HEADER HYDROLASE 16-OCT-14 4V33
TITLE CRYSTAL STRUCTURE OF THE PUTATIVE POLYSACCHARIDE DEACETYLASE BA0330
TITLE 2 FROM BACILLUS ANTHRACIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYSACCHARIDE DEACETYLASE-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: POLYSACCHARIDE DEACETYLASE BA0330;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: HYDROXY PROLINE IN POSITION 302
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 1392;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE, FIBRONECTIN TYPE III DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GIASTAS,A.ANDREOU,V.BOURIOTIS,E.ELIOPOULOS
REVDAT 4 10-JAN-24 4V33 1 REMARK SHEET LINK
REVDAT 3 10-JUN-15 4V33 1 JRNL
REVDAT 2 15-APR-15 4V33 1 JRNL
REVDAT 1 08-APR-15 4V33 0
JRNL AUTH S.ARNAOUTELI,P.GIASTAS,A.ANDREOU,M.TZANODASKALAKI,
JRNL AUTH 2 C.ALDRIDGE,S.J.TZARTOS,W.VOLLMER,E.ELIOPOULOS,V.BOURIOTIS
JRNL TITL TWO PUTATIVE POLYSACCHARIDE DEACETYLASES ARE REQUIRED FOR
JRNL TITL 2 OSMOTIC STABILITY AND CELL SHAPE MAINTENANCE IN BACILLUS
JRNL TITL 3 ANTHRACIS.
JRNL REF J.BIOL.CHEM. V. 290 13465 2015
JRNL REFN ISSN 0021-9258
JRNL PMID 25825488
JRNL DOI 10.1074/JBC.M115.640029
REMARK 2
REMARK 2 RESOLUTION. 1.48 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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 155203
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 14922
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 48.0468 - 4.5966 0.96 9612 500 0.1409 0.1516
REMARK 3 2 4.5966 - 3.6489 0.95 9577 498 0.1278 0.1471
REMARK 3 3 3.6489 - 3.1878 0.95 9570 497 0.1468 0.1671
REMARK 3 4 3.1878 - 2.8963 0.95 9612 512 0.1532 0.1735
REMARK 3 5 2.8963 - 2.6888 0.95 9500 491 0.1522 0.1601
REMARK 3 6 2.6888 - 2.5302 0.96 9685 518 0.1517 0.1615
REMARK 3 7 2.5302 - 2.4035 0.95 9580 502 0.1499 0.1768
REMARK 3 8 2.4035 - 2.2989 0.96 9545 503 0.1380 0.1664
REMARK 3 9 2.2989 - 2.2104 0.96 9667 507 0.1474 0.1713
REMARK 3 10 2.2104 - 2.1341 0.96 9637 508 0.1484 0.1647
REMARK 3 11 2.1341 - 2.0674 0.96 9622 509 0.1580 0.1783
REMARK 3 12 2.0674 - 2.0083 0.96 9516 495 0.1523 0.1772
REMARK 3 13 2.0083 - 1.9554 0.95 9633 503 0.1485 0.1689
REMARK 3 14 1.9554 - 1.9077 0.95 9530 503 0.1475 0.1702
REMARK 3 15 1.9077 - 1.8644 0.95 9604 509 0.1512 0.1800
REMARK 3 16 1.8644 - 1.8247 0.95 9505 499 0.1550 0.1627
REMARK 3 17 1.8247 - 1.7882 0.95 9429 493 0.1655 0.1899
REMARK 3 18 1.7882 - 1.7544 0.94 9553 499 0.1721 0.1807
REMARK 3 19 1.7544 - 1.7231 0.95 9534 494 0.1756 0.2069
REMARK 3 20 1.7231 - 1.6939 0.94 9400 495 0.1896 0.2171
REMARK 3 21 1.6939 - 1.6666 0.94 9562 494 0.1868 0.1982
REMARK 3 22 1.6666 - 1.6409 0.94 9387 484 0.1843 0.1905
REMARK 3 23 1.6409 - 1.6168 0.94 9452 497 0.1855 0.1967
REMARK 3 24 1.6168 - 1.5940 0.94 9467 503 0.1961 0.2222
