HEADER HYDROLASE 24-JUN-10 2XHY
TITLE CRYSTAL STRUCTURE OF E.COLI BGLA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-PHOSPHO-BETA-GLUCOSIDASE BGLA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BGLA;
COMPND 5 EC: 3.2.1.86
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12
KEYWDS HYDROLASE, GLYCOSIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TOTIR,C.ZUBIETA,N.ECHOLS,A.P.MAY,C.L.GEE,M.NANAO,T.ALBER
REVDAT 3 20-DEC-23 2XHY 1 REMARK
REVDAT 2 28-MAR-12 2XHY 1 AUTHOR JRNL REMARK VERSN
REVDAT 1 06-JUL-11 2XHY 0
JRNL AUTH M.TOTIR,N.ECHOLS,M.NANAO,C.L.GEE,A.MOSKALEVA,S.GRADIA,
JRNL AUTH 2 A.T.IAVARONE,J.M.BERGER,A.P.MAY,C.ZUBIETA,T.ALBER
JRNL TITL MACRO-TO-MICRO STRUCTURAL PROTEOMICS: NATIVE SOURCE PROTEINS
JRNL TITL 2 FOR HIGH-THROUGHPUT CRYSTALLIZATION.
JRNL REF PLOS ONE V. 7 32498 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22393408
JRNL DOI 10.1371/JOURNAL.PONE.0032498
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 82815
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4153
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 22.9412 - 7.0784 0.98 2794 149 0.1549 0.1635
REMARK 3 2 7.0784 - 5.6459 0.98 2774 146 0.1535 0.2210
REMARK 3 3 5.6459 - 4.9403 0.98 2767 141 0.1373 0.2102
REMARK 3 4 4.9403 - 4.4923 0.98 2806 149 0.1170 0.1590
REMARK 3 5 4.4923 - 4.1724 0.98 2752 140 0.1178 0.1712
REMARK 3 6 4.1724 - 3.9277 0.98 2810 146 0.1186 0.1793
REMARK 3 7 3.9277 - 3.7319 0.98 2754 141 0.1262 0.1848
REMARK 3 8 3.7319 - 3.5700 0.98 2756 170 0.1259 0.1908
REMARK 3 9 3.5700 - 3.4331 0.98 2763 145 0.1313 0.1996
REMARK 3 10 3.4331 - 3.3150 0.98 2745 147 0.1568 0.2240
REMARK 3 11 3.3150 - 3.2116 0.98 2767 148 0.1647 0.2493
REMARK 3 12 3.2116 - 3.1200 0.98 2791 142 0.1682 0.2297
REMARK 3 13 3.1200 - 3.0381 0.98 2725 144 0.1703 0.2370
REMARK 3 14 3.0381 - 2.9641 0.98 2778 137 0.1754 0.2580
REMARK 3 15 2.9641 - 2.8969 0.97 2758 138 0.1799 0.2656
REMARK 3 16 2.8969 - 2.8353 0.97 2754 136 0.1891 0.2436
REMARK 3 17 2.8353 - 2.7787 0.97 2829 127 0.1864 0.2533
REMARK 3 18 2.7787 - 2.7264 0.97 2664 147 0.1957 0.3134
REMARK 3 19 2.7264 - 2.6777 0.97 2813 134 0.1961 0.2570
REMARK 3 20 2.6777 - 2.6324 0.97 2744 135 0.2070 0.2871
REMARK 3 21 2.6324 - 2.5900 0.97 2761 147 0.1941 0.2773
REMARK 3 22 2.5900 - 2.5502 0.97 2721 157 0.1956 0.2967
REMARK 3 23 2.5502 - 2.5128 0.97 2742 156 0.2111 0.2989
REMARK 3 24 2.5128 - 2.4774 0.97 2732 144 0.2321 0.3657
REMARK 3 25 2.4774 - 2.4440 0.95 2723 144 0.2305 0.2976
REMARK 3 26 2.4440 - 2.4123 0.83 2330 121 0.2231 0.3115
REMARK 3 27 2.4123 - 2.3821 0.74 2070 129 0.2320 0.3293
REMARK 3 28 2.3821 - 2.3535 0.68 1886 104 0.2303 0.2747
REMARK 3 29 2.3535 - 2.3261 0.62 1739 100 0.2317 0.3204
REMARK 3 30 2.3261 - 2.3000 0.57 1614 89 0.2394 0.3222
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 34.76
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.10950
REMARK 3 B22 (A**2) : 0.52690
REMARK 3 B33 (A**2) : 0.58270
REMARK 3 B12 (A**2) : 0.59920
REMARK 3 B13 (A**2) : -0.67730
REMARK 3 B23 (A**2) : 1.39060
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 : 0.003 15755
REMARK 3 ANGLE : 0.704 21324
REMARK 3 CHIRALITY : 0.054 2121
REMARK 3 PLANARITY : 0.002 2763
REMARK 3 DIHEDRAL : 15.998 5613
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 2XHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1290044306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-08
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 : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92004
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83032
