HEADER TOXIN 06-JAN-11 3Q8E
TITLE CRYSTAL STRUCTURE OF PROTECTIVE ANTIGEN W346F (PH 8.5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTECTIVE ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PA, ANTHRAX TOXINS TRANSLOCATING PROTEIN, PA-83, PA83,
COMPND 5 PROTECTIVE ANTIGEN PA-20, PA20, PROTECTIVE ANTIGEN PA-63, PA63;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 1392;
SOURCE 5 GENE: PAGA, PAG, PXO1-110, BXA0164, GBAA_PXO1_0164;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80
KEYWDS PROTECTIVE ANTIGEN; ANTHRAX; PH STABILITY, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LOVELL,K.P.BATTAILE,M.RAJAPAKSHA,B.E.JANOWIAK,K.K.ANDRA,J.G.BANN
REVDAT 4 13-SEP-23 3Q8E 1 REMARK SEQADV LINK
REVDAT 3 03-OCT-12 3Q8E 1 JRNL
REVDAT 2 15-AUG-12 3Q8E 1 JRNL
REVDAT 1 15-FEB-12 3Q8E 0
JRNL AUTH M.RAJAPAKSHA,S.LOVELL,B.E.JANOWIAK,K.K.ANDRA,K.P.BATTAILE,
JRNL AUTH 2 J.G.BANN
JRNL TITL PH EFFECTS ON BINDING BETWEEN THE ANTHRAX PROTECTIVE ANTIGEN
JRNL TITL 2 AND THE HOST CELLULAR RECEPTOR CMG2.
JRNL REF PROTEIN SCI. V. 21 1467 2012
JRNL REFN ISSN 0961-8368
JRNL PMID 22855243
JRNL DOI 10.1002/PRO.2136
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 46482
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2352
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 45.3018 - 4.5187 1.00 4630 277 0.1749 0.1904
REMARK 3 2 4.5187 - 3.5871 1.00 4473 243 0.1530 0.2126
REMARK 3 3 3.5871 - 3.1338 1.00 4468 215 0.2050 0.2406
REMARK 3 4 3.1338 - 2.8473 1.00 4409 240 0.2193 0.3087
REMARK 3 5 2.8473 - 2.6432 1.00 4421 217 0.2217 0.2964
REMARK 3 6 2.6432 - 2.4874 1.00 4403 218 0.2102 0.3201
REMARK 3 7 2.4874 - 2.3628 0.99 4337 233 0.2088 0.2984
REMARK 3 8 2.3628 - 2.2600 0.98 4301 229 0.2447 0.3367
REMARK 3 9 2.2600 - 2.1730 1.00 4347 225 0.2249 0.2973
REMARK 3 10 2.1730 - 2.0980 1.00 4341 255 0.2414 0.3390
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.77
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 42.30
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.96300
REMARK 3 B22 (A**2) : -9.77160
REMARK 3 B33 (A**2) : 18.73460
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 : 0.012 5462
REMARK 3 ANGLE : 1.282 7418
REMARK 3 CHIRALITY : 0.075 855
REMARK 3 PLANARITY : 0.006 969
REMARK 3 DIHEDRAL : 14.464 2012
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 3Q8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063323.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46703
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.098
REMARK 200 RESOLUTION RANGE LOW (A) : 117.205
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : 0.49000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3MHZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%(W/V) PEG 1500, 100MM SPG BUFFER,
REMARK 280 PH 8.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 35.68600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.60250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.80050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.60250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.68600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.80050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 GLU A 1
