HEADER HYDROLASE 26-OCT-10 2XVG
TITLE CRYSTAL STRUCTURE OF ALPHA-XYLOSIDASE (GH31) FROM CELLVIBRIO JAPONICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA XYLOSIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CELLVIBRIO JAPONICUS;
SOURCE 3 ORGANISM_TAXID: 155077
KEYWDS HYDROLASE, GLYCOSYL HYDROLASE FAMILY 31, BETA/ALPHA 8 BARREL
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LARSBRINK,A.IZUMI,F.IBATULLIN,A.NAKHAI,H.J.GILBERT,G.J.DAVIES,
AUTHOR 2 H.BRUMER
REVDAT 3 20-DEC-23 2XVG 1 REMARK LINK
REVDAT 2 08-JUN-11 2XVG 1 JRNL
REVDAT 1 13-APR-11 2XVG 0
JRNL AUTH J.LARSBRINK,A.IZUMI,F.IBATULLIN,A.NAKHAI,H.J.GILBERT,
JRNL AUTH 2 G.J.DAVIES,H.BRUMER
JRNL TITL STRUCTURAL AND ENZYMATIC CHARACTERISATION OF A GLYCOSIDE
JRNL TITL 2 HYDROLASE FAMILY 31 ALPHA-XYLOSIDASE FROM CELLVIBRIO
JRNL TITL 3 JAPONICUS INVOLVED IN XYLOGLUCAN SACCHARIFICATION.
JRNL REF BIOCHEM.J. V. 436 567 2011
JRNL REFN ISSN 0264-6021
JRNL PMID 21426303
JRNL DOI 10.1042/BJ20110299
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 50969
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2587
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 49.8939 - 5.5992 0.99 5181 260 0.1935 0.2395
REMARK 3 2 5.5992 - 4.4452 1.00 4920 259 0.1377 0.2070
REMARK 3 3 4.4452 - 3.8835 1.00 4888 243 0.1492 0.2035
REMARK 3 4 3.8835 - 3.5285 1.00 4831 255 0.1975 0.2466
REMARK 3 5 3.5285 - 3.2757 1.00 4793 260 0.2189 0.2747
REMARK 3 6 3.2757 - 3.0826 1.00 4760 273 0.2561 0.3188
REMARK 3 7 3.0826 - 2.9282 1.00 4786 261 0.2743 0.3080
REMARK 3 8 2.9282 - 2.8008 1.00 4739 275 0.2785 0.3443
REMARK 3 9 2.8008 - 2.6930 1.00 4738 258 0.2794 0.3349
REMARK 3 10 2.6930 - 2.6000 1.00 4746 243 0.3005 0.3678
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 : 0.29
REMARK 3 B_SOL : 34.01
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.009 7798
REMARK 3 ANGLE : 1.156 10585
REMARK 3 CHIRALITY : 0.078 1095
REMARK 3 PLANARITY : 0.005 1387
REMARK 3 DIHEDRAL : 17.681 2773
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 45:169)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0662 75.4955 24.1358
REMARK 3 T TENSOR
REMARK 3 T11: 0.1560 T22: 1.2490
REMARK 3 T33: 0.3932 T12: 0.2432
REMARK 3 T13: -0.0516 T23: -0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 1.0135 L22: 1.9486
REMARK 3 L33: 1.4952 L12: -1.3518
REMARK 3 L13: -0.5031 L23: 0.2222
REMARK 3 S TENSOR
REMARK 3 S11: -0.1336 S12: -0.1101 S13: 0.4163
REMARK 3 S21: -0.0345 S22: 0.1179 S23: -0.5594
REMARK 3 S31: 0.1766 S32: 0.6906 S33: -0.0376
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 170:384)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4626 108.1292 33.7622
REMARK 3 T TENSOR
REMARK 3 T11: 0.1337 T22: 0.8391
REMARK 3 T33: 0.7111 T12: -0.1798
REMARK 3 T13: 0.0127 T23: -0.2819
REMARK 3 L TENSOR
REMARK 3 L11: 0.1535 L22: 1.3770
REMARK 3 L33: 0.7495 L12: -0.2679
REMARK 3 L13: 0.2220 L23: 0.5544
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.2233 S13: 0.6369
REMARK 3 S21: 0.0553 S22: 0.1445 S23: -0.3635
REMARK 3 S31: -0.2028 S32: 0.3600 S33: -0.1843