REMARK 3 25 1.5940 - 1.5725 0.93 9320 484 0.2096 0.2335
REMARK 3 26 1.5725 - 1.5520 0.93 9477 500 0.2258 0.2289
REMARK 3 27 1.5520 - 1.5326 0.93 9154 482 0.2333 0.2532
REMARK 3 28 1.5326 - 1.5142 0.93 9465 503 0.2522 0.2693
REMARK 3 29 1.5142 - 1.4966 0.92 9159 481 0.2619 0.2860
REMARK 3 30 1.4966 - 1.4798 0.86 8819 459 0.2799 0.2921
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.20
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 : 0.010 5279
REMARK 3 ANGLE : 1.024 7132
REMARK 3 CHIRALITY : 0.070 791
REMARK 3 PLANARITY : 0.005 905
REMARK 3 DIHEDRAL : 12.650 2009
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 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6759 33.3366 62.2485
REMARK 3 T TENSOR
REMARK 3 T11: 0.1976 T22: 0.3013
REMARK 3 T33: 0.1511 T12: 0.0275
REMARK 3 T13: 0.0214 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 0.9154 L22: 0.6418
REMARK 3 L33: 3.0383 L12: 0.3458
REMARK 3 L13: -1.4735 L23: -1.1285
REMARK 3 S TENSOR
REMARK 3 S11: -0.1935 S12: -0.3016 S13: -0.1718
REMARK 3 S21: 0.0191 S22: -0.0267 S23: -0.0951
REMARK 3 S31: 0.2688 S32: 0.3665 S33: 0.2004
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1429 50.7550 32.2788
REMARK 3 T TENSOR
REMARK 3 T11: 0.1055 T22: 0.1233
REMARK 3 T33: 0.1166 T12: -0.0476
REMARK 3 T13: 0.0148 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.7910 L22: 1.2988
REMARK 3 L33: 2.0483 L12: 0.0471
REMARK 3 L13: 0.5965 L23: 0.2835
REMARK 3 S TENSOR
REMARK 3 S11: -0.0178 S12: 0.0421 S13: 0.0989
REMARK 3 S21: -0.1199 S22: 0.0595 S23: 0.0638
REMARK 3 S31: -0.1575 S32: 0.0136 S33: -0.0361
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 360 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1072 54.9730 36.1181
REMARK 3 T TENSOR
REMARK 3 T11: 0.1202 T22: 0.1617
REMARK 3 T33: 0.0841 T12: -0.0316
REMARK 3 T13: 0.0211 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.5114 L22: 0.9631
REMARK 3 L33: 1.1946 L12: 0.5234
REMARK 3 L13: 0.0044 L23: -0.3373
REMARK 3 S TENSOR
REMARK 3 S11: 0.0593 S12: -0.1976 S13: 0.0705
REMARK 3 S21: 0.0872 S22: -0.0701 S23: 0.0239
REMARK 3 S31: -0.0903 S32: 0.0958 S33: 0.0127
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9260 31.5403 -5.0991
REMARK 3 T TENSOR
REMARK 3 T11: 0.2781 T22: 0.1211
REMARK 3 T33: 0.2723 T12: -0.0283
REMARK 3 T13: -0.1219 T23: -0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 1.2018 L22: 1.6896
REMARK 3 L33: 0.4750 L12: -0.4052
REMARK 3 L13: -0.3242 L23: -0.3885
REMARK 3 S TENSOR
REMARK 3 S11: 0.2525 S12: 0.2834 S13: -0.2473
REMARK 3 S21: -0.5463 S22: -0.0293 S23: 0.4380
REMARK 3 S31: 0.2648 S32: -0.1484 S33: -0.0749
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 180 THROUGH 360 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7821 36.2525 11.6091
REMARK 3 T TENSOR
REMARK 3 T11: 0.1136 T22: 0.0674
