 ASN E 38 TRP E 104 PHE E 167 PHE E 204
SITE 2 AG7 5 PRO E 205
SITE 1 AG8 4 GLY E 37 THR E 40 GLN E 102 GLN E 274
SITE 1 AG9 1 MET E 147
SITE 1 AH1 5 ASN F 38 TRP F 104 PHE F 204 PRO F 205
SITE 2 AH1 5 HOH F 553
SITE 1 AH2 4 GLY F 37 THR F 40 GLN F 102 GLN F 274
SITE 1 AH3 2 MET F 147 HOH F 544
SITE 1 AH4 1 LEU F 92
SITE 1 AH5 6 ARG F 199 LEU F 202 ARG F 203 ARG F 206
SITE 2 AH5 6 HOH F 510 HOH F 563
SITE 1 AH6 3 GLU E 222 ASP F 86 HOH F 589
SITE 1 AH7 4 ALA F 87 ASP F 90 HOH F 517 HOH F 519
CRYST1 109.580 166.620 100.290 90.00 90.00 90.00 P 21 21 2 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 0.009126 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009971 0.00000
TER 2300 SER A 296
TER 4618 SER B 296
TER 6932 SER C 296
TER 9281 ALA D 297
TER 11570 ALA E 295
TER 13875 ALA F 295
MASTER 654 0 52 101 48 0 68 615013 6 200 144
END |