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 22.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -10.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ENTRY 1XK6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 5220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.5 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 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: 5650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.4 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 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 ILE A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 329
REMARK 465 ASP A 330
REMARK 465 ALA A 331
REMARK 465 ILE A 332
REMARK 465 SER A 333
REMARK 465 GLY A 334
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 VAL B 3
REMARK 465 THR B 328
REMARK 465 GLY B 329
REMARK 465 ASP B 330
REMARK 465 ALA B 331
REMARK 465 ILE B 332
REMARK 465 SER B 333
REMARK 465 GLY B 334
REMARK 465 PHE B 335
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 VAL C 3
REMARK 465 LYS C 4
REMARK 465 THR C 328
REMARK 465 GLY C 329
REMARK 465 ASP C 330
REMARK 465 ALA C 331
REMARK 465 ILE C 332
REMARK 465 SER C 333
REMARK 465 GLY C 334
REMARK 465 PHE C 335
REMARK 465 GLU C 336
REMARK 465 MET D 1
REMARK 465 ILE D 2
REMARK 465 VAL D 3
REMARK 465 LYS D 4
REMARK 465 GLU D 325
REMARK 465 GLY D 326
REMARK 465 GLY D 327
REMARK 465 THR D 328
REMARK 465 GLY D 329
REMARK 465 ASP D 330
REMARK 465 ALA D 331
REMARK 465 ILE D 332
REMARK 465 SER D 333
REMARK 465 GLY D 334
REMARK 465 PHE D 335
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 ASP A 348 OD1 OD2
REMARK 470 ASP B 348 OD1 OD2
REMARK 470 LYS C 5 CG CD CE NZ
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 VAL A 23 -42.58 -130.07
REMARK 500 ALA A 44 -174.26 -171.75
REMARK 500 ALA A 66 -127.36 53.43
REMARK 500 GLU A 136 38.53 -163.74
REMARK 500 SER A 147 -147.82 62.17
REMARK 500 THR A 177 -73.93 -83.62
REMARK 500 GLU A 180 63.09 34.28
REMARK 500 ASN A 233 97.61 -165.22
REMARK 500 TYR A 317 -31.60 -137.03
REMARK 500 GLU A 325 -122.12 -98.86
REMARK 500 ASN A 378 124.99 173.20
REMARK 500 ASP A 394 59.79 -98.20
REMARK 500 VAL B 23 -39.75 -131.86
REMARK 500 ALA B 66 -124.63 50.63
REMARK 500 GLU B 136 43.13 -147.50
REMARK 500 SER B 147 -150.05 67.20
REMARK 500 THR B 177 -75.54 -82.85
REMARK 500 GLU B 180 57.09 31.73
REMARK 500 ASN B 233 98.56 -162.60
REMARK 500 ASP B 354 77.51 -160.43
REMARK 500 PHE B 374 104.58 -162.97
REMARK 500 ASP B 394 66.44 -101.34
REMARK 500 VAL C 23 -39.13 -130.14
REMARK 500 ALA C 66 -129.44 44.12
REMARK 500 ALA C 93 109.88 -55.15
REMARK 500 GLU C 136 40.60 -157.90
REMARK 500 SER C 147 -150.47 64.95
REMARK 500 THR C 177 -79.25 -89.03
REMARK 500 GLU C 180 54.21 32.30
REMARK 500 ASN C 233 96.03 -168.38
REMARK 500 TYR C 317 -33.76 -133.32
REMARK 500 SER C 338 -167.01 -114.13
REMARK 500 ASN C 378 145.04 -172.76
REMARK 500 ASP C 394 60.85 -107.24
REMARK 500 ALA D 66 -129.16 49.58
REMARK 500 GLU D 136 39.91 -154.10
REMARK 500 SER D 147 -151.26 62.79
REMARK 500 THR D 177 -76.15 -76.73
REMARK 500 GLU D 180 54.23 33.45
REMARK 500 ASN D 233 90.67 -171.37
REMARK 500 PRO D 234 -5.34 -58.34
REMARK 500 ASN D 378 127.43 -171.15
REMARK 500 ASP D 394 56.96 -104.08
REMARK 500 TYR D 414 -61.55 -90.31
REMARK 500 TYR D 422 112.78 -160.45
REMARK 500 ASP D 429 133.05 -40.00
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 A2008 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A2018 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A2075 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH B2027 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH B2049 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B2134 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH C2016 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH D2050 DISTANCE = 6.61 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D 1487