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 385:584)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3009 86.5695 42.1281
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.6561
REMARK 3 T33: 0.0596 T12: 0.1719
REMARK 3 T13: -0.0592 T23: -0.1170
REMARK 3 L TENSOR
REMARK 3 L11: 0.9906 L22: 0.9207
REMARK 3 L33: 0.5227 L12: -0.5490
REMARK 3 L13: 0.0397 L23: -0.0315
REMARK 3 S TENSOR
REMARK 3 S11: -0.1413 S12: -0.5309 S13: 0.0901
REMARK 3 S21: 0.3596 S22: 0.2690 S23: -0.1229
REMARK 3 S31: 0.0119 S32: 0.3483 S33: -0.1195
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 585:950)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7892 91.8023 23.6678
REMARK 3 T TENSOR
REMARK 3 T11: 0.1734 T22: 0.4379
REMARK 3 T33: 0.1139 T12: 0.0214
REMARK 3 T13: -0.0096 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.4354 L22: 1.3971
REMARK 3 L33: 0.4890 L12: -1.2085
REMARK 3 L13: 0.1767 L23: -0.1071
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: -0.0247 S13: 0.2522
REMARK 3 S21: 0.0229 S22: 0.0557 S23: -0.2186
REMARK 3 S31: 0.0263 S32: 0.3481 S33: -0.0344
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 951:989)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5357 84.0814 2.6507
REMARK 3 T TENSOR
REMARK 3 T11: 0.3637 T22: 0.6490
REMARK 3 T33: 0.1787 T12: 0.2342
REMARK 3 T13: -0.0628 T23: -0.0729
REMARK 3 L TENSOR
REMARK 3 L11: 1.0830 L22: 2.7987
REMARK 3 L33: 0.6088 L12: -0.7499
REMARK 3 L13: 0.5383 L23: 0.5152
REMARK 3 S TENSOR
REMARK 3 S11: 0.2385 S12: 0.3598 S13: -0.0103
REMARK 3 S21: -0.6059 S22: -0.1801 S23: 0.4904
REMARK 3 S31: -0.2441 S32: -0.0696 S33: 0.0476
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED SIDE CHAINS WERE MODELED
REMARK 3 STEREOCHEMICALLY AND HAVE ZERO OCCUPANCIES.
REMARK 4
REMARK 4 2XVG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1290045906.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : SI (311)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50969
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.30
REMARK 200 R MERGE FOR SHELL (I) : 0.81000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 2G3M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG MONOMETHYL ETHER 550 (PEG MME
REMARK 280 550), 0.1 M BIS-TRIS (PH 7.0)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.87950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 113.87950
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.87950
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 113.87950
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 113.87950
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 113.87950
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 LEU A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 HIS A 5
REMARK 465 GLN A 6
REMARK 465 TRP A 7
REMARK 465 LEU A 8
REMARK 465 ARG A 9
REMARK 465 HIS A 10
REMARK 465 CYS A 11
REMARK 465 ILE A 12
REMARK 465 ILE A 13
REMARK 465 GLY A 14
REMARK 465 VAL A 15
REMARK 465 ALA A 16
REMARK 465 SER A 17
REMARK 465 VAL A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 LEU A 21
REMARK 465 GLN A 22
REMARK 465 ALA A 23
