5a2g-pdb | HEADER HYDROLASE 19-MAY-15 5A2G
TITLE AN ESTERASE FROM ANAEROBIC CLOSTRIDIUM HATHEWAYI CAN
TITLE 2 HYDROLYZE ALIPHATIC AROMATIC POLYESTERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ESTERASE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUNGATELLA HATHEWAYI;
SOURCE 3 ORGANISM_TAXID: 566550;
SOURCE 4 STRAIN: DSM 13479;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: GOLD
KEYWDS HYDROLASE, MICROBIAL POLYESTERASE, ANAEROBIC ESTERASE, POLYESTER
KEYWDS 2 BIODEGRADATION, BIOGAS BATCH, ANAEROBIC BIODEGRADATION, CLOSTRIDIUM
KEYWDS 3 HATHEWAYI
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HROMIC,T.PAVKOV KELLER,G.STEINKELLNER,K.GRUBER,V.PERZ,
AUTHOR 2 A.BAUMSCHLAGER,K.BLEYMAIER,S.ZITZENBACHER,A.ZANKEL,C.MAYRHOFER,
AUTHOR 3 C.SINKEL,U.KUEPER,K.A.SCHLEGEL,D.RIBITSCH,G.M.GUEBITZ
REVDAT 1 24-FEB-16 5A2G 0
JRNL AUTH V.PERZ,K.BLEYMAIER,C.SINKEL,U.KUEPER,M.BONNEKESSEL,
JRNL AUTH 2 D.RIBITSCH,G.M.GUEBITZ
JRNL TITL SUBSTRATE SPECIFICITIES OF CUTINASES ON ALIPHATIC-AROMATIC
JRNL TITL 2 POLYESTERS AND ON THEIR MODEL SUBSTRATES.
JRNL REF N.BIOTECHNOL V. 33 295 2016
JRNL REFN ISSN 1876-4347
JRNL PMID 26594021
JRNL DOI 10.1016/J.NBT.2015.11.004
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.899
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.103
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.39
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.53
REMARK 3 NUMBER OF REFLECTIONS : 163038
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1910
REMARK 3 R VALUE (WORKING SET) : 0.1886
REMARK 3 FREE R VALUE : 0.2374
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 8044
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 60.1332 - 5.8991 0.91 5674 273 0.1442 0.1663
REMARK 3 2 5.8991 - 4.6829 0.96 5855 295 0.1358 0.1623
REMARK 3 3 4.6829 - 4.0911 0.86 5296 303 0.1308 0.1597
REMARK 3 4 4.0911 - 3.7171 0.90 5477 266 0.1460 0.1717
REMARK 3 5 3.7171 - 3.4507 0.92 5669 270 0.1642 0.2082
REMARK 3 6 3.4507 - 3.2473 0.94 5747 277 0.1813 0.2311
REMARK 3 7 3.2473 - 3.0846 0.94 5805 274 0.1904 0.2313
REMARK 3 8 3.0846 - 2.9504 0.90 5489 303 0.1970 0.2474
REMARK 3 9 2.9504 - 2.8368 0.78 4737 280 0.1950 0.2477
REMARK 3 10 2.8368 - 2.7389 0.85 5221 274 0.1993 0.2556
REMARK 3 11 2.7389 - 2.6533 0.87 5375 237 0.1974 0.2423
REMARK 3 12 2.6533 - 2.5774 0.89 5350 295 0.1973 0.2671
REMARK 3 13 2.5774 - 2.5096 0.89 5452 305 0.1996 0.2495
REMARK 3 14 2.5096 - 2.4483 0.90 5525 274 0.1989 0.2697
REMARK 3 15 2.4483 - 2.3927 0.90 5455 282 0.1991 0.2723
REMARK 3 16 2.3927 - 2.3418 0.91 5556 297 0.2089 0.2798
REMARK 3 17 2.3418 - 2.2949 0.87 5238 269 0.2163 0.2940
REMARK 3 18 2.2949 - 2.2516 0.74 4568 262 0.2260 0.3033
REMARK 3 19 2.2516 - 2.2114 0.80 4815 292 0.2439 0.3016
REMARK 3 20 2.2114 - 2.1739 0.82 5033 268 0.2331 0.3120
REMARK 3 21 2.1739 - 2.1388 0.81 4931 237 0.2296 0.2821
REMARK 3 22 2.1388 - 2.1059 0.82 5140 227 0.2243 0.2662
REMARK 3 23 2.1059 - 2.0750 0.82 4898 279 0.2350 0.3032
REMARK 3 24 2.0750 - 2.0457 0.81 4951 267 0.2454 0.3195
REMARK 3 25 2.0457 - 2.0181 0.80 4965 237 0.2505 0.3032
REMARK 3 26 2.0181 - 1.9919 0.79 4804 232 0.2600 0.3145
REMARK 3 27 1.9919 - 1.9670 0.78 4757 254 0.2647 0.3201
REMARK 3 28 1.9670 - 1.9433 0.77 4672 250 0.2748 0.3439
REMARK 3 29 1.9433 - 1.9207 0.75 4625 245 0.2951 0.3421
REMARK 3 30 1.9207 - 1.8991 0.65 3914 220 0.3274 0.3891
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.27
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.99
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.92
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 : 0.005 16204
REMARK 3 ANGLE : 0.914 22004
REMARK 3 CHIRALITY : 0.036 2320
REMARK 3 PLANARITY : 0.005 2888
REMARK 3 DIHEDRAL : 13.544 5904
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 5A2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-15.