DBREF 2XHY A 1 479 UNP Q46829 BGLA_ECOLI 1 479
DBREF 2XHY B 1 479 UNP Q46829 BGLA_ECOLI 1 479
DBREF 2XHY C 1 479 UNP Q46829 BGLA_ECOLI 1 479
DBREF 2XHY D 1 479 UNP Q46829 BGLA_ECOLI 1 479
SEQRES 1 A 479 MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU
SEQRES 2 A 479 TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY
SEQRES 3 A 479 TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL
SEQRES 4 A 479 LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR
SEQRES 5 A 479 LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU
SEQRES 6 A 479 ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS
SEQRES 7 A 479 LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER
SEQRES 8 A 479 ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA
SEQRES 9 A 479 GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET
SEQRES 10 A 479 PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE
SEQRES 11 A 479 THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN
SEQRES 12 A 479 GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE
SEQRES 13 A 479 PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS
SEQRES 14 A 479 HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN
SEQRES 15 A 479 ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS
SEQRES 16 A 479 CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU
SEQRES 17 A 479 GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA
SEQRES 18 A 479 SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO
SEQRES 19 A 479 GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU
SEQRES 20 A 479 TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA
SEQRES 21 A 479 GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL
SEQRES 22 A 479 GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU
SEQRES 23 A 479 TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY
SEQRES 24 A 479 ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU
SEQRES 25 A 479 GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU
SEQRES 26 A 479 GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER
SEQRES 27 A 479 VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP
SEQRES 28 A 479 GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU
SEQRES 29 A 479 LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU
SEQRES 30 A 479 ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY
SEQRES 31 A 479 SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA
SEQRES 32 A 479 HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY
SEQRES 33 A 479 VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP
SEQRES 34 A 479 CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR
SEQRES 35 A 479 GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY
SEQRES 36 A 479 ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR
SEQRES 37 A 479 LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU
SEQRES 1 B 479 MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU
SEQRES 2 B 479 TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY
SEQRES 3 B 479 TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL
SEQRES 4 B 479 LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR
SEQRES 5 B 479 LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU
SEQRES 6 B 479 ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS
SEQRES 7 B 479 LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER
SEQRES 8 B 479 ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA
SEQRES 9 B 479 GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET
SEQRES 10 B 479 PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE
SEQRES 11 B 479 THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN
SEQRES 12 B 479 GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE
SEQRES 13 B 479 PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS
SEQRES 14 B 479 HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN
SEQRES 15 B 479 ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS
SEQRES 16 B 479 CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU
SEQRES 17 B 479 GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA
SEQRES 18 B 479 SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO
SEQRES 19 B 479 GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU
SEQRES 20 B 479 TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA
SEQRES 21 B 479 GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL
SEQRES 22 B 479 GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU
SEQRES 23 B 479 TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY
SEQRES 24 B 479 ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU
SEQRES 25 B 479 GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU
SEQRES 26 B 479 GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER
SEQRES 27 B 479 VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP
SEQRES 28 B 479 GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU
SEQRES 29 B 479 LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU
SEQRES 30 B 479 ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY
SEQRES 31 B 479 SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA
SEQRES 32 B 479 HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY
SEQRES 33 B 479 VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP
SEQRES 34 B 479 CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR
SEQRES 35 B 479 GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY
SEQRES 36 B 479 ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR
SEQRES 37 B 479 LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU
SEQRES 1 C 479 MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU
SEQRES 2 C 479 TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY
SEQRES 3 C 479 TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL
SEQRES 4 C 479 LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR
SEQRES 5 C 479 LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU
SEQRES 6 C 479 ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS
SEQRES 7 C 479 LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER
SEQRES 8 C 479 ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA
SEQRES 9 C 479 GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET
SEQRES 10 C 479 PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE
SEQRES 11 C 479 THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN
SEQRES 12 C 479 GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE
SEQRES 13 C 479 PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS
SEQRES 14 C 479 HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN
SEQRES 15 C 479 ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS
SEQRES 16 C 479 CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU
SEQRES 17 C 479 GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA
SEQRES 18 C 479 SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO
SEQRES 19 C 479 GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU
SEQRES 20 C 479 TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA
SEQRES 21 C 479 GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL
SEQRES 22 C 479 GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU
SEQRES 23 C 479 TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY
SEQRES 24 C 479 ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU
SEQRES 25 C 479 GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU
SEQRES 26 C 479 GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER
SEQRES 27 C 479 VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP
SEQRES 28 C 479 GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU
SEQRES 29 C 479 LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU
SEQRES 30 C 479 ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY
SEQRES 31 C 479 SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA
SEQRES 32 C 479 HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY
SEQRES 33 C 479 VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP
SEQRES 34 C 479 CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR
SEQRES 35 C 479 GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY
SEQRES 36 C 479 ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR
SEQRES 37 C 479 LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU
SEQRES 1 D 479 MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU
SEQRES 2 D 479 TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY
SEQRES 3 D 479 TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL
SEQRES 4 D 479 LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR
SEQRES 5 D 479 LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU
SEQRES 6 D 479 ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS
SEQRES 7 D 479 LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER
SEQRES 8 D 479 ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA
SEQRES 9 D 479 GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET
SEQRES 10 D 479 PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE
SEQRES 11 D 479 THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN
SEQRES 12 D 479 GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE
SEQRES 13 D 479 PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS
SEQRES 14 D 479 HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN
SEQRES 15 D 479 ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS
SEQRES 16 D 479 CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU
SEQRES 17 D 479 GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA
SEQRES 18 D 479 SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO
SEQRES 19 D 479 GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU
SEQRES 20 D 479 TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA
SEQRES 21 D 479 GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL
SEQRES 22 D 479 GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU
SEQRES 23 D 479 TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY
SEQRES 24 D 479 ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU
SEQRES 25 D 479 GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU
SEQRES 26 D 479 GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER
SEQRES 27 D 479 VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP
SEQRES 28 D 479 GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU
SEQRES 29 D 479 LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU
SEQRES 30 D 479 ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY
SEQRES 31 D 479 SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA
SEQRES 32 D 479 HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY
SEQRES 33 D 479 VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP
SEQRES 34 D 479 CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR
SEQRES 35 D 479 GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY
SEQRES 36 D 479 ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR
SEQRES 37 D 479 LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU
HET BR A1480 1
HET SO4 A1481 5
HET BR A1482 1
HET BR A1483 1
HET BR B1480 1
HET BR B1481 1
HET BR B1482 1
HET BR B1483 1
HET SO4 B1484 5
HET SO4 B1485 5
HET BR B1486 1
HET BR B1487 1
HET BR C1480 1
HET BR C1481 1
HET SO4 C1482 5
HET BR C1483 1
HET BR D1480 1
HET BR D1481 1
HET BR D1482 1
HET BR D1483 1
HET BR D1484 1
HET BR D1485 1
HET SO4 D1486 5
HET BR D1487 1
HETNAM BR BROMIDE ION
HETNAM SO4 SULFATE ION