REMARK 465 CYS A 24
REMARK 465 SER A 25
REMARK 465 LYS A 26
REMARK 465 GLN A 27
REMARK 465 THR A 28
REMARK 465 GLY A 29
REMARK 465 ASN A 30
REMARK 465 GLU A 31
REMARK 465 SER A 32
REMARK 465 SER A 33
REMARK 465 SER A 34
REMARK 465 SER A 35
REMARK 465 ALA A 36
REMARK 465 LYS A 37
REMARK 465 SER A 38
REMARK 465 ALA A 39
REMARK 465 THR A 40
REMARK 465 GLU A 41
REMARK 465 GLN A 42
REMARK 465 VAL A 43
REMARK 465 LYS A 44
REMARK 465 GLY A 255
REMARK 465 VAL A 990
REMARK 465 VAL A 991
REMARK 465 ILE A 992
REMARK 465 ASN A 993
REMARK 465 SER A 994
REMARK 465 LYS A 995
REMARK 465 LEU A 996
REMARK 465 GLU A 997
REMARK 465 GLY A 998
REMARK 465 LYS A 999
REMARK 465 PRO A 1000
REMARK 465 ILE A 1001
REMARK 465 PRO A 1002
REMARK 465 ASN A 1003
REMARK 465 PRO A 1004
REMARK 465 LEU A 1005
REMARK 465 LEU A 1006
REMARK 465 GLY A 1007
REMARK 465 LEU A 1008
REMARK 465 ASP A 1009
REMARK 465 SER A 1010
REMARK 465 THR A 1011
REMARK 465 ARG A 1012
REMARK 465 THR A 1013
REMARK 465 GLY A 1014
REMARK 465 HIS A 1015
REMARK 465 HIS A 1016
REMARK 465 HIS A 1017
REMARK 465 HIS A 1018
REMARK 465 HIS A 1019
REMARK 465 HIS A 1020
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 48 CG CD OE1 NE2
REMARK 480 LYS A 66 CD CE NZ
REMARK 480 GLU A 93 OE1 OE2
REMARK 480 ARG A 137 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 246 CG CD CE NZ
REMARK 480 LEU A 247 CG CD1 CD2
REMARK 480 GLU A 254 CD OE1 OE2
REMARK 480 ASN A 285 CG OD1 ND2
REMARK 480 GLU A 286 CG CD OE1 OE2
REMARK 480 GLN A 390 CG CD OE1 NE2
REMARK 480 LYS A 545 CD CE NZ
REMARK 480 LYS A 980 CE NZ
REMARK 480 LYS A 985 CD CE NZ
REMARK 480 ARG A 988 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 989 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 THR A 120 -168.75 -108.11
REMARK 500 ASP A 138 -171.93 -67.87
REMARK 500 GLU A 148 -76.17 -82.63
REMARK 500 ASN A 149 -163.41 -102.50
REMARK 500 HIS A 158 48.34 -83.58
REMARK 500 LEU A 185 -13.26 78.92
REMARK 500 ASP A 249 -150.08 -75.97
REMARK 500 GLN A 283 -76.58 -125.45
REMARK 500 PRO A 292 150.38 -46.29
REMARK 500 MET A 345 141.85 -32.21
REMARK 500 ASP A 373 36.86 33.21
REMARK 500 HIS A 381 147.37 -174.92
REMARK 500 PRO A 386 159.51 -42.39
REMARK 500 HIS A 391 71.33 -108.82
REMARK 500 SER A 472 26.91 81.78
REMARK 500 ALA A 478 35.92 -143.46
REMARK 500 ASP A 485 124.67 -32.54
REMARK 500 ASP A 541 -158.29 -73.10
REMARK 500 ASN A 591 11.06 85.74
REMARK 500 ILE A 612 20.96 -145.34
REMARK 500 SER A 662 62.29 -61.44
REMARK 500 ALA A 714 -52.38 -27.74
REMARK 500 TYR A 784 -65.47 -91.31
REMARK 500 LYS A 826 -5.89 77.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A1999 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 500 ND1
REMARK 620 2 HOH A2015 O 108.0
REMARK 620 3 HOH A2016 O 137.5 80.3
REMARK 620 4 HOH A2040 O 143.8 87.0 76.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A1998 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 882 NE2
REMARK 620 2 CL A1990 CL 122.9
REMARK 620 3 CL A1991 CL 108.4 75.0
REMARK 620 4 CL A1992 CL 127.9 108.7 90.4
REMARK 620 5 CL A1993 CL 122.4 68.4 127.8 68.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1990