REMARK 100 THE PDBE ID CODE IS EBI-63816.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-14
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 : PETRA III
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M-F)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 163181
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 60.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.1
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.1
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09
REMARK 200 FOR THE DATA SET : 7.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.7
REMARK 200 R MERGE FOR SHELL (I) : 0.59
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XDS
REMARK 200 STARTING MODEL: PDB ENTRY 2OGS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE, 0.1 M
REMARK 280 HEPES, PH 7.0 AND 0.5 % W/V POLYETHYLENE GLYCOL 8000
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 120.91500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.7 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 350
REMARK 350 BIOMOLECULE: 2
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: 3990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 503
REMARK 465 ASN A 504
REMARK 465 LEU A 505
REMARK 465 THR A 506
REMARK 465 LEU A 507
REMARK 465 ALA A 508
REMARK 465 ASN A 509
REMARK 465 ILE A 510
REMARK 465 THR A 511
REMARK 465 GLN A 512
REMARK 465 GLU A 513
REMARK 465 ASP A 514
REMARK 465 ASN A 515
REMARK 465 GLN A 516
REMARK 465 ILE A 517
REMARK 465 GLN A 518
REMARK 465 HIS A 519
REMARK 465 ALA A 520
REMARK 465 LEU A 521
REMARK 465 GLU A 522
REMARK 465 MET B 1
REMARK 465 PRO B 503
REMARK 465 ASN B 504
REMARK 465 LEU B 505
REMARK 465 THR B 506
REMARK 465 LEU B 507
REMARK 465 ALA B 508
REMARK 465 ASN B 509
REMARK 465 ILE B 510
REMARK 465 THR B 511
REMARK 465 GLN B 512
REMARK 465 GLU B 513
REMARK 465 ASP B 514
REMARK 465 ASN B 515
REMARK 465 GLN B 516
REMARK 465 ILE B 517
REMARK 465 GLN B 518
REMARK 465 HIS B 519
REMARK 465 ALA B 520
REMARK 465 LEU B 521
REMARK 465 GLU B 522
REMARK 465 MET C 1
REMARK 465 PRO C 503
REMARK 465 ASN C 504
REMARK 465 LEU C 505
REMARK 465 THR C 506
REMARK 465 LEU C 507
REMARK 465 ALA C 508
REMARK 465 ASN C 509
REMARK 465 ILE C 510
REMARK 465 THR C 511
REMARK 465 GLN C 512
REMARK 465 GLU C 513
REMARK 465 ASP C 514
REMARK 465 ASN C 515
REMARK 465 GLN C 516
REMARK 465 ILE C 517
REMARK 465 GLN C 518
REMARK 465 HIS C 519
REMARK 465 ALA C 520
REMARK 465 LEU C 521
REMARK 465 GLU C 522
REMARK 465 MET D 1
REMARK 465 PRO D 503
REMARK 465 ASN D 504
REMARK 465 LEU D 505
REMARK 465 THR D 506
REMARK 465 LEU D 507
REMARK 465 ALA D 508
REMARK 465 ASN D 509
REMARK 465 ILE D 510
REMARK 465 THR D 511
REMARK 465 GLN D 512
REMARK 465 GLU D 513
REMARK 465 ASP D 514
REMARK 465 ASN D 515
REMARK 465 GLN D 516
REMARK 465 ILE D 517
REMARK 465 GLN D 518
REMARK 465 HIS D 519
REMARK 465 ALA D 520
REMARK 465 LEU D 521
REMARK 465 GLU D 522
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 86 NH1 ARG B 69 2.18
REMARK 500 O LEU B 153 OG SER B 165 2.19
REMARK 500 OH TYR B 498 O HOH B 2261 2.17
REMARK 500 N ALA D 2 O HOH C 2413 2.17
REMARK 500 O LYS D 16 O HOH D 2019 2.18
REMARK 500 O HOH A 2030 O HOH A 2189 2.15
REMARK 500 O HOH A 2072 O HOH A 2226 2.11
REMARK 500 O HOH B 2119 O HOH B 2121 2.19
REMARK 500 O HOH C 2052 O HOH C 2133 2.14
REMARK 500 O HOH D 2089 O HOH D 2191 2.13
REMARK 500 O HOH D 2165 O HOH D 2314 2.19
REMARK 500 O HOH D 2230 O HOH C 2286 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 7 -61.78 -141.34
REMARK 500 ALA A 57 77.52 -117.92
REMARK 500 ALA A 115 -133.55 46.65
REMARK 500 ASN A 148 -130.24 36.59