REMARK 3 T33: 0.1070 T12: -0.0038
REMARK 3 T13: 0.0001 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 1.0830 L22: 0.5817
REMARK 3 L33: 0.5533 L12: 0.4502
REMARK 3 L13: 0.0898 L23: -0.0818
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: -0.0364 S13: 0.0217
REMARK 3 S21: -0.0004 S22: -0.0158 S23: 0.0346
REMARK 3 S31: -0.0046 S32: 0.0119 S33: 0.0085
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 1-44 WERE NOT LOCATED IN THE
REMARK 3 EXPERIMENT
REMARK 4
REMARK 4 4V33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1290062009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155207
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 48.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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 4HD5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 6.5, 20%
REMARK 280 PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 54.48200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.38150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 54.48200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.38150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2035 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2076 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 LYS A 3
REMARK 465 TYR A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 ILE A 7
REMARK 465 ALA A 8
REMARK 465 LEU A 9
REMARK 465 CYS A 10
REMARK 465 THR A 11
REMARK 465 SER A 12
REMARK 465 ALA A 13
REMARK 465 ILE A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 GLY A 17
REMARK 465 CYS A 18
REMARK 465 ASN A 19
REMARK 465 THR A 20
REMARK 465 SER A 21
REMARK 465 ASN A 22
REMARK 465 VAL A 23
REMARK 465 SER A 24
REMARK 465 GLN A 25
REMARK 465 GLU A 26
REMARK 465 PRO A 27
REMARK 465 ASN A 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 ARG A 31
REMARK 465 LYS A 32
REMARK 465 VAL A 33
REMARK 465 GLN A 34
REMARK 465 GLU A 35
REMARK 465 THR A 36
REMARK 465 LYS A 37
REMARK 465 LYS A 38
REMARK 465 GLN A 39
REMARK 465 ALA A 40
REMARK 465 GLU A 41
REMARK 465 THR A 42
REMARK 465 VAL A 43
REMARK 465 GLN A 44
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LYS B 3
REMARK 465 TYR B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 ILE B 7
REMARK 465 ALA B 8
REMARK 465 LEU B 9
REMARK 465 CYS B 10
REMARK 465 THR B 11
REMARK 465 SER B 12
REMARK 465 ALA B 13
REMARK 465 ILE B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 GLY B 17
REMARK 465 CYS B 18
REMARK 465 ASN B 19
REMARK 465 THR B 20
REMARK 465 SER B 21
REMARK 465 ASN B 22
REMARK 465 VAL B 23
REMARK 465 SER B 24
REMARK 465 GLN B 25
REMARK 465 GLU B 26
REMARK 465 PRO B 27
REMARK 465 ASN B 28
REMARK 465 LYS B 29
REMARK 465 GLU B 30
REMARK 465 ARG B 31
REMARK 465 LYS B 32
REMARK 465 VAL B 33
REMARK 465 GLN B 34