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1991
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1992
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1993
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1994
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1995
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1996
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1998
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XVK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHA-XYLOSIDASE (GH31) FROM CELLVIBRIO
REMARK 900 JAPONICUS IN COMPLEX WITH 5 -FLUORO-ALPHA-D-XYLOPYRANOSYL FLUORIDE
REMARK 900 RELATED ID: 2XVL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHA-XYLOSIDASE (GH31) FROM CELLVIBRIO
REMARK 900 JAPONICUS IN COMPLEX WITH PENTAERYTHRITOL PROPOXYLATE (5 4 PO OH)
DBREF 2XVG A 1 988 UNP B3PBD9 B3PBD9_CELJU 1 988
SEQADV 2XVG LYS A 989 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG VAL A 990 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG VAL A 991 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG ILE A 992 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG ASN A 993 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG SER A 994 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG LYS A 995 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG LEU A 996 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG GLU A 997 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG GLY A 998 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG LYS A 999 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG PRO A 1000 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG ILE A 1001 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG PRO A 1002 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG ASN A 1003 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG PRO A 1004 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG LEU A 1005 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG LEU A 1006 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG GLY A 1007 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG LEU A 1008 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG ASP A 1009 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG SER A 1010 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG THR A 1011 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG ARG A 1012 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG THR A 1013 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG GLY A 1014 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG HIS A 1015 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG HIS A 1016 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG HIS A 1017 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG HIS A 1018 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG HIS A 1019 UNP B3PBD9 EXPRESSION TAG
SEQADV 2XVG HIS A 1020 UNP B3PBD9 EXPRESSION TAG
SEQRES 1 A 1020 MET LEU SER ALA HIS GLN TRP LEU ARG HIS CYS ILE ILE