REMARK 500 PRO A 157 2.99 -69.68
REMARK 500 SER A 200 -119.28 58.86
REMARK 500 ASP A 294 -153.38 -159.23
REMARK 500 GLU A 323 -76.03 -35.27
REMARK 500 ASN A 410 73.08 65.56
REMARK 500 CYS A 417 -0.60 87.04
REMARK 500 ILE A 438 -54.30 -134.76
REMARK 500 ASN A 489 41.44 38.17
REMARK 500 TYR B 7 -56.57 -140.01
REMARK 500 ALA B 115 -132.87 48.60
REMARK 500 ASN B 148 -125.48 36.02
REMARK 500 SER B 200 -119.71 51.99
REMARK 500 ASP B 294 -158.88 -163.12
REMARK 500 GLU B 323 -86.35 -25.40
REMARK 500 CYS B 417 -10.25 86.48
REMARK 500 ILE B 438 -47.68 -132.47
REMARK 500 ALA B 501 33.78 -84.57
REMARK 500 TYR C 7 -58.85 -141.93
REMARK 500 ALA C 115 -132.66 45.37
REMARK 500 ASN C 148 -127.42 38.36
REMARK 500 SER C 200 -117.28 54.75
REMARK 500 LEU C 233 75.66 -118.89
REMARK 500 ASP C 294 -152.62 -159.00
REMARK 500 GLU C 323 -72.18 -39.82
REMARK 500 ASN C 410 74.08 62.22
REMARK 500 CYS C 417 -9.20 80.98
REMARK 500 ILE C 438 -50.32 -133.70
REMARK 500 TYR D 7 -58.25 -134.33
REMARK 500 ALA D 58 12.92 -141.35
REMARK 500 ALA D 115 -135.88 46.41
REMARK 500 ASN D 148 -126.13 41.20
REMARK 500 SER D 200 -119.48 54.60
REMARK 500 ASP D 294 -148.93 -150.63
REMARK 500 GLU D 323 -83.58 -33.53
REMARK 500 PRO D 330 20.38 -70.50
REMARK 500 ASN D 410 66.54 61.95
REMARK 500 CYS D 417 -6.82 80.66
REMARK 500 GLU D 437 -61.65 75.17
REMARK 500 ALA D 501 44.29 -87.20
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 PO4 A1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D1503
DBREF 5A2G A 1 414 UNP D3AU79 D3AU79_9FIRM 1 414
DBREF 5A2G A 415 522 PDB 5A2G 5A2G 415 522
DBREF 5A2G B 1 414 UNP D3AU79 D3AU79_9FIRM 1 414
DBREF 5A2G B 415 522 PDB 5A2G 5A2G 415 522
DBREF 5A2G C 1 414 UNP D3AU79 D3AU79_9FIRM 1 414
DBREF 5A2G C 415 522 PDB 5A2G 5A2G 415 522
DBREF 5A2G D 1 414 UNP D3AU79 D3AU79_9FIRM 1 414
DBREF 5A2G D 415 522 PDB 5A2G 5A2G 415 522
SEQRES 1 A 522 MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL
SEQRES 2 A 522 GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU
SEQRES 3 A 522 GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA
SEQRES 4 A 522 ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU
SEQRES 5 A 522 GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO
SEQRES 6 A 522 MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL
SEQRES 7 A 522 PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER
SEQRES 8 A 522 LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS
SEQRES 9 A 522 LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER
SEQRES 10 A 522 MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU
SEQRES 11 A 522 ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL
SEQRES 12 A 522 ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER
SEQRES 13 A 522 PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY
SEQRES 14 A 522 GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP
SEQRES 15 A 522 ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR
SEQRES 16 A 522 ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY
SEQRES 17 A 522 LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG
SEQRES 18 A 522 ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO
SEQRES 19 A 522 TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET
SEQRES 20 A 522 LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG
SEQRES 21 A 522 LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR
SEQRES 22 A 522 ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR
SEQRES 23 A 522 ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY
SEQRES 24 A 522 GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR
SEQRES 25 A 522 ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA
SEQRES 26 A 522 MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU
SEQRES 27 A 522 ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY
SEQRES 28 A 522 HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR
SEQRES 29 A 522 PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR
SEQRES 30 A 522 ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU
SEQRES 31 A 522 ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA
SEQRES 32 A 522 LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS
SEQRES 33 A 522 CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU
SEQRES 34 A 522 VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU
SEQRES 35 A 522 GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU
SEQRES 36 A 522 THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO
SEQRES 37 A 522 VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP
SEQRES 38 A 522 ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU
SEQRES 39 A 522 LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU
SEQRES 40 A 522 ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA
SEQRES 41 A 522 LEU GLU
SEQRES 1 B 522 MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL
SEQRES 2 B 522 GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU
SEQRES 3 B 522 GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA
SEQRES 4 B 522 ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU
SEQRES 5 B 522 GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO
SEQRES 6 B 522 MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL
SEQRES 7 B 522 PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER
SEQRES 8 B 522 LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS
SEQRES 9 B 522 LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER
SEQRES 10 B 522 MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU
SEQRES 11 B 522 ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL
SEQRES 12 B 522 ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER
SEQRES 13 B 522 PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY
SEQRES 14 B 522 GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP
SEQRES 15 B 522 ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR
SEQRES 16 B 522 ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY
SEQRES 17 B 522 LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG
SEQRES 18 B 522 ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO
SEQRES 19 B 522 TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET
SEQRES 20 B 522 LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG
SEQRES 21 B 522 LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR
SEQRES 22 B 522 ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR
SEQRES 23 B 522 ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY
SEQRES 24 B 522 GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR
SEQRES 25 B 522 ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA
SEQRES 26 B 522 MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU
SEQRES 27 B 522 ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY
SEQRES 28 B 522 HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR
SEQRES 29 B 522 PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR
SEQRES 30 B 522 ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU
SEQRES 31 B 522 ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA
SEQRES 32 B 522 LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS
SEQRES 33 B 522 CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU
SEQRES 34 B 522 VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU
SEQRES 35 B 522 GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU
SEQRES 36 B 522 THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO
SEQRES 37 B 522 VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP
SEQRES 38 B 522 ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU
SEQRES 39 B 522 LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU
SEQRES 40 B 522 ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA
SEQRES 41 B 522 LEU GLU
SEQRES 1 C 522 MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL
SEQRES 2 C 522 GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU
SEQRES 3 C 522 GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA
SEQRES 4 C 522 ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU
SEQRES 5 C 522 GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO
SEQRES 6 C 522 MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL
SEQRES 7 C 522 PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER
SEQRES 8 C 522 LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS
SEQRES 9 C 522 LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER
SEQRES 10 C 522 MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU
SEQRES 11 C 522 ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL
SEQRES 12 C 522 ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER
SEQRES 13 C 522 PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY
SEQRES 14 C 522 GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP
SEQRES 15 C 522 ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR
SEQRES 16 C 522 ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY
SEQRES 17 C 522 LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG
SEQRES 18 C 522 ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO
SEQRES 19 C 522 TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET
SEQRES 20 C 522 LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG
SEQRES 21 C 522 LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR
SEQRES 22 C 522 ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR
SEQRES 23 C 522 ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY
SEQRES 24 C 522 GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR
SEQRES 25 C 522 ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA
SEQRES 26 C 522 MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU
SEQRES 27 C 522 ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY
SEQRES 28 C 522 HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR
SEQRES 29 C 522 PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR
SEQRES 30 C 522 ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU
SEQRES 31 C 522 ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA
SEQRES 32 C 522 LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS
SEQRES 33 C 522 CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU
SEQRES 34 C 522 VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU
SEQRES 35 C 522 GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU
SEQRES 36 C 522 THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO
SEQRES 37 C 522 VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP
SEQRES 38 C 522 ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU
SEQRES 39 C 522 LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU
SEQRES 40 C 522 ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA
SEQRES 41 C 522 LEU GLU
SEQRES 1 D 522 MET ALA LYS GLN PHE LEU TYR ASP ASN LEU PRO VAL VAL
SEQRES 2 D 522 GLU THR LYS ALA GLY LYS LEU ARG GLY TYR GLN TRP GLU
SEQRES 3 D 522 GLY THR TYR ILE PHE LYS GLY ILE ARG TYR ALA ARG ALA