REMARK 465 VAL A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 GLU A 5
REMARK 465 ASN A 6
REMARK 465 ARG A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 ASN A 10
REMARK 465 GLU A 11
REMARK 465 SER A 12
REMARK 465 GLU A 13
REMARK 465 SER A 14
REMARK 465 LYS A 99
REMARK 465 ALA A 100
REMARK 465 SER A 101
REMARK 465 ASN A 102
REMARK 465 SER A 168
REMARK 465 THR A 169
REMARK 465 SER A 170
REMARK 465 ALA A 171
REMARK 465 GLY A 172
REMARK 465 PRO A 173
REMARK 465 THR A 174
REMARK 465 GLU A 302
REMARK 465 VAL A 303
REMARK 465 HIS A 304
REMARK 465 GLY A 305
REMARK 465 ASN A 306
REMARK 465 ALA A 307
REMARK 465 GLU A 308
REMARK 465 VAL A 309
REMARK 465 HIS A 310
REMARK 465 ALA A 311
REMARK 465 SER A 312
REMARK 465 PHE A 313
REMARK 465 PHE A 314
REMARK 465 ASP A 315
REMARK 465 ILE A 316
REMARK 465 GLY A 317
REMARK 465 GLY A 318
REMARK 465 SER A 319
REMARK 465 VAL A 320
REMARK 465 LEU A 340
REMARK 465 ALA A 341
REMARK 465 GLY A 735
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 GLU A 51 CG CD OE1 OE2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 ARG A 107 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 ASN A 162 CG OD1 ND2
REMARK 470 LYS A 165 CE NZ
REMARK 470 ARG A 167 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 198 CG OD1 ND2
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 LYS A 213 CG CD CE NZ
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 GLN A 277 CG CD OE1 NE2
REMARK 470 GLN A 280 CG CD OE1 NE2
REMARK 470 PHE A 324 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 387 CD CE NZ
REMARK 470 LYS A 397 CE NZ
REMARK 470 LYS A 444 CG CD CE NZ
REMARK 470 GLN A 556 CD OE1 NE2
REMARK 470 GLU A 568 CD OE1 OE2
REMARK 470 ARG A 600 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 614 CG CD OE1 OE2
REMARK 470 ARG A 617 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 633 CG CD CE NZ
REMARK 470 ARG A 636 NE CZ NH1 NH2
REMARK 470 GLN A 670 CG CD OE1 NE2
REMARK 470 LYS A 684 CG CD CE NZ
REMARK 470 GLU A 712 CG CD OE1 OE2
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 OE2 GLU A 479 O HOH A 811 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 365 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
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 ALA A 83 58.90 -145.02
REMARK 500 ASP A 93 -1.61 70.67
REMARK 500 GLN A 140 10.17 -66.51
REMARK 500 ASP A 177 72.37 -153.33
REMARK 500 LYS A 197 -163.06 -79.92
REMARK 500 ASN A 198 -87.35 -39.40
REMARK 500 ASP A 244 113.40 -37.98
REMARK 500 ASN A 376 10.66 -140.27
REMARK 500 ASN A 388 33.26 -161.99
REMARK 500 ASN A 399 19.57 46.35
REMARK 500 ASP A 425 40.65 -93.38
REMARK 500 GLN A 454 40.65 -108.49
REMARK 500 ASP A 497 34.89 -157.74
REMARK 500 ASN A 537 61.97 -156.11
REMARK 500 ASN A 657 74.67 -104.15
REMARK 500 ASP A 658 56.48 -95.24