FORMUL 5 BR 19(BR 1-)
FORMUL 6 SO4 5(O4 S 2-)
FORMUL 29 HOH *1648(H2 O)
HELIX 1 1 ALA A 19 GLU A 24 1 6
HELIX 2 2 TYR A 61 ALA A 66 1 6
HELIX 3 3 ASP A 68 GLY A 84 1 17
HELIX 4 4 ALA A 93 PHE A 98 1 6
HELIX 5 5 ASN A 107 TYR A 124 1 18
HELIX 6 6 PRO A 138 TYR A 145 1 8
HELIX 7 7 GLY A 146 ASN A 150 5 5
HELIX 8 8 ARG A 151 TYR A 168 1 18
HELIX 9 9 ASN A 182 ASN A 186 5 5
HELIX 10 10 LEU A 191 GLY A 198 1 8
HELIX 11 11 VAL A 200 HIS A 204 5 5
HELIX 12 12 ASN A 206 ASN A 233 1 28
HELIX 13 13 ASN A 253 MET A 264 1 12
HELIX 14 14 MET A 264 GLY A 277 1 14
HELIX 15 15 PRO A 280 GLY A 291 1 12
HELIX 16 16 GLY A 299 GLY A 307 1 9
HELIX 17 17 ASP A 354 GLN A 370 1 17
HELIX 18 18 ASP A 394 TYR A 414 1 21
HELIX 19 19 LYS A 462 SER A 474 1 13
HELIX 20 20 ALA B 19 GLU B 24 1 6
HELIX 21 21 ILE B 36 VAL B 39 5 4
HELIX 22 22 TYR B 61 ALA B 66 1 6
HELIX 23 23 ASP B 68 GLY B 84 1 17
HELIX 24 24 ALA B 93 PHE B 98 1 6
HELIX 25 25 ASN B 107 TYR B 124 1 18
HELIX 26 26 PRO B 138 GLY B 146 1 9
HELIX 27 27 SER B 147 ASN B 150 5 4
HELIX 28 28 ARG B 151 TYR B 168 1 18
HELIX 29 29 GLU B 180 ASN B 186 5 7
HELIX 30 30 LEU B 191 GLY B 198 1 8
HELIX 31 31 VAL B 200 HIS B 204 5 5
HELIX 32 32 ASN B 206 ASN B 233 1 28
HELIX 33 33 ASN B 253 MET B 264 1 12
HELIX 34 34 MET B 264 GLY B 277 1 14
HELIX 35 35 PRO B 280 ARG B 290 1 11
HELIX 36 36 GLY B 299 GLY B 307 1 9
HELIX 37 37 ASP B 354 GLN B 370 1 17
HELIX 38 38 ASP B 394 TYR B 414 1 21
HELIX 39 39 LYS B 462 SER B 474 1 13
HELIX 40 40 ALA C 19 GLU C 24 1 6
HELIX 41 41 ASP C 68 GLY C 84 1 17
HELIX 42 42 ALA C 93 PHE C 98 1 6
HELIX 43 43 ASN C 107 TYR C 124 1 18
HELIX 44 44 PRO C 138 GLY C 146 1 9
HELIX 45 45 SER C 147 THR C 149 5 3
HELIX 46 46 ASN C 150 TYR C 168 1 19
HELIX 47 47 ASN C 182 ASN C 186 5 5
HELIX 48 48 LEU C 191 GLY C 198 1 8
HELIX 49 49 VAL C 200 HIS C 204 5 5
HELIX 50 50 ASN C 206 ASN C 233 1 28
HELIX 51 51 ASN C 253 MET C 264 1 12
HELIX 52 52 MET C 264 GLY C 277 1 14
HELIX 53 53 PRO C 280 GLY C 291 1 12
HELIX 54 54 GLY C 299 GLY C 307 1 9
HELIX 55 55 ASP C 354 GLN C 370 1 17
HELIX 56 56 ASP C 394 TYR C 414 1 21
HELIX 57 57 LYS C 462 SER C 474 1 13
HELIX 58 58 ALA D 19 GLU D 24 1 6
HELIX 59 59 ILE D 36 VAL D 39 5 4
HELIX 60 60 TYR D 61 ALA D 66 1 6
HELIX 61 61 ASP D 68 GLY D 84 1 17
HELIX 62 62 ALA D 93 PHE D 98 1 6
HELIX 63 63 ASN D 107 TYR D 124 1 18
HELIX 64 64 PRO D 138 GLY D 146 1 9
HELIX 65 65 SER D 147 ASN D 150 5 4
HELIX 66 66 ARG D 151 TYR D 168 1 18
HELIX 67 67 GLU D 180 ASN D 186 5 7
HELIX 68 68 LEU D 191 GLY D 198 1 8
HELIX 69 69 VAL D 200 HIS D 204 5 5
HELIX 70 70 ASN D 206 ASN D 233 1 28
HELIX 71 71 ASN D 253 MET D 264 1 12
HELIX 72 72 MET D 264 GLY D 277 1 14
HELIX 73 73 PRO D 280 GLY D 291 1 12
HELIX 74 74 GLY D 299 GLY D 307 1 9
HELIX 75 75 ASP D 354 GLN D 370 1 17
HELIX 76 76 ASP D 394 TYR D 414 1 21
HELIX 77 77 LYS D 462 SER D 474 1 13
SHEET 1 AA 8 LEU A 13 TRP A 14 0
SHEET 2 AA 8 LEU A 419 TYR A 422 1 O MET A 420 N LEU A 13
SHEET 3 AA 8 LEU A 373 GLU A 377 1 O LEU A 373 N MET A 420
SHEET 4 AA 8 LEU A 312 SER A 315 1 O LEU A 312 N PHE A 374
SHEET 5 AA 8 LYS A 237 ALA A 243 1 O CYS A 240 N GLY A 313
SHEET 6 AA 8 TYR A 174 PHE A 178 1 O TRP A 175 N GLY A 239
SHEET 7 AA 8 GLU A 127 SER A 133 1 O PRO A 128 N TYR A 174
SHEET 8 AA 8 CYS A 87 SER A 91 1 O PHE A 88 N VAL A 129
SHEET 1 AB 3 LEU A 247 PRO A 249 0
SHEET 2 AB 3 ASN A 320 VAL A 322 1 O ASN A 320 N TYR A 248
SHEET 3 AB 3 SER A 338 VAL A 339 -1 O VAL A 339 N ALA A 321
SHEET 1 AC 2 LYS A 345 ALA A 346 0
SHEET 2 AC 2 GLN A 352 ILE A 353 -1 O ILE A 353 N LYS A 345
SHEET 1 AD 2 ILE A 445 VAL A 447 0
SHEET 2 AD 2 ARG A 459 ARG A 461 -1 O SER A 460 N TYR A 446
SHEET 1 BA 8 LEU B 13 TRP B 14 0
SHEET 2 BA 8 LEU B 419 TYR B 422 1 O MET B 420 N LEU B 13