SEQRES 2 A 1020 GLY VAL ALA SER VAL ALA LEU LEU GLN ALA CYS SER LYS
SEQRES 3 A 1020 GLN THR GLY ASN GLU SER SER SER SER ALA LYS SER ALA
SEQRES 4 A 1020 THR GLU GLN VAL LYS ALA LEU ALA GLN VAL GLU ARG THR
SEQRES 5 A 1020 ALA GLU GLY VAL VAL LEU THR LEU PRO GLU GLY THR VAL
SEQRES 6 A 1020 LYS LYS LEU ARG LEU GLN VAL MET GLY GLU ARG ILE ILE
SEQRES 7 A 1020 ARG VAL THR ALA LEU PRO GLY THR ASP PHE GLY ILE VAL
SEQRES 8 A 1020 PRO GLU SER ILE GLN VAL VAL ALA LYS PRO ALA THR ASN
SEQRES 9 A 1020 VAL PRO PHE SER VAL ASP GLN ALA GLY GLU LYS LEU VAL
SEQRES 10 A 1020 LEU LYS THR SER GLN VAL SER ALA GLU VAL SER LEU LEU
SEQRES 11 A 1020 ASP GLY THR VAL SER PHE ARG ASP ALA LYS GLY ASN VAL
SEQRES 12 A 1020 LEU LEU GLN GLU GLU ASN ARG GLY THR PHE SER PRO VAL
SEQRES 13 A 1020 ILE HIS ASP PRO ASP PRO VAL ASP ALA ASP SER TYR ALA
SEQRES 14 A 1020 LEU ARG GLN GLU PHE ASN ARG GLY SER ASP GLU GLY PHE
SEQRES 15 A 1020 PHE GLY LEU GLY GLN HIS GLN ASN GLY GLN VAL ASN TYR
SEQRES 16 A 1020 ALA GLY GLU ASN VAL GLU LEU THR THR TYR ASN LEU VAL
SEQRES 17 A 1020 ILE SER ILE PRO PHE LEU VAL SER SER ARG ASN TYR GLY
SEQRES 18 A 1020 LEU LEU TRP ASP ASN ASN SER ILE THR ARG PHE GLY ASP
SEQRES 19 A 1020 PRO ARG GLU ALA GLN PRO LEU ASN GLN SER LEU LYS LEU
SEQRES 20 A 1020 TYR ASP ALA GLU GLY LYS GLU GLY GLY LEU THR VAL ARG
SEQRES 21 A 1020 TYR PHE VAL GLY ASP GLU LEU LYS LEU THR ARG VAL GLU
SEQRES 22 A 1020 ALA ASP PHE ASN HIS GLN PHE TYR LYS GLN GLY ASN GLU
SEQRES 23 A 1020 LEU GLU ASN PRO PHE PRO GLU GLU VAL ALA GLY ALA TYR
SEQRES 24 A 1020 LYS ASN ASN THR LEU ARG ILE GLU LEU GLU GLY SER ILE
SEQRES 25 A 1020 GLU ALA GLN ALA THR GLY LYS HIS GLN PHE LYS MET TYR
SEQRES 26 A 1020 ASN SER GLY TYR ALA GLN LEU SER LEU ASP GLY GLU VAL
SEQRES 27 A 1020 VAL LEU ASP ARG TRP ARG MET ASN TRP ASN PRO TRP TYR
SEQRES 28 A 1020 HIS ASN PHE TYR ARG GLU LEU ASN ALA GLY ASP LYS HIS
SEQRES 29 A 1020 LYS LEU LYS VAL SER TRP LYS PRO ASP GLY GLY PHE PHE
SEQRES 30 A 1020 HIS LEU ARG HIS LEU ASP PRO LEU PRO ALA ASN GLU GLN
SEQRES 31 A 1020 HIS GLU LEU SER LEU ALA SER GLU THR GLY LYS ALA ILE
SEQRES 32 A 1020 ASP TYR TYR PHE VAL ALA GLY ASP THR LYS ASP ASP ILE
SEQRES 33 A 1020 ILE SER GLY TYR ARG GLN LEU THR GLY LYS SER VAL MET
SEQRES 34 A 1020 LEU PRO LYS TRP ALA TYR GLY PHE TRP GLN SER ARG GLU
SEQRES 35 A 1020 ARG TYR LYS SER SER ASP GLU ILE ILE GLN ASN LEU LYS
SEQRES 36 A 1020 GLU TYR ARG ASP ARG LYS ILE PRO ILE ASP ASN ILE VAL
SEQRES 37 A 1020 LEU ASP TRP SER TYR TRP PRO GLU ASP ALA TRP GLY SER
SEQRES 38 A 1020 HIS ASP PHE ASP LYS GLN PHE PHE PRO ASP PRO LYS ALA
SEQRES 39 A 1020 LEU VAL ASP LYS VAL HIS ALA MET ASN ALA GLN ILE MET
SEQRES 40 A 1020 ILE SER VAL TRP PRO LYS PHE TYR PRO THR THR ASP ASN
SEQRES 41 A 1020 TYR LYS GLU LEU ASN ALA LYS GLY PHE MET PHE ASN ARG
SEQRES 42 A 1020 ASN LEU ASP GLU LYS ASN LEU ASP TRP ILE GLY LYS GLY
SEQRES 43 A 1020 TYR LEU ASN ALA PHE TYR ASP PRO PHE SER PRO GLU ALA
SEQRES 44 A 1020 THR ALA ILE PHE TRP LYS GLN ILE ARG ASP LYS ILE ASN
SEQRES 45 A 1020 VAL HIS GLY PHE ASP ALA TRP TRP LEU ASP ALA VAL GLU
SEQRES 46 A 1020 PRO ASP ILE HIS SER ASN LEU THR PHE GLU LYS ARG LYS