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 CA A 737 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 177 OD1
REMARK 620 2 ASP A 179 OD1 79.5
REMARK 620 3 ASP A 181 OD1 94.7 81.9
REMARK 620 4 ILE A 183 O 84.9 163.3 93.6
REMARK 620 5 GLU A 188 OE1 168.0 105.6 96.8 90.8
REMARK 620 6 HOH A 744 O 88.8 86.5 167.0 99.2 80.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 736 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 179 OD2
REMARK 620 2 ASP A 181 OD2 85.4
REMARK 620 3 GLU A 188 OE2 120.7 96.5
REMARK 620 4 GLU A 188 OE1 74.5 82.0 47.7
REMARK 620 5 SER A 222 O 78.8 160.1 81.4 82.1
REMARK 620 6 LYS A 225 O 77.9 103.3 154.1 151.3 85.4
REMARK 620 7 ASP A 235 OD2 155.4 95.4 83.7 130.1 104.0 78.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 736
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 737
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q8A RELATED DB: PDB
REMARK 900 RELATED ID: 3Q8B RELATED DB: PDB
REMARK 900 RELATED ID: 3Q8C RELATED DB: PDB
REMARK 900 RELATED ID: 3Q8F RELATED DB: PDB
DBREF 3Q8E A 1 735 UNP P13423 PAG_BACAN 30 764
SEQADV 3Q8E PHE A 346 UNP P13423 TRP 375 ENGINEERED MUTATION
SEQRES 1 A 735 GLU VAL LYS GLN GLU ASN ARG LEU LEU ASN GLU SER GLU
SEQRES 2 A 735 SER SER SER GLN GLY LEU LEU GLY TYR TYR PHE SER ASP
SEQRES 3 A 735 LEU ASN PHE GLN ALA PRO MET VAL VAL THR SER SER THR
SEQRES 4 A 735 THR GLY ASP LEU SER ILE PRO SER SER GLU LEU GLU ASN
SEQRES 5 A 735 ILE PRO SER GLU ASN GLN TYR PHE GLN SER ALA ILE TRP
SEQRES 6 A 735 SER GLY PHE ILE LYS VAL LYS LYS SER ASP GLU TYR THR
SEQRES 7 A 735 PHE ALA THR SER ALA ASP ASN HIS VAL THR MET TRP VAL
SEQRES 8 A 735 ASP ASP GLN GLU VAL ILE ASN LYS ALA SER ASN SER ASN
SEQRES 9 A 735 LYS ILE ARG LEU GLU LYS GLY ARG LEU TYR GLN ILE LYS
SEQRES 10 A 735 ILE GLN TYR GLN ARG GLU ASN PRO THR GLU LYS GLY LEU
SEQRES 11 A 735 ASP PHE LYS LEU TYR TRP THR ASP SER GLN ASN LYS LYS
SEQRES 12 A 735 GLU VAL ILE SER SER ASP ASN LEU GLN LEU PRO GLU LEU
SEQRES 13 A 735 LYS GLN LYS SER SER ASN SER ARG LYS LYS ARG SER THR
SEQRES 14 A 735 SER ALA GLY PRO THR VAL PRO ASP ARG ASP ASN ASP GLY
SEQRES 15 A 735 ILE PRO ASP SER LEU GLU VAL GLU GLY TYR THR VAL ASP
SEQRES 16 A 735 VAL LYS ASN LYS ARG THR PHE LEU SER PRO TRP ILE SER
SEQRES 17 A 735 ASN ILE HIS GLU LYS LYS GLY LEU THR LYS TYR LYS SER
SEQRES 18 A 735 SER PRO GLU LYS TRP SER THR ALA SER ASP PRO TYR SER
SEQRES 19 A 735 ASP PHE GLU LYS VAL THR GLY ARG ILE ASP LYS ASN VAL
SEQRES 20 A 735 SER PRO GLU ALA ARG HIS PRO LEU VAL ALA ALA TYR PRO
SEQRES 21 A 735 ILE VAL HIS VAL ASP MET GLU ASN ILE ILE LEU SER LYS
SEQRES 22 A 735 ASN GLU ASP GLN SER THR GLN ASN THR ASP SER GLN THR
SEQRES 23 A 735 ARG THR ILE SER LYS ASN THR SER THR SER ARG THR HIS
SEQRES 24 A 735 THR SER GLU VAL HIS GLY ASN ALA GLU VAL HIS ALA SER
SEQRES 25 A 735 PHE PHE ASP ILE GLY GLY SER VAL SER ALA GLY PHE SER
SEQRES 26 A 735 ASN SER ASN SER SER THR VAL ALA ILE ASP HIS SER LEU
SEQRES 27 A 735 SER LEU ALA GLY GLU ARG THR PHE ALA GLU THR MET GLY
SEQRES 28 A 735 LEU ASN THR ALA ASP THR ALA ARG LEU ASN ALA ASN ILE