REMARK 465 GLU B 35
REMARK 465 THR B 36
REMARK 465 LYS B 37
REMARK 465 LYS B 38
REMARK 465 GLN B 39
REMARK 465 ALA B 40
REMARK 465 GLU B 41
REMARK 465 THR B 42
REMARK 465 VAL B 43
REMARK 465 GLN B 44
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 O HOH B 2223 O HOH B 2224 2.11
REMARK 500 O HOH B 2067 O HOH B 2160 2.18
REMARK 500 O HOH A 2199 O HOH A 2200 2.19
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 ARG A 114 -167.07 -122.96
REMARK 500 LEU A 133 -91.37 -110.78
REMARK 500 HIS A 150 -94.97 -121.94
REMARK 500 ASP A 206 -32.10 115.63
REMARK 500 THR A 265 177.30 72.00
REMARK 500 GLN B 46 -85.26 -131.33
REMARK 500 LYS B 99 42.82 -109.49
REMARK 500 ARG B 114 -157.45 -127.27
REMARK 500 LEU B 133 -87.76 -77.21
REMARK 500 HIS B 150 -95.60 -125.34
REMARK 500 ASP B 206 -31.50 117.18
REMARK 500 ASP B 223 -166.86 -163.99
REMARK 500 THR B 265 175.49 73.49
REMARK 500 THR B 323 -169.27 -105.32
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 A2145 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A2192 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A2205 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH B2148 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B2156 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH B2170 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B2181 DISTANCE = 5.86 ANGSTROMS
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 ZN A1362 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 206 OD1
REMARK 620 2 HIS A 264 NE2 85.6
REMARK 620 3 HIS A 268 NE2 111.2 98.0
REMARK 620 4 ACT A1361 O 115.9 91.2 132.5
REMARK 620 5 HOH A2196 O 89.4 164.8 97.1 78.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1362 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 206 OD1
REMARK 620 2 HIS B 264 NE2 86.6
REMARK 620 3 HIS B 268 NE2 109.3 96.3
REMARK 620 4 ACT B1361 O 117.6 90.1 133.0
REMARK 620 5 HOH B2152 O 86.2 164.6 98.8 81.3
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 8-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 ACT A 1361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1364
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1365
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HYDROXY PROLINE AT POSITION 302
DBREF 4V33 A 1 360 UNP Q81ZD9 Q81ZD9_BACAN 1 360
DBREF 4V33 B 1 360 UNP Q81ZD9 Q81ZD9_BACAN 1 360
SEQRES 1 A 360 MET ARG LYS TYR ALA ALA ILE ALA LEU CYS THR SER ALA
SEQRES 2 A 360 ILE LEU ALA GLY CYS ASN THR SER ASN VAL SER GLN GLU
SEQRES 3 A 360 PRO ASN LYS GLU ARG LYS VAL GLN GLU THR LYS LYS GLN
SEQRES 4 A 360 ALA GLU THR VAL GLN GLU GLN GLY LYS ILE SER TYR ASN
SEQRES 5 A 360 PRO ILE THR HIS GLU SER THR ASN THR THR ILE HIS MET
SEQRES 6 A 360 THR ASP ILE LYS ASP THR LEU THR GLU VAL GLN TYR LYS
SEQRES 7 A 360 ILE TRP ARG THR ALA ASP GLY LYS GLU THR ALA LYS SER