SEQRES 47 A 1020 TRP LEU MET THR PRO ASN ALA ARG GLY ASN GLY ALA GLU
SEQRES 48 A 1020 ILE PHE ASN ALA TYR ALA VAL PRO HIS ALA GLU GLY VAL
SEQRES 49 A 1020 TYR GLN GLY GLU LEU ALA THR ASP GLY ASP LYS ARG SER
SEQRES 50 A 1020 PHE ILE LEU THR ARG SER GLY PHE GLY GLY ILE GLN ARG
SEQRES 51 A 1020 THR GLY SER ALA ILE TRP SER GLY ASP ILE VAL SER ARG
SEQRES 52 A 1020 TRP SER ASP MET LYS ASP GLN ILE ALA ALA GLY ILE GLY
SEQRES 53 A 1020 THR ASN LEU ALA GLY VAL THR ASN TRP THR PHE ASP ILE
SEQRES 54 A 1020 GLY GLY PHE THR PRO GLU ASP ARG PHE ARG HIS GLY LYS
SEQRES 55 A 1020 LYS GLY PHE VAL GLY SER TRP THR ALA LEU ASP ALA GLU
SEQRES 56 A 1020 GLN VAL ASP GLU TRP GLN GLU LEU ASN THR ARG TRP TYR
SEQRES 57 A 1020 GLN PHE GLY ALA PHE VAL PRO LEU TYR ARG SER HIS GLY
SEQRES 58 A 1020 GLN ASN PRO TYR ARG GLU ILE PHE ASN ILE ALA ASP GLU
SEQRES 59 A 1020 GLY THR GLU VAL TYR ASN ALA MET VAL TRP TYR THR LYS
SEQRES 60 A 1020 LEU ARG TYR TYR LEU MET PRO TYR ILE TYR THR LEU GLY
SEQRES 61 A 1020 GLY ASP THR TYR HIS LYS ASP GLY THR ILE MET ARG GLY
SEQRES 62 A 1020 LEU VAL MET ASP PHE PRO ASN ASP ARG LYS ALA TRP ASP
SEQRES 63 A 1020 ILE ASN THR GLN TYR MET PHE GLY PRO ALA PHE LEU VAL
SEQRES 64 A 1020 ASN PRO VAL TYR GLU TYR LYS ALA ARG SER ARG ASP VAL
SEQRES 65 A 1020 TYR LEU PRO ALA GLY SER ASP TRP TYR ASN PHE TYR THR
SEQRES 66 A 1020 GLY GLU LYS LEU ALA GLY GLY GLN THR ILE THR ALA ASP
SEQRES 67 A 1020 ALA PRO LEU ALA ARG VAL PRO LEU PHE VAL LYS ALA GLY
SEQRES 68 A 1020 ALA ILE VAL PRO THR GLY PRO LEU ILE GLN HIS VAL ASP
SEQRES 69 A 1020 GLU GLY LEU ASN SER PRO LEU LEU ILE THR VAL TYR THR
SEQRES 70 A 1020 GLY ALA ASN GLY SER PHE ASP ILE TYR GLU ASP ASP GLY
SEQRES 71 A 1020 ARG SER LEU LYS TYR GLN GLN GLY GLU TRP SER ARG ILE
SEQRES 72 A 1020 PRO LEU SER TYR ASP ASP VAL THR GLY THR LEU ILE ILE
SEQRES 73 A 1020 GLY ASP ARG VAL GLY SER PHE THR GLY MET ALA ASP GLU
SEQRES 74 A 1020 ARG ASN ILE ARG VAL ARG PHE ILE ALA GLY PRO THR ALA
SEQRES 75 A 1020 ASP ALA THR ASN PHE ASP LYS ALA ALA ALA GLU ALA VAL
SEQRES 76 A 1020 THR TYR THR GLY LYS SER VAL SER ILE LYS ARG PRO ARG
SEQRES 77 A 1020 LYS VAL VAL ILE ASN SER LYS LEU GLU GLY LYS PRO ILE
SEQRES 78 A 1020 PRO ASN PRO LEU LEU GLY LEU ASP SER THR ARG THR GLY
SEQRES 79 A 1020 HIS HIS HIS HIS HIS HIS
HET CL A1990 1
HET CL A1991 1
HET CL A1992 1
HET CL A1993 1
HET EDO A1994 4
HET SO4 A1995 5
HET EDO A1996 4
HET EDO A1997 4
HET NI A1998 1
HET NI A1999 1
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM NI NICKEL (II) ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CL 4(CL 1-)
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 7 SO4 O4 S 2-
FORMUL 10 NI 2(NI 2+)
FORMUL 12 HOH *103(H2 O)
HELIX 1 1 ASP A 87 VAL A 91 5 5
HELIX 2 2 PRO A 292 GLU A 294 5 3
HELIX 3 3 VAL A 295 ASN A 301 1 7
HELIX 4 4 THR A 412 GLY A 425 1 14
HELIX 5 5 PRO A 431 TYR A 435 5 5
HELIX 6 6 SER A 446 ARG A 460 1 15
HELIX 7 7 ASP A 491 MET A 502 1 12
HELIX 8 8 THR A 518 LYS A 527 1 10
HELIX 9 9 ASN A 532 GLU A 537 1 6
HELIX 10 10 SER A 556 ILE A 571 1 16
HELIX 11 11 ASN A 572 GLY A 575 5 4
HELIX 12 12 THR A 593 MET A 601 1 9
