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HEADER HYDROLASE 15-DEC-17 5YZO
TITLE CRYSTAL STRUCTURE OF S9 PEPTIDASE MUTANT (S514A) FROM DEINOCOCCUS
TITLE 2 RADIODURANS R1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PEPTIDE HYDROLASE, PUTATIVE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: S9 PROLYL OLIGOPEPTIDASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS (STRAIN ATCC 13939 /
SOURCE 3 DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 /
SOURCE 4 VKM B-1422);
SOURCE 5 ORGANISM_TAXID: 243230;
SOURCE 6 STRAIN: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
SOURCE 7 NCIMB 9279 / R1 / VKM B-1422;
SOURCE 8 GENE: DR_0165;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PST50TR
KEYWDS SERINE PEPTIDASE, MEROPS S9, POP FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.YADAV,S.N.JAMDAR,A.KUMAR,B.GHOSH,R.D.MAKDE
REVDAT 1 14-NOV-18 5YZO 0
JRNL AUTH P.YADAV,S.N.JAMDAR,A.KUMAR,B.GHOSH,S.M.GOKHALE,R.D.MAKDE
JRNL TITL CRYSTAL STRUCTURE OF S9C PEPTIDASE (S154A) MUTANT FROM
JRNL TITL 2 DEINOCOCCUS RADIODURANS R1
JRNL REF J.BIOL.CHEM. 2018
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 37.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 356416
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 17744
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 37.8076 - 5.2777 0.99 11401 586 0.1555 0.1642
REMARK 3 2 5.2777 - 4.1908 1.00 11375 589 0.1245 0.1386
REMARK 3 3 4.1908 - 3.6615 1.00 11227 619 0.1355 0.1524
REMARK 3 4 3.6615 - 3.3270 1.00 11307 585 0.1445 0.1675
REMARK 3 5 3.3270 - 3.0886 1.00 11294 587 0.1499 0.1677
REMARK 3 6 3.0886 - 2.9066 1.00 11309 594 0.1508 0.1765
REMARK 3 7 2.9066 - 2.7611 1.00 11303 583 0.1565 0.1824
REMARK 3 8 2.7611 - 2.6409 1.00 11320 577 0.1608 0.1811
REMARK 3 9 2.6409 - 2.5393 1.00 11274 613 0.1685 0.2110
REMARK 3 10 2.5393 - 2.4517 1.00 11307 558 0.1649 0.2007
REMARK 3 11 2.4517 - 2.3750 1.00 11275 616 0.1708 0.2054
REMARK 3 12 2.3750 - 2.3072 1.00 11246 589 0.1751 0.2123
REMARK 3 13 2.3072 - 2.2464 1.00 11289 604 0.1854 0.2187
REMARK 3 14 2.2464 - 2.1916 1.00 11294 609 0.1817 0.2121
REMARK 3 15 2.1916 - 2.1418 1.00 11186 591 0.1782 0.1982
REMARK 3 16 2.1418 - 2.0962 1.00 11262 621 0.1854 0.2171
REMARK 3 17 2.0962 - 2.0543 1.00 11386 580 0.1901 0.2163
REMARK 3 18 2.0543 - 2.0155 1.00 11271 598 0.1941 0.2351
REMARK 3 19 2.0155 - 1.9795 1.00 11242 574 0.1991 0.2467
REMARK 3 20 1.9795 - 1.9460 1.00 11343 583 0.2120 0.2474
REMARK 3 21 1.9460 - 1.9146 1.00 11271 597 0.2243 0.2689
REMARK 3 22 1.9146 - 1.8851 1.00 11187 612 0.2200 0.2460
REMARK 3 23 1.8851 - 1.8574 1.00 11349 595 0.2201 0.2531
REMARK 3 24 1.8574 - 1.8313 1.00 11245 583 0.2165 0.2472
REMARK 3 25 1.8313 - 1.8065 1.00 11314 566 0.2204 0.2584
REMARK 3 26 1.8065 - 1.7831 1.00 11289 571 0.2336 0.2667
REMARK 3 27 1.7831 - 1.7608 1.00 11260 590 0.2319 0.2648
REMARK 3 28 1.7608 - 1.7395 1.00 11313 551 0.2422 0.2780
REMARK 3 29 1.7395 - 1.7193 1.00 11254 621 0.2581 0.3116
REMARK 3 30 1.7193 - 1.7000 1.00 11279 602 0.2657 0.3129
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.007 20908
REMARK 3 ANGLE : 0.892 28512
REMARK 3 CHIRALITY : 0.056 2937
REMARK 3 PLANARITY : 0.007 3812
REMARK 3 DIHEDRAL : 13.190 12130
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1189 -46.8818 -32.1251
REMARK 3 T TENSOR
REMARK 3 T11: 0.1602 T22: 0.1820
REMARK 3 T33: 0.1606 T12: 0.0050
REMARK 3 T13: -0.0126 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.0232 L22: 0.2267
REMARK 3 L33: 0.0837 L12: 0.0177
REMARK 3 L13: -0.0218 L23: -0.0498
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: -0.0125 S13: 0.0057
REMARK 3 S21: 0.0289 S22: 0.0042 S23: 0.0275
REMARK 3 S31: -0.0077 S32: -0.0034 S33: -0.0115
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 5YZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1300005996.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5-5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : RRCAT INDUS-2
REMARK 200 BEAMLINE : PX-BL21
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97947
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 356745
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4000
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) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.91400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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: 5YZN