SEQRES 29 A 735 ARG TYR VAL ASN THR GLY THR ALA PRO ILE TYR ASN VAL
SEQRES 30 A 735 LEU PRO THR THR SER LEU VAL LEU GLY LYS ASN GLN THR
SEQRES 31 A 735 LEU ALA THR ILE LYS ALA LYS GLU ASN GLN LEU SER GLN
SEQRES 32 A 735 ILE LEU ALA PRO ASN ASN TYR TYR PRO SER LYS ASN LEU
SEQRES 33 A 735 ALA PRO ILE ALA LEU ASN ALA GLN ASP ASP PHE SER SER
SEQRES 34 A 735 THR PRO ILE THR MET ASN TYR ASN GLN PHE LEU GLU LEU
SEQRES 35 A 735 GLU LYS THR LYS GLN LEU ARG LEU ASP THR ASP GLN VAL
SEQRES 36 A 735 TYR GLY ASN ILE ALA THR TYR ASN PHE GLU ASN GLY ARG
SEQRES 37 A 735 VAL ARG VAL ASP THR GLY SER ASN TRP SER GLU VAL LEU
SEQRES 38 A 735 PRO GLN ILE GLN GLU THR THR ALA ARG ILE ILE PHE ASN
SEQRES 39 A 735 GLY LYS ASP LEU ASN LEU VAL GLU ARG ARG ILE ALA ALA
SEQRES 40 A 735 VAL ASN PRO SER ASP PRO LEU GLU THR THR LYS PRO ASP
SEQRES 41 A 735 MET THR LEU LYS GLU ALA LEU LYS ILE ALA PHE GLY PHE
SEQRES 42 A 735 ASN GLU PRO ASN GLY ASN LEU GLN TYR GLN GLY LYS ASP
SEQRES 43 A 735 ILE THR GLU PHE ASP PHE ASN PHE ASP GLN GLN THR SER
SEQRES 44 A 735 GLN ASN ILE LYS ASN GLN LEU ALA GLU LEU ASN ALA THR
SEQRES 45 A 735 ASN ILE TYR THR VAL LEU ASP LYS ILE LYS LEU ASN ALA
SEQRES 46 A 735 LYS MET ASN ILE LEU ILE ARG ASP LYS ARG PHE HIS TYR
SEQRES 47 A 735 ASP ARG ASN ASN ILE ALA VAL GLY ALA ASP GLU SER VAL
SEQRES 48 A 735 VAL LYS GLU ALA HIS ARG GLU VAL ILE ASN SER SER THR
SEQRES 49 A 735 GLU GLY LEU LEU LEU ASN ILE ASP LYS ASP ILE ARG LYS
SEQRES 50 A 735 ILE LEU SER GLY TYR ILE VAL GLU ILE GLU ASP THR GLU
SEQRES 51 A 735 GLY LEU LYS GLU VAL ILE ASN ASP ARG TYR ASP MET LEU
SEQRES 52 A 735 ASN ILE SER SER LEU ARG GLN ASP GLY LYS THR PHE ILE
SEQRES 53 A 735 ASP PHE LYS LYS TYR ASN ASP LYS LEU PRO LEU TYR ILE
SEQRES 54 A 735 SER ASN PRO ASN TYR LYS VAL ASN VAL TYR ALA VAL THR
SEQRES 55 A 735 LYS GLU ASN THR ILE ILE ASN PRO SER GLU ASN GLY ASP
SEQRES 56 A 735 THR SER THR ASN GLY ILE LYS LYS ILE LEU ILE PHE SER
SEQRES 57 A 735 LYS LYS GLY TYR GLU ILE GLY
HET CA A 736 1
HET CA A 737 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
FORMUL 4 HOH *243(H2 O)
HELIX 1 1 PRO A 46 LEU A 50 5 5
HELIX 2 2 PRO A 54 TYR A 59 5 6
HELIX 3 3 ALA A 83 ASN A 85 5 3
HELIX 4 4 SER A 147 ASP A 149 5 3
HELIX 5 5 PRO A 184 GLY A 191 1 8
HELIX 6 6 ILE A 207 GLU A 212 1 6
HELIX 7 7 SER A 234 GLY A 241 1 8
HELIX 8 8 SER A 248 HIS A 253 5 6
HELIX 9 9 THR A 345 GLY A 351 1 7
HELIX 10 10 ASN A 435 LYS A 446 1 12
HELIX 11 11 VAL A 480 THR A 487 1 8
HELIX 12 12 ASP A 512 THR A 517 1 6
HELIX 13 13 THR A 522 GLY A 532 1 11
HELIX 14 14 ASP A 555 LEU A 569 1 15
HELIX 15 15 ASN A 573 ILE A 581 5 9
HELIX 16 16 ASP A 608 HIS A 616 1 9
HELIX 17 17 ASP A 632 ILE A 638 1 7
HELIX 18 18 GLU A 704 THR A 706 5 3
HELIX 19 19 TYR A 732 ILE A 734 5 3
SHEET 1 A 6 PRO A 32 SER A 38 0
SHEET 2 A 6 LEU A 19 PHE A 24 -1 N GLY A 21 O THR A 36
SHEET 3 A 6 SER A 62 LYS A 70 -1 O ILE A 64 N TYR A 22
SHEET 4 A 6 LEU A 113 GLN A 121 -1 O TYR A 114 N ILE A 69
SHEET 5 A 6 VAL A 87 VAL A 91 -1 N THR A 88 O GLN A 119
SHEET 6 A 6 GLN A 94 ILE A 97 -1 O GLN A 94 N VAL A 91