HELIX 13 13 GLY A 609 PHE A 613 5 5
HELIX 14 14 TYR A 616 ASP A 632 1 17
HELIX 15 15 GLY A 647 THR A 651 5 5
HELIX 16 16 ARG A 663 LEU A 679 1 17
HELIX 17 17 GLU A 695 ARG A 699 1 5
HELIX 18 18 SER A 708 LEU A 712 5 5
HELIX 19 19 ASP A 713 GLU A 715 5 3
HELIX 20 20 GLN A 716 ALA A 732 1 17
HELIX 21 21 GLU A 747 ALA A 752 1 6
HELIX 22 22 THR A 756 LEU A 772 1 17
HELIX 23 23 LEU A 772 LYS A 786 1 15
HELIX 24 24 GLY A 793 PHE A 798 1 6
HELIX 25 25 ASP A 801 ILE A 807 1 7
HELIX 26 26 HIS A 882 LEU A 887 5 6
HELIX 27 27 LEU A 913 GLY A 918 5 6
SHEET 1 AA 8 GLN A 48 ARG A 51 0
SHEET 2 AA 8 GLY A 55 THR A 59 -1 O VAL A 57 N GLU A 50
SHEET 3 AA 8 LYS A 67 GLY A 74 -1 O LEU A 68 N LEU A 58
SHEET 4 AA 8 ILE A 77 LEU A 83 -1 O ILE A 77 N MET A 73
SHEET 5 AA 8 ILE A 403 ALA A 409 -1 O ILE A 403 N ALA A 82
SHEET 6 AA 8 TYR A 220 TRP A 224 -1 O GLY A 221 N VAL A 408
SHEET 7 AA 8 ILE A 209 SER A 216 -1 O PRO A 212 N TRP A 224
SHEET 8 AA 8 PHE A 182 GLN A 187 -1 O PHE A 183 N VAL A 215
SHEET 1 AB 5 SER A 108 ALA A 112 0
SHEET 2 AB 5 LYS A 115 LYS A 119 -1 O LYS A 115 N ALA A 112
SHEET 3 AB 5 SER A 124 SER A 128 -1 O ALA A 125 N LEU A 118
SHEET 4 AB 5 VAL A 134 ARG A 137 -1 O SER A 135 N GLU A 126
SHEET 5 AB 5 VAL A 143 GLN A 146 -1 N LEU A 144 O PHE A 136
SHEET 1 AC 4 GLN A 172 PHE A 174 0
SHEET 2 AC 4 LEU A 393 SER A 397 -1 O LEU A 393 N PHE A 174
SHEET 3 AC 4 THR A 230 PHE A 232 -1 O ARG A 231 N ALA A 396
SHEET 4 AC 4 VAL A 200 LEU A 202 -1 O VAL A 200 N PHE A 232
SHEET 1 AD 2 GLN A 239 PRO A 240 0
SHEET 2 AD 2 PHE A 377 LEU A 382 -1 O HIS A 381 N GLN A 239
SHEET 1 AE 2 ASN A 277 HIS A 278 0
SHEET 2 AE 2 PHE A 377 LEU A 382 1 O PHE A 377 N HIS A 278
SHEET 1 AF 4 TRP A 350 LEU A 358 0
SHEET 2 AF 4 GLY A 318 ASN A 326 -1 O GLY A 318 N LEU A 358
SHEET 3 AF 4 PHE A 377 LEU A 382 -1 O HIS A 378 N TYR A 325
SHEET 4 AF 4 ASN A 277 HIS A 278 1 O HIS A 278 N PHE A 377
SHEET 1 AG 4 TRP A 350 LEU A 358 0
SHEET 2 AG 4 GLY A 318 ASN A 326 -1 O GLY A 318 N LEU A 358
SHEET 3 AG 4 PHE A 377 LEU A 382 -1 O HIS A 378 N TYR A 325
SHEET 4 AG 4 GLN A 239 PRO A 240 -1 O GLN A 239 N HIS A 381
SHEET 1 AH 2 LEU A 245 TYR A 248 0
SHEET 2 AH 2 LEU A 304 ALA A 314 1 O SER A 311 N TYR A 248
SHEET 1 AI 6 GLU A 266 GLU A 273 0
SHEET 2 AI 6 LEU A 257 VAL A 263 -1 O LEU A 257 N GLU A 273
SHEET 3 AI 6 LEU A 304 ALA A 314 -1 O ARG A 305 N PHE A 262
SHEET 4 AI 6 HIS A 364 LYS A 371 -1 O HIS A 364 N ILE A 312
SHEET 5 AI 6 GLY A 328 LEU A 334 -1 O TYR A 329 N LYS A 371
SHEET 6 AI 6 VAL A 338 ARG A 344 -1 N VAL A 339 O LEU A 332
SHEET 1 AJ 4 GLU A 266 GLU A 273 0
SHEET 2 AJ 4 LEU A 257 VAL A 263 -1 O LEU A 257 N GLU A 273
SHEET 3 AJ 4 LEU A 304 ALA A 314 -1 O ARG A 305 N PHE A 262
SHEET 4 AJ 4 LEU A 245 TYR A 248 1 O LYS A 246 N GLU A 313
SHEET 1 AK 8 TRP A 685 THR A 686 0
SHEET 2 AK 8 SER A 653 TRP A 656 1 O ILE A 655 N THR A 686
SHEET 3 AK 8 ILE A 639 THR A 641 1 O ILE A 639 N ALA A 654
SHEET 4 AK 8 ALA A 578 LEU A 581 1 O TRP A 579 N LEU A 640
SHEET 5 AK 8 GLN A 505 SER A 509 1 O ILE A 508 N TRP A 580
SHEET 6 AK 8 ASN A 466 LEU A 469 1 O ILE A 467 N MET A 507