REMARK 200
REMARK 200 REMARK: PARALLELEPIPED, SIZE 200-300 MICRONS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40MM POTASSIUM PHOSPHATE, 20% PEG
REMARK 280 8000, 20% GLYCEROL, PH 5.3, MICROBATCH, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 95.00750
REMARK 290 SMTRY3 2 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 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 GLY A 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 THR A 6
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 THR B 6
REMARK 465 ALA B 236
REMARK 465 ASP B 237
REMARK 465 ALA B 238
REMARK 465 PRO B 239
REMARK 465 ALA B 240
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 ASN C 3
REMARK 465 SER C 4
REMARK 465 GLU C 5
REMARK 465 THR C 6
REMARK 465 PRO C 7
REMARK 465 ALA C 236
REMARK 465 ASP C 237
REMARK 465 ALA C 238
REMARK 465 PRO C 239
REMARK 465 ALA C 240
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 ASN D 2
REMARK 465 ASN D 3
REMARK 465 SER D 4
REMARK 465 GLU D 5
REMARK 465 THR D 6
REMARK 465 PRO D 7
REMARK 465 ALA D 236
REMARK 465 ASP D 237
REMARK 465 ALA D 238
REMARK 465 PRO D 239
REMARK 465 ALA D 240
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 LYS A 46 CG CD CE NZ
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 ARG A 174 NE CZ NH1 NH2
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 ASP A 237 CG OD1 OD2
REMARK 470 GLU A 400 CD OE1 OE2
REMARK 470 GLN A 402 CG CD OE1 NE2
REMARK 470 LYS B 46 CG CD CE NZ
REMARK 470 LYS B 49 CG CD CE NZ
REMARK 470 GLU B 100 CG CD OE1 OE2
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 GLN B 243 CG CD OE1 NE2
REMARK 470 LYS B 273 CG CD CE NZ
REMARK 470 LYS B 347 CG CD CE NZ
REMARK 470 GLU B 400 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 LYS C 30 CD CE NZ
REMARK 470 LYS C 46 CG CD CE NZ
REMARK 470 GLU C 100 CG CD OE1 OE2
REMARK 470 ARG C 135 NE CZ NH1 NH2
REMARK 470 GLN C 243 CG CD OE1 NE2
REMARK 470 LYS D 30 CD CE NZ
REMARK 470 LYS D 46 CG CD CE NZ
REMARK 470 LYS D 49 CG CD CE NZ
REMARK 470 GLU D 64 CG CD OE1 OE2
REMARK 470 GLU D 100 CG CD OE1 OE2
REMARK 470 ARG D 135 CZ NH1 NH2
REMARK 470 ARG D 174 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 GLN D 243 CG CD OE1 NE2
REMARK 470 GLU D 423 CG CD OE1 OE2
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 103 78.81 -172.55
REMARK 500 ALA A 143 -121.95 60.48
REMARK 500 ASP A 169 -122.66 61.27
REMARK 500 ARG A 480 43.86 -147.94
REMARK 500 THR A 483 -98.00 -110.44
REMARK 500 ALA A 514 -119.06 69.17
REMARK 500 ARG A 537 53.73 37.72
REMARK 500 ARG A 554 -17.49 -141.11
REMARK 500 GLU A 626 -33.65 71.63
REMARK 500 SER A 634 16.13 -156.24
REMARK 500 ALA B 103 77.69 -172.44
REMARK 500 ALA B 143 -122.17 60.79
REMARK 500 ASP B 169 -122.58 61.36
REMARK 500 SER B 250 -170.00 -163.54
REMARK 500 LYS B 273 -90.16 -65.03
REMARK 500 ASP B 297 58.82 -90.61
REMARK 500 ARG B 480 43.45 -147.55
REMARK 500 THR B 483 -98.91 -108.43
REMARK 500 ALA B 514 -118.30 68.67
REMARK 500 ARG B 537 54.59 38.39
REMARK 500 ARG B 554 -17.70 -140.25
REMARK 500 GLU B 626 -33.35 73.20
REMARK 500 SER B 634 17.39 -155.78
REMARK 500 ALA C 103 79.36 -172.14
REMARK 500 ALA C 143 -120.99 61.02
REMARK 500 ASP C 169 -120.63 61.73
REMARK 500 ASP C 293 57.07 -91.90
REMARK 500 ARG C 480 44.80 -147.39
REMARK 500 THR C 483 -98.66 -107.82
REMARK 500 ALA C 514 -117.46 68.81
REMARK 500 ARG C 537 54.03 37.98
REMARK 500 GLU C 626 -32.83 73.59
REMARK 500 ASN C 628 -161.73 -129.64
REMARK 500 SER C 634 16.57 -156.51
REMARK 500 ALA D 103 79.38 -171.00
REMARK 500 ALA D 143 -121.43 61.08
REMARK 500 ASP D 169 -121.50 61.57
REMARK 500 ASP D 293 57.57 -92.13
REMARK 500 ARG D 480 45.02 -147.82
REMARK 500 THR D 483 -99.08 -108.31
REMARK 500 ALA D 514 -117.80 67.36
REMARK 500 ARG D 537 55.17 36.00
REMARK 500 GLU D 626 -33.63 72.15
REMARK 500 SER D 634 17.14 -155.92
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 A1649 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1650 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A1651 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A1652 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A1653 DISTANCE = 8.29 ANGSTROMS