SEQRES 4 D 522 ASN ARG PHE GLN LEU PRO GLU GLU VAL GLU PRO TRP GLU
SEQRES 5 D 522 GLY VAL LYS GLU ALA ALA SER TYR GLY PHE VAL CYS PRO
SEQRES 6 D 522 MET LEU THR ARG ASP HIS PRO GLN GLY GLU LEU LEU VAL
SEQRES 7 D 522 PRO HIS ARG TYR TRP PRO GLN ASP GLU ASP CYS LEU SER
SEQRES 8 D 522 LEU ASN ILE TRP SER GLN SER LEU ASP ARG SER ALA LYS
SEQRES 9 D 522 LYS PRO VAL MET PHE TRP ILE HIS GLY GLY ALA PHE SER
SEQRES 10 D 522 MET GLY SER SER ILE GLU GLN LYS ALA TYR ASN GLY GLU
SEQRES 11 D 522 ASN MET SER ARG TYR GLY ASP VAL VAL VAL VAL THR VAL
SEQRES 12 D 522 ASN HIS ARG LEU ASN ILE LEU GLY TYR LEU ASP LEU SER
SEQRES 13 D 522 PRO TYR GLY GLU ARG TYR ALA GLY SER ALA ASN ALA GLY
SEQRES 14 D 522 GLN ALA ASP LEU VAL ALA ALA LEU LYS TRP VAL ARG ASP
SEQRES 15 D 522 ASN ILE GLU ALA PHE GLY GLY ASP PRO ASP ASN VAL THR
SEQRES 16 D 522 ILE PHE GLY GLN SER GLY GLY GLY MET LYS VAL SER GLY
SEQRES 17 D 522 LEU MET GLN THR PRO GLU ALA ASP GLY LEU PHE HIS ARG
SEQRES 18 D 522 ALA MET ILE MET SER GLY VAL ALA GLY ASP VAL LEU PRO
SEQRES 19 D 522 TYR SER THR GLY ASP SER ARG PRO LEU ILE GLN ALA MET
SEQRES 20 D 522 LEU LYS GLU LEU GLY LEU ALA GLU GLN GLU ALA GLY ARG
SEQRES 21 D 522 LEU GLU THR VAL PRO TYR TYR ASP LEU ALA ALA ALA TYR
SEQRES 22 D 522 ASN ARG VAL SER PRO ALA ILE ALA ARG ALA GLY GLY TYR
SEQRES 23 D 522 ILE GLY CYS THR PRO ARG PRO ASP ASP PHE TYR LYS GLY
SEQRES 24 D 522 GLU GLY PRO ALA VAL GLY PHE THR ASP HIS ALA LYS THR
SEQRES 25 D 522 ILE PRO VAL MET VAL GLY THR VAL PHE GLY GLU PHE ALA
SEQRES 26 D 522 MET MET PRO LEU PRO PHE ASN LYS GLU THR ILE SER GLU
SEQRES 27 D 522 ALA GLU LEU ASP GLU ILE LEU ASP LYS ARG PHE GLN GLY
SEQRES 28 D 522 HIS GLY LYS GLU LEU LYS THR VAL PHE ALA GLU ALA TYR
SEQRES 29 D 522 PRO GLY LYS SER PRO VAL ASP LEU LEU THR LEU ASP THR
SEQRES 30 D 522 ILE PHE ARG GLY PRO THR LYS GLU PHE VAL ARG SER LEU
SEQRES 31 D 522 ALA ALA ALA GLY GLY SER VAL TYR SER TYR LEU PHE ALA
SEQRES 32 D 522 LEU GLU PHE PRO TYR GLN ASN GLN LYS THR ALA TRP HIS
SEQRES 33 D 522 CYS SER ASP ILE PRO PHE ILE PHE HIS ASN THR GLU LEU
SEQRES 34 D 522 VAL PRO VAL THR ASN ILE PRO GLU ILE SER ASP LYS LEU
SEQRES 35 D 522 GLU LYS GLN MET PHE ASP ALA VAL ILE HIS PHE VAL GLU
SEQRES 36 D 522 THR GLY ASP PRO ASN HIS LEU GLY ILE PRO GLN TRP PRO
SEQRES 37 D 522 VAL SER THR GLU ASP ARG GLU ALA THR MET ILE PHE ASP
SEQRES 38 D 522 ARG VAL CYS THR VAL ARG PHE ASN PHE ASP ASP TYR LEU
SEQRES 39 D 522 LEU GLU LEU TYR LYS LYS ALA LEU PRO ASN LEU THR LEU
SEQRES 40 D 522 ALA ASN ILE THR GLN GLU ASP ASN GLN ILE GLN HIS ALA
SEQRES 41 D 522 LEU GLU
HET PO4 A1503 5
HET PO4 B1503 5
HET PO4 C1503 5
HET PO4 D1503 5
HETNAM PO4 PHOSPHATE ION
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 9 HOH *1592(H2 O)
HELIX 1 1 LYS A 125 ASN A 128 5 4
HELIX 2 2 GLY A 129 ASP A 137 1 9
HELIX 3 3 LEU A 147 TYR A 152 1 6
HELIX 4 4 LEU A 155 GLY A 159 5 5
HELIX 5 5 GLY A 159 ALA A 163 5 5
HELIX 6 6 GLY A 164 ALA A 166 5 3
HELIX 7 7 ASN A 167 ILE A 184 1 18
HELIX 8 8 GLU A 185 PHE A 187 5 3
HELIX 9 9 SER A 200 GLN A 211 1 12
HELIX 10 10 THR A 212 ASP A 216 5 5
HELIX 11 11 ALA A 229 LEU A 233 5 5
HELIX 12 12 SER A 240 LEU A 251 1 12
HELIX 13 13 ALA A 254 THR A 263 5 10
HELIX 14 14 PRO A 265 ALA A 283 1 19
HELIX 15 15 GLU A 300 GLY A 305 1 6
HELIX 16 16 HIS A 309 ILE A 313 5 5
HELIX 17 17 SER A 337 PHE A 349 1 13
HELIX 18 18 HIS A 352 TYR A 364 1 13
HELIX 19 19 SER A 368 THR A 374 5 7
HELIX 20 20 PHE A 379 ALA A 393 1 15
HELIX 21 21 ASP A 419 PHE A 424 1 6
HELIX 22 22 ASN A 426 VAL A 430 5 5
HELIX 23 23 VAL A 430 ASN A 434 5 5
HELIX 24 24 ILE A 438 GLY A 457 1 20
HELIX 25 25 ASP A 491 LEU A 502 1 12