SHEET 1 B 4 PRO A 32 SER A 38 0
SHEET 2 B 4 LEU A 19 PHE A 24 -1 N GLY A 21 O THR A 36
SHEET 3 B 4 SER A 62 LYS A 70 -1 O ILE A 64 N TYR A 22
SHEET 4 B 4 LEU A 151 GLN A 152 -1 O GLN A 152 N PHE A 68
SHEET 1 C 4 LYS A 105 LEU A 108 0
SHEET 2 C 4 ASP A 75 THR A 81 -1 N ASP A 75 O LEU A 108
SHEET 3 C 4 LEU A 134 THR A 137 -1 O TYR A 135 N ALA A 80
SHEET 4 C 4 LYS A 143 VAL A 145 -1 O GLU A 144 N TRP A 136
SHEET 1 D 2 TYR A 192 VAL A 196 0
SHEET 2 D 2 THR A 201 PRO A 205 -1 O SER A 204 N THR A 193
SHEET 1 E 8 GLN A 389 ILE A 394 0
SHEET 2 E 8 THR A 381 LEU A 385 -1 N THR A 381 O ILE A 394
SHEET 3 E 8 GLN A 447 THR A 452 -1 O ARG A 449 N VAL A 384
SHEET 4 E 8 ASN A 328 ILE A 334 -1 N VAL A 332 O LEU A 448
SHEET 5 E 8 ILE A 289 ARG A 297 -1 N SER A 294 O ALA A 333
SHEET 6 E 8 VAL A 262 LYS A 273 -1 N LEU A 271 O ILE A 289
SHEET 7 E 8 ALA A 358 ASN A 368 -1 O ARG A 365 N ASP A 265
SHEET 8 E 8 ILE A 419 ALA A 420 -1 O ILE A 419 N ILE A 364
SHEET 1 F 3 ASN A 409 TYR A 411 0
SHEET 2 F 3 ALA A 358 ASN A 368 -1 N TYR A 366 O TYR A 411
SHEET 3 F 3 ILE A 432 MET A 434 -1 O MET A 434 N ALA A 358
SHEET 1 G 2 ASN A 458 TYR A 462 0
SHEET 2 G 2 VAL A 469 ASN A 476 -1 O ASP A 472 N ILE A 459
SHEET 1 H 4 VAL A 501 ALA A 506 0
SHEET 2 H 4 THR A 488 PHE A 493 -1 N ILE A 491 O ARG A 503
SHEET 3 H 4 ASN A 588 ASP A 593 1 O ILE A 591 N ILE A 492
SHEET 4 H 4 PHE A 550 PHE A 554 -1 N ASN A 553 O LEU A 590
SHEET 1 I 2 GLN A 541 TYR A 542 0
SHEET 2 I 2 LYS A 545 ASP A 546 -1 O LYS A 545 N TYR A 542
SHEET 1 J 2 PHE A 596 TYR A 598 0
SHEET 2 J 2 ALA A 604 ALA A 607 -1 O VAL A 605 N HIS A 597
SHEET 1 K 4 VAL A 619 SER A 623 0
SHEET 2 K 4 GLY A 626 LEU A 629 -1 O LEU A 628 N ASN A 621
SHEET 3 K 4 THR A 674 ASP A 677 -1 O ILE A 676 N LEU A 627
SHEET 4 K 4 SER A 666 LEU A 668 -1 N SER A 667 O PHE A 675
SHEET 1 L 4 LYS A 653 VAL A 655 0
SHEET 2 L 4 LEU A 639 GLU A 647 -1 N ILE A 646 O GLU A 654
SHEET 3 L 4 LYS A 695 THR A 702 -1 O ASN A 697 N GLU A 645
SHEET 4 L 4 ILE A 724 LYS A 730 -1 O ILE A 724 N ALA A 700
LINK OD1 ASP A 177 CA CA A 737 1555 1555 2.48
LINK OD2 ASP A 179 CA CA A 736 1555 1555 2.50
LINK OD1 ASP A 179 CA CA A 737 1555 1555 2.45
LINK OD2 ASP A 181 CA CA A 736 1555 1555 2.25
LINK OD1 ASP A 181 CA CA A 737 1555 1555 2.40
LINK O ILE A 183 CA CA A 737 1555 1555 2.33
LINK OE2 GLU A 188 CA CA A 736 1555 1555 2.35
LINK OE1 GLU A 188 CA CA A 736 1555 1555 2.90
LINK OE1 GLU A 188 CA CA A 737 1555 1555 2.39
LINK O SER A 222 CA CA A 736 1555 1555 2.40
LINK O LYS A 225 CA CA A 736 1555 1555 2.49
LINK OD2 ASP A 235 CA CA A 736 1555 1555 2.52
LINK CA CA A 737 O HOH A 744 1555 1555 2.42
CISPEP 1 TYR A 411 PRO A 412 0 -6.69
SITE 1 AC1 6 ASP A 179 ASP A 181 GLU A 188 SER A 222
SITE 2 AC1 6 LYS A 225 ASP A 235
SITE 1 AC2 6 ASP A 177 ASP A 179 ASP A 181 ILE A 183
SITE 2 AC2 6 GLU A 188 HOH A 744
CRYST1 71.372 93.601 117.205 90.00 90.00 90.00 P 21 21 21 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 0.014011 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