REMARK 525 HOH B1615 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B1616 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B1617 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH B1618 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B1619 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH B1620 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH C1593 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C1594 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH C1595 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH C1596 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH C1597 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH D1543 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH D1544 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH D1545 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH D1546 DISTANCE = 6.96 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS D 702
DBREF 5YZO A 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 5YZO B 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 5YZO C 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 5YZO D 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
SEQADV 5YZO GLY A 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO SER A 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO ALA A 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQADV 5YZO GLY B 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO SER B 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO ALA B 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQADV 5YZO GLY C 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO SER C 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO ALA C 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQADV 5YZO GLY D 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO SER D 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 5YZO ALA D 514 UNP Q9RXY9 SER 514 ENGINEERED MUTATION
SEQRES 1 A 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 A 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 A 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 A 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 A 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 A 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 A 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 A 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 A 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 A 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 A 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 A 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 A 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 A 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 A 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 A 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 A 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 A 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 A 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 A 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 A 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 A 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 A 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 A 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 A 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 A 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 A 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 A 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 A 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 A 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 A 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 A 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 A 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 A 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 A 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 A 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 A 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 A 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 A 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 A 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 A 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 A 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 A 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 A 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 A 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 A 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 A 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 A 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 A 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 A 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 A 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 B 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 B 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 B 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 B 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 B 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 B 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 B 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 B 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 B 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 B 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 B 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 B 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 B 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 B 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 B 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 B 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 B 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 B 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 B 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 B 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 B 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 B 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 B 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 B 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 B 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 B 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 B 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 B 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 B 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 B 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 B 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 B 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 B 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 B 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 B 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 B 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 B 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 B 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 B 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 B 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 B 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 B 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 B 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 B 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 B 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 B 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 B 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 B 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 B 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 B 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 B 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 C 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 C 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 C 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 C 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 C 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 C 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 C 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 C 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 C 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 C 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 C 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 C 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 C 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 C 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 C 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 C 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 C 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 C 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 C 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 C 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 C 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 C 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 C 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 