HELIX 26 26 LYS B 125 ASN B 128 5 4
HELIX 27 27 GLY B 129 ASP B 137 1 9
HELIX 28 28 LEU B 147 TYR B 152 1 6
HELIX 29 29 LEU B 155 GLY B 159 5 5
HELIX 30 30 GLY B 164 ALA B 166 5 3
HELIX 31 31 ASN B 167 ILE B 184 1 18
HELIX 32 32 GLU B 185 PHE B 187 5 3
HELIX 33 33 SER B 200 GLN B 211 1 12
HELIX 34 34 THR B 212 ASP B 216 5 5
HELIX 35 35 ALA B 229 LEU B 233 5 5
HELIX 36 36 SER B 240 LEU B 251 1 12
HELIX 37 37 GLU B 257 THR B 263 5 7
HELIX 38 38 PRO B 265 ALA B 283 1 19
HELIX 39 39 GLU B 300 GLY B 305 1 6
HELIX 40 40 HIS B 309 ILE B 313 5 5
HELIX 41 41 SER B 337 PHE B 349 1 13
HELIX 42 42 HIS B 352 TYR B 364 1 13
HELIX 43 43 SER B 368 THR B 374 5 7
HELIX 44 44 PHE B 379 ALA B 393 1 15
HELIX 45 45 ASP B 419 PHE B 424 1 6
HELIX 46 46 ASN B 426 VAL B 430 5 5
HELIX 47 47 VAL B 430 ASN B 434 5 5
HELIX 48 48 ILE B 438 GLY B 457 1 20
HELIX 49 49 ASP B 491 ALA B 501 1 11
HELIX 50 50 LYS C 125 ASN C 128 5 4
HELIX 51 51 GLY C 129 ASP C 137 1 9
HELIX 52 52 LEU C 147 TYR C 152 1 6
HELIX 53 53 LEU C 155 GLY C 159 5 5
HELIX 54 54 GLY C 159 ALA C 163 5 5
HELIX 55 55 GLY C 164 ALA C 166 5 3
HELIX 56 56 ASN C 167 ILE C 184 1 18
HELIX 57 57 GLU C 185 PHE C 187 5 3
HELIX 58 58 SER C 200 GLN C 211 1 12
HELIX 59 59 THR C 212 ASP C 216 5 5
HELIX 60 60 ALA C 229 LEU C 233 5 5
HELIX 61 61 SER C 240 LEU C 251 1 12
HELIX 62 62 ALA C 254 THR C 263 5 10
HELIX 63 63 PRO C 265 ALA C 283 1 19
HELIX 64 64 GLU C 300 GLY C 305 1 6
HELIX 65 65 HIS C 309 ILE C 313 5 5
HELIX 66 66 SER C 337 PHE C 349 1 13
HELIX 67 67 HIS C 352 TYR C 364 1 13
HELIX 68 68 SER C 368 THR C 374 5 7
HELIX 69 69 PHE C 379 ALA C 393 1 15
HELIX 70 70 ASP C 419 PHE C 424 1 6
HELIX 71 71 ASN C 426 VAL C 430 5 5
HELIX 72 72 VAL C 430 ASN C 434 5 5
HELIX 73 73 ILE C 438 GLY C 457 1 20
HELIX 74 74 ASP C 491 LEU C 502 1 12
HELIX 75 75 LYS D 125 ASN D 128 5 4
HELIX 76 76 GLY D 129 ASP D 137 1 9
HELIX 77 77 LEU D 147 TYR D 152 1 6
HELIX 78 78 GLY D 164 ALA D 166 5 3
HELIX 79 79 ASN D 167 ILE D 184 1 18
HELIX 80 80 GLU D 185 PHE D 187 5 3
HELIX 81 81 SER D 200 GLN D 211 1 12
HELIX 82 82 THR D 212 ASP D 216 5 5
HELIX 83 83 ALA D 229 LEU D 233 5 5
HELIX 84 84 SER D 240 LEU D 251 1 12
HELIX 85 85 GLU D 257 THR D 263 5 7
HELIX 86 86 PRO D 265 ALA D 283 1 19
HELIX 87 87 GLU D 300 GLY D 305 1 6
HELIX 88 88 THR D 307 THR D 312 1 6
HELIX 89 89 SER D 337 PHE D 349 1 13
HELIX 90 90 HIS D 352 TYR D 364 1 13
HELIX 91 91 SER D 368 THR D 374 5 7
HELIX 92 92 PHE D 379 ALA D 393 1 15
HELIX 93 93 ASP D 419 PHE D 424 1 6
HELIX 94 94 ASN D 426 VAL D 430 5 5
HELIX 95 95 VAL D 430 ASN D 434 5 5
HELIX 96 96 GLU D 437 GLY D 457 1 21
HELIX 97 97 ASP D 491 ALA D 501 1 11
SHEET 1 AA12 PHE A 5 LEU A 6 0
SHEET 2 AA12 TYR A 23 TRP A 25 -1 O GLN A 24 N LEU A 6
SHEET 3 AA12 THR A 28 ARG A 35 -1 O THR A 28 N TRP A 25
SHEET 4 AA12 SER A 91 SER A 96 -1 O LEU A 92 N ILE A 34
SHEET 5 AA12 VAL A 139 VAL A 143 -1 O VAL A 140 N TRP A 95
SHEET 6 AA12 LYS A 105 ILE A 111 1 O PRO A 106 N VAL A 139
SHEET 7 AA12 GLY A 189 GLN A 199 1 N ASP A 190 O LYS A 105
SHEET 8 AA12 ARG A 221 MET A 225 1 O ARG A 221 N ILE A 196
SHEET 9 AA12 VAL A 315 VAL A 320 1 O MET A 316 N ILE A 224
SHEET 10 AA12 VAL A 397 PHE A 402 1 O TYR A 398 N VAL A 317
SHEET 11 AA12 ALA A 476 PHE A 480 1 O ALA A 476 N SER A 399
SHEET 12 AA12 THR A 485 PHE A 488 -1 O THR A 485 N ILE A 479
SHEET 1 AB 3 VAL A 13 GLU A 14 0
SHEET 2 AB 3 LYS A 19 ARG A 21 -1 O LEU A 20 N VAL A 13
SHEET 3 AB 3 VAL A 54 GLU A 56 1 O LYS A 55 N ARG A 21
SHEET 1 BA12 PHE B 5 LEU B 6 0
SHEET 2 BA12 TYR B 23 TRP B 25 -1 O GLN B 24 N LEU B 6
SHEET 3 BA12 THR B 28 ARG B 35 -1 O THR B 28 N TRP B 25