SEQRES 8 A 360 LEU SER SER LYS GLU LYS GLU LYS GLN PHE SER LEU PRO
SEQRES 9 A 360 PHE ASP THR LYS GLU PHE GLU GLY LYS ARG GLY GLU PHE
SEQRES 10 A 360 GLN ILE GLU ALA ILE GLY ILE LYS GLU ASP GLY LYS THR
SEQRES 11 A 360 ILE PRO LEU THR LYS SER ALA ILE THR PHE GLU GLN LYS
SEQRES 12 A 360 VAL PRO VAL LEU MET TYR HIS ALA ILE ASP ASP TYR HIS
SEQRES 13 A 360 GLY GLN GLY ILE LYS ASP LEU PHE VAL SER PRO ALA ASN
SEQRES 14 A 360 PHE GLU ALA GLN MET LYS TYR LEU LYS ASP ASN GLY TYR
SEQRES 15 A 360 THR LEU LEU THR PHE GLU ARG TRP GLY ASP ILE ASN LYS
SEQRES 16 A 360 VAL ASN LYS PRO ILE PHE VAL THR PHE ASP ASP GLY MET
SEQRES 17 A 360 LYS ASN ASN MET ASN ALA PHE HIS VAL LEU GLN LYS LEU
SEQRES 18 A 360 LYS ASP ASP THR PHE LYS PRO VAL ALA THR GLU TYR MET
SEQRES 19 A 360 ILE VAL ASN ASN VAL ASP ALA GLU GLY SER LEU SER THR
SEQRES 20 A 360 SER ASP ILE LYS GLU MET VAL ASP SER GLY ILE PHE SER
SEQRES 21 A 360 MET GLN SER HIS THR ALA THR HIS ALA ASP LEU PRO LYS
SEQRES 22 A 360 ILE THR ASN TYR GLU GLU GLU LEU LYS GLU SER LYS GLU
SEQRES 23 A 360 LYS LEU GLU LYS ILE THR GLY LYS PRO VAL ILE ALA VAL
SEQRES 24 A 360 ALA TYR PXU PHE GLY HIS VAL ASP ASP LYS VAL VAL ALA
SEQRES 25 A 360 GLU THR LYS LYS TYR TYR GLN PHE ALA THR THR THR LYS
SEQRES 26 A 360 PRO GLY LYS PHE ILE THR LYS GLY GLU PRO ASP GLU LEU
SEQRES 27 A 360 LEU LYS MET LYS ARG VAL ARG ILE HIS HIS THR THR THR
SEQRES 28 A 360 VAL GLU GLN PHE ALA SER SER ILE LYS
SEQRES 1 B 360 MET ARG LYS TYR ALA ALA ILE ALA LEU CYS THR SER ALA
SEQRES 2 B 360 ILE LEU ALA GLY CYS ASN THR SER ASN VAL SER GLN GLU
SEQRES 3 B 360 PRO ASN LYS GLU ARG LYS VAL GLN GLU THR LYS LYS GLN
SEQRES 4 B 360 ALA GLU THR VAL GLN GLU GLN GLY LYS ILE SER TYR ASN
SEQRES 5 B 360 PRO ILE THR HIS GLU SER THR ASN THR THR ILE HIS MET
SEQRES 6 B 360 THR ASP ILE LYS ASP THR LEU THR GLU VAL GLN TYR LYS
SEQRES 7 B 360 ILE TRP ARG THR ALA ASP GLY LYS GLU THR ALA LYS SER
SEQRES 8 B 360 LEU SER SER LYS GLU LYS GLU LYS GLN PHE SER LEU PRO
SEQRES 9 B 360 PHE ASP THR LYS GLU PHE GLU GLY LYS ARG GLY GLU PHE
SEQRES 10 B 360 GLN ILE GLU ALA ILE GLY ILE LYS GLU ASP GLY LYS THR
SEQRES 11 B 360 ILE PRO LEU THR LYS SER ALA ILE THR PHE GLU GLN LYS
SEQRES 12 B 360 VAL PRO VAL LEU MET TYR HIS ALA ILE ASP ASP TYR HIS
SEQRES 13 B 360 GLY GLN GLY ILE LYS ASP LEU PHE VAL SER PRO ALA ASN
SEQRES 14 B 360 PHE GLU ALA GLN MET LYS TYR LEU LYS ASP ASN GLY TYR
SEQRES 15 B 360 THR LEU LEU THR PHE GLU ARG TRP GLY ASP ILE ASN LYS
SEQRES 16 B 360 VAL ASN LYS PRO ILE PHE VAL THR PHE ASP ASP GLY MET
SEQRES 17 B 360 LYS ASN ASN MET ASN ALA PHE HIS VAL LEU GLN LYS LEU
SEQRES 18 B 360 LYS ASP ASP THR PHE LYS PRO VAL ALA THR GLU TYR MET
SEQRES 19 B 360 ILE VAL ASN ASN VAL ASP ALA GLU GLY SER LEU SER THR
SEQRES 20 B 360 SER ASP ILE LYS GLU MET VAL ASP SER GLY ILE PHE SER