SHEET 7 AK 8 PHE A 437 GLN A 439 1 O GLN A 439 N VAL A 468
SHEET 8 AK 8 TYR A 737 SER A 739 1 O TYR A 737 N TRP A 438
SHEET 1 AL 3 LYS A 513 PHE A 514 0
SHEET 2 AL 3 ALA A 550 TYR A 552 -1 O ALA A 550 N PHE A 514
SHEET 3 AL 3 MET A 530 PHE A 531 -1 O PHE A 531 N PHE A 551
SHEET 1 AM 2 HIS A 700 GLY A 701 0
SHEET 2 AM 2 GLY A 704 PHE A 705 -1 O GLY A 704 N GLY A 701
SHEET 1 AN 6 MET A 791 ARG A 792 0
SHEET 2 AN 6 TYR A 811 PHE A 813 -1 O MET A 812 N ARG A 792
SHEET 3 AN 6 PHE A 817 VAL A 819 -1 O PHE A 817 N PHE A 813
SHEET 4 AN 6 LEU A 866 LYS A 869 -1 O PHE A 867 N LEU A 818
SHEET 5 AN 6 ASP A 839 ASN A 842 -1 O TYR A 841 N VAL A 868
SHEET 6 AN 6 LYS A 848 ALA A 850 -1 O LEU A 849 N TRP A 840
SHEET 1 AO 2 SER A 829 LEU A 834 0
SHEET 2 AO 2 GLN A 853 ASP A 858 -1 O GLN A 853 N LEU A 834
SHEET 1 AP 4 ILE A 873 THR A 876 0
SHEET 2 AP 4 LEU A 891 TYR A 896 -1 O LEU A 892 N THR A 876
SHEET 3 AP 4 ARG A 950 ILE A 957 1 O ASN A 951 N LEU A 891
SHEET 4 AP 4 GLU A 973 TYR A 977 -1 O GLU A 973 N VAL A 954
SHEET 1 AQ 2 GLY A 901 GLU A 907 0
SHEET 2 AQ 2 TRP A 920 ASP A 928 -1 O SER A 921 N GLU A 907
SHEET 1 AR 2 VAL A 940 SER A 942 0
SHEET 2 AR 2 TRP A 920 ASP A 928 1 O TRP A 920 N SER A 942
SHEET 1 AS 4 VAL A 982 LYS A 985 0
SHEET 2 AS 4 THR A 933 ILE A 936 -1 O LEU A 934 N ILE A 984
SHEET 3 AS 4 TRP A 920 ASP A 928 -1 O SER A 926 N ILE A 935
SHEET 4 AS 4 VAL A 940 SER A 942 1 O VAL A 940 N ARG A 922
SHEET 1 AT 4 VAL A 982 LYS A 985 0
SHEET 2 AT 4 THR A 933 ILE A 936 -1 O LEU A 934 N ILE A 984
SHEET 3 AT 4 TRP A 920 ASP A 928 -1 O SER A 926 N ILE A 935
SHEET 4 AT 4 GLY A 901 GLU A 907 -1 O GLY A 901 N TYR A 927
LINK ND1 HIS A 500 NI NI A1999 1555 1555 2.18
LINK NE2 HIS A 882 NI NI A1998 1555 1555 2.01
LINK CL CL A1990 NI NI A1998 1555 1555 2.32
LINK CL CL A1991 NI NI A1998 1555 1555 2.20
LINK CL CL A1992 NI NI A1998 1555 1555 2.33
LINK CL CL A1993 NI NI A1998 1555 1555 2.32
LINK NI NI A1999 O HOH A2015 1555 1555 2.67
LINK NI NI A1999 O HOH A2016 1555 1555 2.24
LINK NI NI A1999 O HOH A2040 1555 1555 2.52
CISPEP 1 GLU A 442 ARG A 443 0 0.33
CISPEP 2 GLU A 585 PRO A 586 0 -1.31
CISPEP 3 THR A 602 PRO A 603 0 -1.70
CISPEP 4 ASN A 743 PRO A 744 0 8.01
SITE 1 AC1 6 GLU A 754 CL A1991 CL A1993 NI A1998
SITE 2 AC1 6 HOH A2014 HOH A2033
SITE 1 AC2 7 ASN A 503 GLU A 754 HIS A 882 CL A1990
SITE 2 AC2 7 CL A1992 NI A1998 HOH A2033
SITE 1 AC3 5 ASN A 503 CL A1991 CL A1993 NI A1998
SITE 2 AC3 5 HOH A2033
SITE 1 AC4 5 GLU A 885 CL A1990 CL A1992 NI A1998
SITE 2 AC4 5 HOH A2014
SITE 1 AC5 2 TRP A 542 EDO A1997
SITE 1 AC6 1 ASP A 164
SITE 1 AC7 2 PHE A 107 HOH A2103
SITE 1 AC8 2 TRP A 542 EDO A1994
SITE 1 AC9 7 ASN A 503 HIS A 882 CL A1990 CL A1991
SITE 2 AC9 7 CL A1992 CL A1993 HOH A2033
SITE 1 BC1 4 HIS A 500 HOH A2015 HOH A2016 HOH A2040
CRYST1 156.193 156.193 227.759 90.00 90.00 120.00 P 63 2 2 12
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 0.006402 0.003696 0.000000 0.00000
SCALE2 0.000000 0.007393 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004391 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