SHEET 4 BA12 SER B 91 SER B 96 -1 O LEU B 92 N ILE B 34
SHEET 5 BA12 VAL B 139 VAL B 143 -1 O VAL B 140 N TRP B 95
SHEET 6 BA12 LYS B 105 ILE B 111 1 O PRO B 106 N VAL B 139
SHEET 7 BA12 GLY B 189 GLN B 199 1 N ASP B 190 O LYS B 105
SHEET 8 BA12 ARG B 221 MET B 225 1 O ARG B 221 N ILE B 196
SHEET 9 BA12 VAL B 315 VAL B 320 1 O MET B 316 N ILE B 224
SHEET 10 BA12 VAL B 397 PHE B 402 1 O TYR B 398 N VAL B 317
SHEET 11 BA12 ALA B 476 PHE B 480 1 O ALA B 476 N SER B 399
SHEET 12 BA12 THR B 485 PHE B 488 -1 O THR B 485 N ILE B 479
SHEET 1 BB 3 VAL B 13 THR B 15 0
SHEET 2 BB 3 GLY B 18 ARG B 21 -1 O GLY B 18 N THR B 15
SHEET 3 BB 3 VAL B 54 GLU B 56 1 O LYS B 55 N ARG B 21
SHEET 1 BC 2 GLU B 405 PHE B 406 0
SHEET 2 BC 2 LYS B 412 THR B 413 -1 O LYS B 412 N PHE B 406
SHEET 1 CA12 PHE C 5 LEU C 6 0
SHEET 2 CA12 TYR C 23 TRP C 25 -1 O GLN C 24 N LEU C 6
SHEET 3 CA12 THR C 28 ARG C 35 -1 O THR C 28 N TRP C 25
SHEET 4 CA12 SER C 91 SER C 96 -1 O LEU C 92 N ILE C 34
SHEET 5 CA12 VAL C 139 VAL C 143 -1 O VAL C 140 N TRP C 95
SHEET 6 CA12 LYS C 105 ILE C 111 1 O PRO C 106 N VAL C 139
SHEET 7 CA12 GLY C 189 GLN C 199 1 N ASP C 190 O LYS C 105
SHEET 8 CA12 ARG C 221 MET C 225 1 O ARG C 221 N ILE C 196
SHEET 9 CA12 VAL C 315 VAL C 320 1 O MET C 316 N ILE C 224
SHEET 10 CA12 VAL C 397 PHE C 402 1 O TYR C 398 N VAL C 317
SHEET 11 CA12 ALA C 476 PHE C 480 1 O ALA C 476 N SER C 399
SHEET 12 CA12 THR C 485 PHE C 488 -1 O THR C 485 N ILE C 479
SHEET 1 CB 3 VAL C 13 GLU C 14 0
SHEET 2 CB 3 LYS C 19 ARG C 21 -1 O LEU C 20 N VAL C 13
SHEET 3 CB 3 VAL C 54 GLU C 56 1 O LYS C 55 N ARG C 21
SHEET 1 CC 2 GLU C 405 PHE C 406 0
SHEET 2 CC 2 LYS C 412 THR C 413 -1 O LYS C 412 N PHE C 406
SHEET 1 DA12 PHE D 5 LEU D 6 0
SHEET 2 DA12 TYR D 23 TRP D 25 -1 O GLN D 24 N LEU D 6
SHEET 3 DA12 THR D 28 ARG D 35 -1 O THR D 28 N TRP D 25
SHEET 4 DA12 SER D 91 SER D 96 -1 O LEU D 92 N ILE D 34
SHEET 5 DA12 VAL D 139 VAL D 143 -1 O VAL D 140 N TRP D 95
SHEET 6 DA12 LYS D 105 ILE D 111 1 O PRO D 106 N VAL D 139
SHEET 7 DA12 GLY D 189 GLN D 199 1 N ASP D 190 O LYS D 105
SHEET 8 DA12 ARG D 221 MET D 225 1 O ARG D 221 N ILE D 196
SHEET 9 DA12 VAL D 315 VAL D 320 1 O MET D 316 N ILE D 224
SHEET 10 DA12 VAL D 397 PHE D 402 1 O TYR D 398 N VAL D 317
SHEET 11 DA12 ALA D 476 PHE D 480 1 O ALA D 476 N SER D 399
SHEET 12 DA12 THR D 485 PHE D 488 -1 O THR D 485 N ILE D 479
SHEET 1 DB 3 VAL D 13 GLU D 14 0
SHEET 2 DB 3 LYS D 19 ARG D 21 -1 O LEU D 20 N VAL D 13
SHEET 3 DB 3 VAL D 54 GLU D 56 1 O LYS D 55 N ARG D 21
SHEET 1 DC 2 GLU D 405 PHE D 406 0
SHEET 2 DC 2 LYS D 412 THR D 413 -1 O LYS D 412 N PHE D 406
SITE 1 AC1 11 LYS A 32 TYR A 60 ARG A 81 ASN A 128
SITE 2 AC1 11 HOH A2026 HOH A2042 HOH A2131 HOH A2148
SITE 3 AC1 11 HOH A2189 LYS B 125 HOH B3460
SITE 1 AC2 11 LYS A 125 HOH A2183 LYS B 32 TYR B 60
SITE 2 AC2 11 ARG B 81 ASN B 128 HOH B2027 HOH B2041
SITE 3 AC2 11 HOH B2114 HOH B2144 HOH B3330
SITE 1 AC3 10 LYS C 32 TYR C 60 ARG C 81 ASN C 128
SITE 2 AC3 10 HOH C2036 HOH C2054 HOH C2137 HOH C2152
SITE 3 AC3 10 HOH C2191 LYS D 125
SITE 1 AC4 11 LYS C 125 LYS D 32 TYR D 60 ARG D 81
SITE 2 AC4 11 ASN D 128 HOH D2027 HOH D2045 HOH D2119
SITE 3 AC4 11 HOH D2133 HOH D2168 HOH D2169
CRYST1 62.050 241.830 83.580 90.00 90.00 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 0.016116 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004135 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011965 0.00000
TER 3941 LEU A 502
TER 7882 LEU B 502
TER 11823 LEU C 502
TER 15764 LEU D 502
MASTER 414 0 4 97 66 0 12 617372 4 20 164
END
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