C 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 C 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 C 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 C 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 C 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 C 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 C 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 C 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 C 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 C 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 C 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 C 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 C 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 C 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 C 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 C 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 C 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 C 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 C 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 C 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 C 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 C 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 C 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 C 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 C 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 C 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 C 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 C 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 D 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 D 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 D 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 D 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 D 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 D 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 D 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 D 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 D 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 D 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 D 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 D 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 D 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 D 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 D 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 D 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 D 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 D 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 D 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 D 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 D 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 D 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 D 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 D 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 D 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 D 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 D 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 D 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 D 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 D 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 D 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 D 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 D 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 D 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 D 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 D 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 D 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 D 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 D 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 D 656 LYS THR ALA VAL MET GLY GLY ALA TYR GLY GLY PHE MET
SEQRES 41 D 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 D 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 D 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 D 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 D 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 D 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 D 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 D 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 D 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 D 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 D 656 TRP LEU GLU ARG TRP LEU
HET DMS A 701 10
HET DMS A 702 10
HET DMS A 703 10
HET GOL A 704 6
HET GOL A 705 6
HET DMS B 701 10
HET DMS B 702 10
HET GOL B 703 14
HET GOL B 704 6
HET DMS C 701 10
HET DMS C 702 10
HET GOL C 703 6
HET GOL C 704 6
HET DMS D 701 10
HET DMS D 702 10
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 DMS 9(C2 H6 O S)
FORMUL 8 GOL 6(C3 H8 O3)
FORMUL 20 HOH *3216(H2 O)
HELIX 1 AA1 GLY A 10 LEU A 17 5 8
HELIX 2 AA2 LYS A 148 GLY A 153 1 6
HELIX 3 AA3 ASP A 217 GLN A 223 1 7
HELIX 4 AA4 LEU A 390 PHE A 394 5 5
HELIX 5 AA5 THR A 445 ARG A 454 1 10
HELIX 6 AA6 GLY A 470 ALA A 476 1 7
HELIX 7 AA7 THR A 483 VAL A 500 1 18
HELIX 8 AA8 ALA A 514 GLY A 525 1 12
HELIX 9 AA9 ASN A 541 SER A 549 1 9
HELIX 10 AB1 ARG A 554 GLY A 561 1 8
HELIX 11 AB2 ARG A 566 LEU A 576 1 11
HELIX 12 AB3 SER A 577 VAL A 585 5 9
HELIX 13 AB4 VAL A 602 HIS A 615 1 14
HELIX 14 AB5 GLU A 630 GLY A 635 1 6
HELIX 15 AB6 ARG A 636 LEU A 655 1 20
HELIX 16 AB7 GLY B 10 LEU B 17 5 8
HELIX 17 AB8 LYS B 148 GLY B 153 1 6
HELIX 18 AB9 ASP B 217 GLN B 223 1 7
HELIX 19 AC1 LEU B 390 PHE B 394 5 5
HELIX 20 AC2 THR B 445 ARG B 454 1 10
HELIX 21 AC3 GLY B 470 ALA B 476 1 7
HELIX 22 AC4 THR B 483 VAL B 500 1 18
HELIX 23 AC5 ALA B 514 GLY B 525 1 12
HELIX 24 AC6 ASN B 541 SER B 549 1 9
HELIX 25 AC7 ARG B 554 GLY B 561 1 8
HELIX 26 AC8 ARG B 566 LEU B 576 1 11
HELIX 27 AC9 SER B 577 VAL B 585 5 9
HELIX 28 AD1 VAL B 602 HIS B 615 1 14
HELIX 29 AD2 GLU B 630 GLY B 635 1 6
HELIX 30 AD3 ARG B 636 LEU B 655 1 20
HELIX 31 AD4 GLY C 10 LEU C 17 5 8
HELIX 32 AD5 LYS C 148 GLY C 153 1 6
HELIX 33 AD6 ASP C 217 GLN C 223 1 7
HELIX 34 AD7 LEU C 390 PHE C 394 5 5
HELIX 35 AD8 THR C 445 ARG C 454 1 10
HELIX 36 AD9 GLY C 470 ALA C 476 1 7
HELIX 37 AE1 THR C 483 VAL C 500 1 18
HELIX 38 AE2 ALA C 514 GLY C 525 1 12
HELIX 39 AE3 ASN C 541 SER C 549 1 9
HELIX 40 AE4 ARG C 554 GLY C 561 1 8
HELIX 41 AE5 ARG C 566 LEU C 576 1 11
HELIX 42 AE6 SER C 577 VAL C 585 5 9
HELIX 43 AE7 VAL C 602 HIS C 615 1 14
HELIX 44 AE8 GLU C 630 GLY C 635 1 6
HELIX 45 AE9 ARG C 636 LEU C 655 1 20
HELIX 46 AF1 GLY D 10 LEU D 17 5 8
HELIX 47 AF2 LYS D 148 GLY D 153 1 6
HELIX 48 AF3 ASP D 217 GLN D 223 1 7
HELIX 49 AF4 LEU D 390 PHE D 394 5 5
HELIX 50 AF5 THR D 445 ARG D 454 1 10
HELIX 51 AF6 GLY D 470 ALA D 476 1 7
HELIX 52 AF7 THR D 483 VAL D 500 1 18
HELIX 53 AF8 ALA D 514 GLY D 525 1 12
HELIX 54 AF9 ASN D 541 SER D 549 1 9
HELIX 55 AG1 ARG D 554 GLY D 561 1 8
HELIX 56 AG2 ARG D 566 LEU D 576 1 11
HELIX 57 AG3 SER D 577 VAL D 585 5 9
HELIX 58 AG4 VAL D 602 HIS D 615 1 14
HELIX 59 AG5 GLU D 630 GLY D 635 1 6
HELIX 60 AG6 ARG D 636 LEU D 655 1 20
SHEET 1 AA1 4 PHE A 19 VAL A 25 0
SHEET 2 AA1 4 VAL A 32 GLU A 41 -1 O ALA A 33 N GLN A 24
SHEET 3 AA1 4 PRO A 54 SER A 63 -1 O ARG A 55 N SER A 40
SHEET 4 AA1 4 ARG A 69 PRO A 70 -1 O ARG A 69 N LEU A 62
SHEET 1 AA2 4 GLY A 79 TRP A 85 0
SHEET 2 AA2 4 ASN A 91 ALA A 98 -1 O ALA A 93 N ARG A 84
SHEET 3 AA2 4 VAL A 101 PRO A 109 -1 O LEU A 108 N LEU A 92
SHEET 4 AA2 4 ARG A 116 ARG A 117 -1 O ARG A 116 N LEU A 107
SHEET 1 AA3 4 SER A 126 TRP A 130 0
SHEET 2 AA3 4 PHE A 136 THR A 141 -1 O ALA A 138 N GLN A 129
SHEET 3 AA3 4 ALA A 177 ASP A 182 -1 O TRP A 179 N PHE A 139
SHEET 4 AA3 4 LYS A 187 TYR A 192 -1 O LYS A 187 N ASP A 182
SHEET 1 AA4 9 ARG A 156 LEU A 158 0
SHEET 2 AA4 9 VAL D 619 PHE D 624 -1 O PHE D 621 N LEU A 158
SHEET 3 AA4 9 THR D 589 SER D 594 1 N ILE D 591 O ARG D 620
SHEET 4 AA4 9 ALA D 532 ASP D 536 1 N THR D 535 O LEU D 590
SHEET 5 AA4 9 LEU D 503 GLY D 513 1 N GLY D 512 O ASP D 536
SHEET 6 AA4 9 VAL D 426 ILE D 432 1 N LEU D 430 O ALA D 509
SHEET 7 AA4 9 GLY D 457 SER D 461 1 O GLY D 457 N LEU D 429
SHEET 8 AA4 9 GLY D 411 LEU D 418 -1 N TRP D 416 O TYR D 460
SHEET 9 AA4 9 GLN D 402 THR D 408 -1 N PHE D 406 O GLY D 413
SHEET 1 AA5 2 ARG A 164 ALA A 165 0
SHEET 2 AA5 2 ASP A 169 TRP A 170 -1 O ASP A 169 N ALA A 165
SHEET 1 AA6 4 LEU A 201 TRP A 203 0
SHEET 2 AA6 4 GLY A 209 GLN A 214 -1 O LEU A 211 N SER A 202
SHEET 3 AA6 4 GLN A 226 PRO A 232 -1 O TYR A 229 N ILE A 212
SHEET 4 AA6 4 GLN A 243 SER A 250 -1 O LEU A 245 N VAL A 228
SHEET 1 AA7 4 ALA A 252 PRO A 257 0
SHEET 2 AA7 4 PHE A 264 GLY A 268 -1 O ILE A 267 N HIS A 253
SHEET 3 AA7 4 HIS A 280 GLU A 285 -1 O ILE A 284 N PHE A 264
SHEET 4 AA7 4 GLN A 288 ARG A 291 -1 O ARG A 290 N LEU A 283
SHEET 1 AA8 4 ARG A 318 TRP A 319 0