SEQRES 21 B 360 MET GLN SER HIS THR ALA THR HIS ALA ASP LEU PRO LYS
SEQRES 22 B 360 ILE THR ASN TYR GLU GLU GLU LEU LYS GLU SER LYS GLU
SEQRES 23 B 360 LYS LEU GLU LYS ILE THR GLY LYS PRO VAL ILE ALA VAL
SEQRES 24 B 360 ALA TYR PXU PHE GLY HIS VAL ASP ASP LYS VAL VAL ALA
SEQRES 25 B 360 GLU THR LYS LYS TYR TYR GLN PHE ALA THR THR THR LYS
SEQRES 26 B 360 PRO GLY LYS PHE ILE THR LYS GLY GLU PRO ASP GLU LEU
SEQRES 27 B 360 LEU LYS MET LYS ARG VAL ARG ILE HIS HIS THR THR THR
SEQRES 28 B 360 VAL GLU GLN PHE ALA SER SER ILE LYS
MODRES 4V33 PXU A 302 PRO 2-HYDROXY-L-PROLINE
MODRES 4V33 PXU B 302 PRO 2-HYDROXY-L-PROLINE
HET PXU A 302 8
HET PXU B 302 8
HET ACT A1361 4
HET ZN A1362 1
HET ACT A1363 4
HET EDO A1364 4
HET EDO A1365 4
HET ACT B1361 4
HET ZN B1362 1
HET ACT B1363 4
HET EDO B1364 4
HET EDO B1365 4
HETNAM PXU 2-HYDROXY-L-PROLINE
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 PXU 2(C5 H9 N O3)
FORMUL 3 ACT 4(C2 H3 O2 1-)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 6 EDO 4(C2 H6 O2)
FORMUL 13 HOH *942(H2 O)
HELIX 1 1 GLY A 85 ALA A 89 5 5
HELIX 2 2 GLU A 96 GLN A 100 5 5
HELIX 3 3 LYS A 108 GLU A 111 5 4
HELIX 4 4 ILE A 160 ASP A 162 5 3
HELIX 5 5 SER A 166 ASN A 180 1 15
HELIX 6 6 THR A 186 ILE A 193 5 8
HELIX 7 7 ASN A 210 LYS A 222 1 13
HELIX 8 8 VAL A 236 VAL A 239 5 4
HELIX 9 9 SER A 246 SER A 256 1 11
HELIX 10 10 ASP A 270 ILE A 274 5 5
HELIX 11 11 ASN A 276 GLY A 293 1 18
HELIX 12 12 ASP A 307 LYS A 316 1 10
HELIX 13 13 ASP A 336 LYS A 340 5 5
HELIX 14 14 THR A 351 LYS A 360 1 10
HELIX 15 15 GLY B 85 ALA B 89 5 5
HELIX 16 16 GLU B 96 GLN B 100 5 5
HELIX 17 17 LYS B 108 GLU B 111 5 4
HELIX 18 18 ILE B 160 ASP B 162 5 3
HELIX 19 19 SER B 166 ASN B 180 1 15
HELIX 20 20 THR B 186 ILE B 193 5 8
HELIX 21 21 ASN B 210 LYS B 222 1 13
HELIX 22 22 VAL B 236 VAL B 239 5 4
HELIX 23 23 SER B 246 SER B 256 1 11
HELIX 24 24 ASP B 270 ILE B 274 5 5
HELIX 25 25 ASN B 276 GLY B 293 1 18
HELIX 26 26 ASP B 307 TYR B 318 1 12
HELIX 27 27 ASP B 336 LYS B 340 5 5
HELIX 28 28 THR B 351 LYS B 360 1 10
SHEET 1 AA 3 LYS A 48 TYR A 51 0
SHEET 2 AA 3 ASN A 60 THR A 66 -1 O HIS A 64 N SER A 50
SHEET 3 AA 3 LEU A 103 ASP A 106 -1 O LEU A 103 N ILE A 63
SHEET 1 AB 4 LYS A 90 SER A 94 0
SHEET 2 AB 4 GLU A 74 ARG A 81 -1 O VAL A 75 N SER A 94
SHEET 3 AB 4 GLY A 115 ILE A 124 -1 O GLN A 118 N TRP A 80
SHEET 4 AB 4 THR A 130 PHE A 140 -1 O ILE A 131 N GLY A 123
SHEET 1 AC 8 VAL A 146 TYR A 149 0
SHEET 2 AC 8 PRO A 199 ASP A 206 -1 O PHE A 201 N LEU A 147
SHEET 3 AC 8 ALA A 230 MET A 234 1 O THR A 231 N PHE A 204
SHEET 4 AC 8 PHE A 259 SER A 263 1 O SER A 260 N GLU A 232
SHEET 5 AC 8 ALA A 298 ALA A 300 -1 O ALA A 298 N SER A 263
SHEET 6 AC 8 PHE A 320 PRO A 326 1 O PHE A 320 N VAL A 299
SHEET 7 AC 8 MET A 341 ARG A 345 1 O MET A 341 N THR A 323