SHEET 3 BA 8 LEU B 373 GLU B 377 1 O LEU B 373 N MET B 420
SHEET 4 BA 8 LEU B 312 SER B 315 1 O LEU B 312 N PHE B 374
SHEET 5 BA 8 LYS B 237 ALA B 243 1 O CYS B 240 N GLY B 313
SHEET 6 BA 8 TYR B 174 PHE B 178 1 O TRP B 175 N GLY B 239
SHEET 7 BA 8 GLU B 127 SER B 133 1 O PRO B 128 N TYR B 174
SHEET 8 BA 8 CYS B 87 SER B 91 1 O PHE B 88 N VAL B 129
SHEET 1 BB 3 LEU B 247 PRO B 249 0
SHEET 2 BB 3 ASN B 320 VAL B 322 1 O ASN B 320 N TYR B 248
SHEET 3 BB 3 SER B 338 VAL B 339 -1 O VAL B 339 N ALA B 321
SHEET 1 BC 2 ILE B 445 VAL B 447 0
SHEET 2 BC 2 ARG B 459 ARG B 461 -1 O SER B 460 N TYR B 446
SHEET 1 CA 9 LEU C 13 ALA C 17 0
SHEET 2 CA 9 LEU C 419 TYR C 422 1 O MET C 420 N LEU C 13
SHEET 3 CA 9 LEU C 373 GLU C 377 1 O LEU C 373 N MET C 420
SHEET 4 CA 9 TYR C 311 SER C 315 1 O LEU C 312 N PHE C 374
SHEET 5 CA 9 LYS C 237 ALA C 243 1 O CYS C 240 N GLY C 313
SHEET 6 CA 9 TYR C 174 PHE C 178 1 O TRP C 175 N GLY C 239
SHEET 7 CA 9 GLU C 127 SER C 133 1 O PRO C 128 N TYR C 174
SHEET 8 CA 9 CYS C 87 SER C 91 1 O PHE C 88 N VAL C 129
SHEET 9 CA 9 LEU C 13 ALA C 17 1 O GLY C 16 N ARG C 89
SHEET 1 CB 2 LEU C 247 PRO C 249 0
SHEET 2 CB 2 ASN C 320 VAL C 322 1 O ASN C 320 N TYR C 248
SHEET 1 CC 2 ILE C 445 VAL C 447 0
SHEET 2 CC 2 ARG C 459 ARG C 461 -1 O SER C 460 N TYR C 446
SHEET 1 DA 9 LEU D 13 ALA D 17 0
SHEET 2 DA 9 LEU D 419 TYR D 422 1 O MET D 420 N LEU D 13
SHEET 3 DA 9 LEU D 373 GLU D 377 1 O LEU D 373 N MET D 420
SHEET 4 DA 9 LEU D 312 SER D 315 1 O LEU D 312 N PHE D 374
SHEET 5 DA 9 LYS D 237 ALA D 243 1 O CYS D 240 N GLY D 313
SHEET 6 DA 9 TYR D 174 PHE D 178 1 O TRP D 175 N GLY D 239
SHEET 7 DA 9 GLU D 127 SER D 133 1 O PRO D 128 N TYR D 174
SHEET 8 DA 9 CYS D 87 SER D 91 1 O PHE D 88 N VAL D 129
SHEET 9 DA 9 LEU D 13 ALA D 17 1 O GLY D 16 N ARG D 89
SHEET 1 DB 3 LEU D 247 PRO D 249 0
SHEET 2 DB 3 ASN D 320 VAL D 322 1 O ASN D 320 N TYR D 248
SHEET 3 DB 3 SER D 338 VAL D 339 -1 O VAL D 339 N ALA D 321
SHEET 1 DC 2 LYS D 345 ALA D 346 0
SHEET 2 DC 2 GLN D 352 ILE D 353 -1 O ILE D 353 N LYS D 345
SHEET 1 DD 2 ILE D 445 LYS D 449 0
SHEET 2 DD 2 GLY D 455 ARG D 461 -1 N ASP D 456 O ASN D 448
SITE 1 AC1 1 LYS A 53
SITE 1 AC2 9 TRP A 351 SER A 432 PHE A 433 THR A 434
SITE 2 AC2 9 LYS A 440 TYR A 442 HOH A2368 HOH A2369
SITE 3 AC2 9 HOH A2370
SITE 1 AC3 2 SER A 439 HIS A 450
SITE 1 AC4 2 GLY A 299 LEU A 301
SITE 1 AC5 1 ARG B 231
SITE 1 AC6 1 LYS B 53
SITE 1 AC7 2 PRO B 190 LEU B 191
SITE 1 AC8 10 TRP B 351 SER B 432 PHE B 433 THR B 434
SITE 2 AC8 10 LYS B 440 TYR B 442 HOH B2354 HOH B2395
SITE 3 AC8 10 HOH B2396 HOH B2397
SITE 1 AC9 4 LEU B 247 SER B 263 GLU B 336 HOH B2398
SITE 1 BC1 4 GLY B 299 ASP B 300 LEU B 301 HOH B2281
SITE 1 BC2 4 ASN B 206 GLU B 208 GLU B 209 PHE B 292
SITE 1 BC3 2 SER C 439 HIS C 450
SITE 1 BC4 1 ALA C 104
SITE 1 BC5 10 TRP C 351 SER C 432 PHE C 433 THR C 434
SITE 2 BC5 10 LYS C 440 TYR C 442 HOH C2431 HOH C2477
SITE 3 BC5 10 HOH C2478 HOH C2479
SITE 1 BC6 2 LYS C 53 LYS D 295
SITE 1 BC7 2 LYS D 410 TYR D 414
SITE 1 BC8 2 GLU D 336 HOH D2292
SITE 1 BC9 4 SER D 439 HIS D 450 ASP D 451 HOH D2367
SITE 1 CC1 1 GLN D 144
SITE 1 CC2 2 PRO D 190 LEU D 191
SITE 1 CC3 4 ASN D 206 GLU D 208 GLU D 209 HOH D2206
SITE 1 CC4 8 TRP D 351 PHE D 433 THR D 434 LYS D 440
SITE 2 CC4 8 TYR D 442 HOH D2398 HOH D2399 HOH D2400
SITE 1 CC5 3 GLY D 299 LEU D 301 HOH D2274
CRYST1 73.674 79.424 98.604 99.96 107.21 102.83 P 1 4
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 0.013573 0.003091 0.005169 0.00000
SCALE2 0.000000 0.012913 0.003423 0.00000
SCALE3 0.000000 0.000000 0.010984 0.00000
MTRIX1 1 -0.007992 0.623400 -0.781900 37.38000 1
MTRIX2 1 0.629300 -0.604500 -0.488400 62.28000 1
MTRIX3 1 -0.777100 -0.496000 -0.387500 97.55000 1
(ATOM LINES ARE NOT SHOWN.)
END