SHEET 2 AA8 4 THR A 324 VAL A 331 -1 O LEU A 326 N ARG A 318
SHEET 3 AA8 4 SER A 334 HIS A 341 -1 O ALA A 340 N LEU A 325
SHEET 4 AA8 4 GLY A 344 ASP A 350 -1 O ASP A 350 N LEU A 337
SHEET 1 AA9 4 GLY A 355 ALA A 362 0
SHEET 2 AA9 4 VAL A 367 SER A 373 -1 O GLU A 372 N VAL A 356
SHEET 3 AA9 4 ARG A 376 LEU A 382 -1 O GLU A 381 N LEU A 369
SHEET 4 AA9 4 GLN A 385 ARG A 386 -1 O GLN A 385 N LEU A 382
SHEET 1 AB1 9 GLN A 402 PHE A 406 0
SHEET 2 AB1 9 GLY A 413 LEU A 418 -1 O GLY A 413 N PHE A 406
SHEET 3 AB1 9 GLY A 457 SER A 461 -1 O TYR A 460 N TRP A 416
SHEET 4 AB1 9 VAL A 426 ILE A 432 1 N LEU A 429 O CYS A 459
SHEET 5 AB1 9 LEU A 503 GLY A 513 1 O ALA A 509 N LEU A 430
SHEET 6 AB1 9 ALA A 532 ASP A 536 1 O ASP A 536 N GLY A 512
SHEET 7 AB1 9 THR A 589 SER A 594 1 O LEU A 590 N THR A 535
SHEET 8 AB1 9 VAL A 619 PHE A 624 1 O ARG A 620 N ILE A 591
SHEET 9 AB1 9 ARG D 156 LEU D 158 -1 O LEU D 158 N PHE A 621
SHEET 1 AB2 4 PHE B 19 VAL B 25 0
SHEET 2 AB2 4 VAL B 32 GLU B 41 -1 O ALA B 33 N GLN B 24
SHEET 3 AB2 4 PRO B 54 SER B 63 -1 O ARG B 57 N GLN B 38
SHEET 4 AB2 4 ARG B 69 PRO B 70 -1 O ARG B 69 N LEU B 62
SHEET 1 AB3 4 GLY B 79 TRP B 85 0
SHEET 2 AB3 4 ASN B 91 ALA B 98 -1 O VAL B 95 N SER B 81
SHEET 3 AB3 4 VAL B 101 PRO B 109 -1 O LEU B 108 N LEU B 92
SHEET 4 AB3 4 ARG B 116 ARG B 117 -1 O ARG B 116 N LEU B 107
SHEET 1 AB4 4 VAL B 125 TRP B 130 0
SHEET 2 AB4 4 PHE B 136 THR B 141 -1 O ALA B 138 N GLN B 129
SHEET 3 AB4 4 ALA B 177 ASP B 182 -1 O TRP B 179 N PHE B 139
SHEET 4 AB4 4 LYS B 187 TYR B 192 -1 O LYS B 187 N ASP B 182
SHEET 1 AB5 9 ARG B 156 LEU B 158 0
SHEET 2 AB5 9 VAL C 619 PHE C 624 -1 O PHE C 621 N LEU B 158
SHEET 3 AB5 9 THR C 589 SER C 594 1 N ILE C 591 O ARG C 620
SHEET 4 AB5 9 ALA C 532 ASP C 536 1 N THR C 535 O LEU C 590
SHEET 5 AB5 9 LEU C 503 GLY C 513 1 N GLY C 512 O ASP C 536
SHEET 6 AB5 9 VAL C 426 ILE C 432 1 N LEU C 430 O ALA C 509
SHEET 7 AB5 9 GLY C 457 SER C 461 1 O GLY C 457 N LEU C 429
SHEET 8 AB5 9 GLY C 411 LEU C 418 -1 N TRP C 416 O TYR C 460
SHEET 9 AB5 9 GLN C 402 THR C 408 -1 N PHE C 406 O GLY C 413
SHEET 1 AB6 2 ARG B 164 ALA B 165 0
SHEET 2 AB6 2 ASP B 169 TRP B 170 -1 O ASP B 169 N ALA B 165
SHEET 1 AB7 4 LEU B 201 TRP B 203 0
SHEET 2 AB7 4 GLY B 209 GLN B 214 -1 O LEU B 211 N SER B 202
SHEET 3 AB7 4 GLN B 226 PRO B 232 -1 O TYR B 229 N ILE B 212
SHEET 4 AB7 4 GLN B 243 SER B 250 -1 O LEU B 245 N VAL B 228
SHEET 1 AB8 4 ALA B 252 PRO B 257 0
SHEET 2 AB8 4 PHE B 264 GLY B 268 -1 O ILE B 267 N HIS B 253
SHEET 3 AB8 4 HIS B 280 GLU B 285 -1 O ILE B 284 N PHE B 264
SHEET 4 AB8 4 GLN B 288 ARG B 291 -1 O ARG B 290 N LEU B 283
SHEET 1 AB9 4 ARG B 318 TRP B 319 0
SHEET 2 AB9 4 THR B 324 VAL B 331 -1 O LEU B 326 N ARG B 318
SHEET 3 AB9 4 SER B 334 HIS B 341 -1 O PHE B 338 N PHE B 327
SHEET 4 AB9 4 GLY B 344 ASP B 350 -1 O LYS B 347 N THR B 339
SHEET 1 AC1 4 GLY B 355 ALA B 362 0
SHEET 2 AC1 4 VAL B 367 SER B 373 -1 O GLU B 372 N VAL B 356
SHEET 3 AC1 4 ARG B 376 LEU B 382 -1 O GLU B 381 N LEU B 369
SHEET 4 AC1 4 GLN B 385 ARG B 386 -1 O GLN B 385 N LEU B 382
SHEET 1 AC2 9 GLN B 402 THR B 408 0
SHEET 2 AC2 9 GLY B 411 LEU B 418 -1 O VAL B 417 N GLN B 402
SHEET 3 AC2 9 GLY B 457 SER B 461 -1 O TYR B 460 N TRP B 416
SHEET 4 AC2 9 VAL B 426 ILE B 432 1 N LEU B 429 O GLY B 457
SHEET 5 AC2 9 LEU B 503 GLY B 513 1 O ALA B 509 N LEU B 430
SHEET 6 AC2 9 ALA B 532 ASP B 536 1 O ASP B 536 N GLY B 512
SHEET 7 AC2 9 THR B 589 SER B 594 1 O LEU B 590 N THR B 535
SHEET 8 AC2 9 VAL B 619 PHE B 624 1 O ARG B 620 N ILE B 591
SHEET 9 AC2 9 ARG C 156 LEU C 158 -1 O LEU C 158 N PHE B 621
SHEET 1 AC3 4 PHE C 19 VAL C 25 0
SHEET 2 AC3 4 VAL C 32 GLU C 41 -1 O ALA C 33 N GLN C 24
SHEET 3 AC3 4 PRO C 54 SER C 63 -1 O ARG C 57 N GLN C 38
SHEET 4 AC3 4 ARG C 69 PRO C 70 -1 O ARG C 69 N LEU C 62
SHEET 1 AC4 4 GLY C 79 TRP C 85 0
SHEET 2 AC4 4 ASN C 91 ALA C 98 -1 O ALA C 93 N ARG C 84
SHEET 3 AC4 4 VAL C 101 PRO C 109 -1 O LEU C 108 N LEU C 92
SHEET 4 AC4 4 ARG C 116 ARG C 117 -1 O ARG C 116 N LEU C 107
SHEET 1 AC5 4 SER C 126 TRP C 130 0
SHEET 2 AC5 4 PHE C 136 THR C 141 -1 O ALA C 138 N GLN C 129
SHEET 3 AC5 4 ALA C 177 ASP C 182 -1 O TRP C 179 N PHE C 139
SHEET 4 AC5 4 LYS C 187 TYR C 192 -1 O LYS C 187 N ASP C 182
SHEET 1 AC6 2 ARG C 164 ALA C 165 0
SHEET 2 AC6 2 ASP C 169 TRP C 170 -1 O ASP C 169 N ALA C 165
SHEET 1 AC7 4 LEU C 201 TRP C 203 0