SHEET 8 AC 8 VAL A 146 TYR A 149 0
SHEET 1 AD 2 ALA A 151 ILE A 152 0
SHEET 2 AD 2 PHE A 164 VAL A 165 1 N VAL A 165 O ALA A 151
SHEET 1 BA 3 LYS B 48 TYR B 51 0
SHEET 2 BA 3 ASN B 60 THR B 66 -1 O HIS B 64 N SER B 50
SHEET 3 BA 3 LEU B 103 ASP B 106 -1 O LEU B 103 N ILE B 63
SHEET 1 BB 4 LYS B 90 SER B 94 0
SHEET 2 BB 4 GLU B 74 ARG B 81 -1 O VAL B 75 N SER B 94
SHEET 3 BB 4 GLY B 115 ILE B 124 -1 O GLN B 118 N TRP B 80
SHEET 4 BB 4 THR B 130 PHE B 140 -1 O ILE B 131 N GLY B 123
SHEET 1 BC 8 VAL B 146 TYR B 149 0
SHEET 2 BC 8 PRO B 199 ASP B 206 -1 O PHE B 201 N LEU B 147
SHEET 3 BC 8 ALA B 230 MET B 234 1 O THR B 231 N PHE B 204
SHEET 4 BC 8 PHE B 259 SER B 263 1 O SER B 260 N GLU B 232
SHEET 5 BC 8 ALA B 298 ALA B 300 -1 O ALA B 298 N SER B 263
SHEET 6 BC 8 PHE B 320 PRO B 326 1 O PHE B 320 N VAL B 299
SHEET 7 BC 8 MET B 341 ARG B 345 1 O MET B 341 N THR B 323
SHEET 8 BC 8 VAL B 146 TYR B 149 0
SHEET 1 BD 2 ALA B 151 ILE B 152 0
SHEET 2 BD 2 PHE B 164 VAL B 165 1 N VAL B 165 O ALA B 151
LINK C TYR A 301 N PXU A 302 1555 1555 1.33
LINK C PXU A 302 N PHE A 303 1555 1555 1.34
LINK C TYR B 301 N PXU B 302 1555 1555 1.33
LINK C PXU B 302 N PHE B 303 1555 1555 1.34
LINK OD1 ASP A 206 ZN ZN A1362 1555 1555 2.14
LINK NE2 HIS A 264 ZN ZN A1362 1555 1555 2.16
LINK NE2 HIS A 268 ZN ZN A1362 1555 1555 2.13
LINK O ACT A1361 ZN ZN A1362 1555 1555 2.35
LINK ZN ZN A1362 O HOH A2196 1555 1555 2.04
LINK OD1 ASP B 206 ZN ZN B1362 1555 1555 2.13
LINK NE2 HIS B 264 ZN ZN B1362 1555 1555 2.18
LINK NE2 HIS B 268 ZN ZN B1362 1555 1555 2.10
LINK O ACT B1361 ZN ZN B1362 1555 1555 2.39
LINK ZN ZN B1362 O HOH B2152 1555 1555 2.04
SITE 1 AC1 10 HIS A 150 ASP A 205 HIS A 264 HIS A 268
SITE 2 AC1 10 TYR A 301 PXU A 302 PHE A 303 THR A 324
SITE 3 AC1 10 ZN A1362 HOH A2196
SITE 1 AC2 6 ASP A 206 HIS A 264 HIS A 268 PXU A 302
SITE 2 AC2 6 ACT A1361 HOH A2196
SITE 1 AC3 10 HIS B 150 ASP B 205 HIS B 264 HIS B 268
SITE 2 AC3 10 TYR B 301 PXU B 302 PHE B 303 THR B 324
SITE 3 AC3 10 ZN B1362 HOH B2152
SITE 1 AC4 6 ASP B 206 HIS B 264 HIS B 268 PXU B 302
SITE 2 AC4 6 ACT B1361 HOH B2152
SITE 1 AC5 4 TYR A 176 TYR A 182 LYS A 198 HOH A2277
SITE 1 AC6 4 TYR B 176 TYR B 182 LYS B 198 HOH B2217
SITE 1 AC7 4 PRO B 53 ASN B 60 ASP B 223 ASP B 224
SITE 1 AC8 6 TYR B 182 THR B 183 LEU B 184 PHE B 226
SITE 2 AC8 6 LYS B 227 HOH B2444
SITE 1 AC9 5 THR A 186 GLU A 188 GLY A 257 HOH A2358
SITE 2 AC9 5 HOH A2497
SITE 1 BC1 7 TYR A 182 THR A 183 LEU A 184 THR A 225
SITE 2 BC1 7 PHE A 226 LYS A 227 HOH A2498
CRYST1 108.964 68.763 132.022 90.00 96.86 90.00 C 1 2 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 0.009177 0.000000 0.001104 0.00000
SCALE2 0.000000 0.014543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007629 0.00000
(ATOM LINES ARE NOT SHOWN.)
END