SHEET 2 AC7 4 GLY C 209 GLN C 214 -1 O LEU C 211 N SER C 202
SHEET 3 AC7 4 GLN C 226 PRO C 232 -1 O ASP C 227 N GLN C 214
SHEET 4 AC7 4 GLN C 243 SER C 250 -1 O LEU C 245 N VAL C 228
SHEET 1 AC8 4 ALA C 252 PRO C 257 0
SHEET 2 AC8 4 PHE C 264 GLY C 268 -1 O ILE C 267 N HIS C 253
SHEET 3 AC8 4 HIS C 280 GLU C 285 -1 O ILE C 284 N PHE C 264
SHEET 4 AC8 4 GLN C 288 ARG C 291 -1 O ARG C 290 N LEU C 283
SHEET 1 AC9 4 ARG C 318 ASP C 321 0
SHEET 2 AC9 4 THR C 324 VAL C 331 -1 O LEU C 326 N ARG C 318
SHEET 3 AC9 4 SER C 334 HIS C 341 -1 O PHE C 338 N PHE C 327
SHEET 4 AC9 4 VAL C 346 ASP C 350 -1 O ASP C 350 N LEU C 337
SHEET 1 AD1 4 GLY C 355 ALA C 362 0
SHEET 2 AD1 4 VAL C 367 SER C 373 -1 O GLU C 372 N VAL C 356
SHEET 3 AD1 4 ARG C 376 LEU C 382 -1 O GLU C 381 N LEU C 369
SHEET 4 AD1 4 GLN C 385 ARG C 386 -1 O GLN C 385 N LEU C 382
SHEET 1 AD2 4 PHE D 19 VAL D 25 0
SHEET 2 AD2 4 VAL D 32 GLU D 41 -1 O ALA D 33 N GLN D 24
SHEET 3 AD2 4 PRO D 54 SER D 63 -1 O ARG D 57 N GLN D 38
SHEET 4 AD2 4 ARG D 69 PRO D 70 -1 O ARG D 69 N LEU D 62
SHEET 1 AD3 4 GLY D 79 TRP D 85 0
SHEET 2 AD3 4 ASN D 91 ALA D 98 -1 O VAL D 95 N SER D 81
SHEET 3 AD3 4 VAL D 101 PRO D 109 -1 O LEU D 108 N LEU D 92
SHEET 4 AD3 4 ARG D 116 ARG D 117 -1 O ARG D 116 N LEU D 107
SHEET 1 AD4 4 SER D 126 TRP D 130 0
SHEET 2 AD4 4 PHE D 136 THR D 141 -1 O ALA D 138 N GLN D 129
SHEET 3 AD4 4 ALA D 177 ASP D 182 -1 O TRP D 179 N PHE D 139
SHEET 4 AD4 4 LYS D 187 TYR D 192 -1 O LYS D 187 N ASP D 182
SHEET 1 AD5 2 ARG D 164 ALA D 165 0
SHEET 2 AD5 2 ASP D 169 TRP D 170 -1 O ASP D 169 N ALA D 165
SHEET 1 AD6 4 LEU D 201 TRP D 203 0
SHEET 2 AD6 4 GLY D 209 GLN D 214 -1 O LEU D 211 N SER D 202
SHEET 3 AD6 4 GLN D 226 PRO D 232 -1 O TYR D 229 N ILE D 212
SHEET 4 AD6 4 GLN D 243 SER D 250 -1 O LEU D 245 N VAL D 228
SHEET 1 AD7 4 ALA D 252 PRO D 257 0
SHEET 2 AD7 4 PHE D 264 GLY D 268 -1 O ILE D 267 N HIS D 253
SHEET 3 AD7 4 HIS D 280 GLU D 285 -1 O ILE D 284 N PHE D 264
SHEET 4 AD7 4 GLN D 288 ARG D 291 -1 O ARG D 290 N LEU D 283
SHEET 1 AD8 4 ARG D 318 ASP D 321 0
SHEET 2 AD8 4 THR D 324 VAL D 331 -1 O LEU D 326 N ARG D 318
SHEET 3 AD8 4 SER D 334 HIS D 341 -1 O PHE D 338 N PHE D 327
SHEET 4 AD8 4 VAL D 346 ASP D 350 -1 O LYS D 347 N THR D 339
SHEET 1 AD9 4 VAL D 356 ALA D 362 0
SHEET 2 AD9 4 VAL D 367 SER D 373 -1 O GLU D 372 N VAL D 356
SHEET 3 AD9 4 ARG D 376 LEU D 382 -1 O GLU D 381 N LEU D 369
SHEET 4 AD9 4 GLN D 385 ARG D 386 -1 O GLN D 385 N LEU D 382
CISPEP 1 GLY A 435 PRO A 436 0 8.48
CISPEP 2 GLY B 435 PRO B 436 0 8.08
CISPEP 3 GLY C 435 PRO C 436 0 7.78
CISPEP 4 GLY D 435 PRO D 436 0 7.62
SITE 1 AC1 6 GLY A 434 GLY A 435 ALA A 514 ARG A 537
SITE 2 AC1 6 HIS A 629 ARG A 633
SITE 1 AC2 4 VAL A 310 GLY A 311 SER A 634 HOH A1065
SITE 1 AC3 5 THR A 119 HIS A 120 PHE A 121 LEU A 188
SITE 2 AC3 5 HOH A 947
SITE 1 AC4 10 PRO A 161 VAL A 162 TYR A 163 ARG A 164
SITE 2 AC4 10 GLY A 547 THR A 548 SER A 549 ASP A 550
SITE 3 AC4 10 HOH A 973 HOH A1040
SITE 1 AC5 8 THR A 528 PHE A 530 GLN A 531 LYS A 586
SITE 2 AC5 8 THR A 587 PRO A 588 HOH A 856 HOH A 977
SITE 1 AC6 6 GLY B 434 GLY B 435 ALA B 514 ARG B 537
SITE 2 AC6 6 HIS B 629 ARG B 633
SITE 1 AC7 4 VAL B 310 GLY B 311 SER B 634 HOH B1131
SITE 1 AC8 8 THR B 528 PHE B 530 GLN B 531 LYS B 586
SITE 2 AC8 8 THR B 587 PRO B 588 HOH B 845 HOH B 888
SITE 1 AC9 12 TYR B 440 THR B 445 GLU B 447 PHE B 448
SITE 2 AC9 12 ARG B 537 ARG B 643 HOH B 852 HOH B 920
SITE 3 AC9 12 HOH B 934 HOH B1011 HOH B1135 HOH B1280
SITE 1 AD1 7 GLY C 434 ALA C 514 ARG C 537 HIS C 629
SITE 2 AD1 7 ARG C 633 HOH C1189 HOH C1309
SITE 1 AD2 4 VAL C 310 GLY C 311 SER C 634 HOH C1188
SITE 1 AD3 8 THR C 528 PHE C 530 GLN C 531 LYS C 586
SITE 2 AD3 8 THR C 587 PRO C 588 HOH C 892 HOH C1227
SITE 1 AD4 10 TYR C 440 THR C 445 GLU C 447 ARG C 537
SITE 2 AD4 10 ARG C 643 HOH C 896 HOH C 913 HOH C 951
SITE 3 AD4 10 HOH C 960 HOH C1117
SITE 1 AD5 5 GLY D 434 ALA D 514 ARG D 537 HIS D 629
SITE 2 AD5 5 ARG D 633
SITE 1 AD6 4 VAL D 310 GLY D 311 SER D 634 HOH D1187
CRYST1 77.195 190.015 119.548 90.00 108.46 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012954 0.000000 0.004325 0.00000
SCALE2 0.000000 0.005263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008819 0.00000
TER 5093 LEU A 655
TER 10150 LEU B 655
TER 15205 LEU C 655
TER 20232 LEU D 655
MASTER 467 0 15 60 156 0 29 623451 4 134 204
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