HEADER ADP-RIBOSYLATION 28-APR-95 1DMA
TITLE DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH
TITLE 2 NICOTINAMIDE AND AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXOTOXIN A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PPED5-399
KEYWDS ADP-RIBOSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LI,F.DYDA,I.BENHAR,I.PASTAN,D.DAVIES
REVDAT 3 07-FEB-24 1DMA 1 REMARK
REVDAT 2 24-FEB-09 1DMA 1 VERSN
REVDAT 1 15-SEP-95 1DMA 0
JRNL AUTH M.LI,F.DYDA,I.BENHAR,I.PASTAN,D.R.DAVIES
JRNL TITL THE CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA EXOTOXIN
JRNL TITL 2 DOMAIN III WITH NICOTINAMIDE AND AMP: CONFORMATIONAL
JRNL TITL 3 DIFFERENCES WITH THE INTACT EXOTOXIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 92 9308 1995
JRNL REFN ISSN 0027-8424
JRNL PMID 7568123
JRNL DOI 10.1073/PNAS.92.20.9308
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.B.SIEGALL,V.K.CHAUDHARY,D.J.FITZGERALD,I.PASTAN
REMARK 1 TITL FUNCTIONAL ANALYSIS OF DOMAINS II, IB, AND III OF
REMARK 1 TITL 2 PSEUDOMONAS EXOTOXIN
REMARK 1 REF J.BIOL.CHEM. V. 264 14256 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.S.ALLURED,R.J.COLLIER,S.F.CARROLL,D.B.MCKAY
REMARK 1 TITL STRUCTURE OF EXOTOXIN A OF PSEUDOMONAS AERUGINOSA A
REMARK 1 TITL 2 3.0-ANGSTROM RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 83 1320 1986
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 16513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2999
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.30
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.380
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.140
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172837.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 -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 67.04000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.75500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.75500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 100.56000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.75500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.75500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.52000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.75500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.75500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 100.56000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.75500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.75500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.52000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.04000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ARG A 458
REMARK 465 SER A 459
REMARK 465 GLN A 460
REMARK 465 ASP A 461
REMARK 465 LEU A 462
REMARK 465 ASP A 463
REMARK 465 GLU A 610
REMARK 465 ASP A 611
REMARK 465 LEU A 612
REMARK 465 LYS A 613
REMARK 465 ASP B 484
REMARK 465 GLN B 485
REMARK 465 GLU B 486
REMARK 465 PRO B 487
REMARK 465 ASP B 488
REMARK 465 ALA B 489
REMARK 465 ARG B 490
REMARK 465 GLY B 491
REMARK 465 ARG B 492
REMARK 465 GLY B 579
REMARK 465 GLY B 580
REMARK 465 TYR B 600
REMARK 465 ALA B 601
REMARK 465 SER B 602
REMARK 465 GLN B 603
REMARK 465 PRO B 604
REMARK 465 GLY B 605
REMARK 465 LYS B 606
REMARK 465 PRO B 607
REMARK 465 PRO B 608
REMARK 465 ARG B 609
REMARK 465 GLU B 610
REMARK 465 ASP B 611
REMARK 465 LEU B 612
REMARK 465 LYS B 613
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 486 CG CD OE1 OE2
REMARK 470 GLU B 546 CB CG CD OE1 OE2
REMARK 470 GLU B 547 CB CG CD OE1 OE2
REMARK 470 GLU B 548 CB CG CD OE1 OE2
REMARK 470 ARG B 551 CB CG CD NE CZ NH1 NH2
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 LYS A 606 CB CG CD CE NZ
REMARK 480 ARG B 456 CG CD NE CZ NH1 NH2
REMARK 480 GLN B 460 CG CD OE1 NE2
REMARK 480 ARG B 494 C CB CG CD NE CZ NH1
REMARK 480 ARG B 494 NH2
REMARK 480 ARG B 576 C O CB CG CD NE CZ
REMARK 480 ARG B 576 NH1 NH2
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 ALA B 457 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 LEU B 516 CA - CB - CG ANGL. DEV. = 17.9 DEGREES
REMARK 500 LEU B 537 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 ARG B 576 NE - CZ - NH2 ANGL. DEV. = 3.6 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 TRP A 466 33.28 -95.39
REMARK 500 ASP A 488 -156.18 -99.55
REMARK 500 ASN A 495 172.84 -51.29
REMARK 500 LEU A 518 -4.86 -57.72
REMARK 500 ARG A 538 -105.59 -105.99
REMARK 500 LEU A 539 44.26 -95.45
REMARK 500 GLU A 548 -3.35 65.40
REMARK 500 ASN A 577 58.32 -153.25
REMARK 500 ARG B 458 119.34 99.33
REMARK 500 SER B 459 20.41 -73.92
REMARK 500 ALA B 482 107.19 167.67
REMARK 500 ARG B 494 45.52 -140.38
REMARK 500 ASN B 495 122.69 78.04
REMARK 500 ARG B 505 -7.82 -58.54
REMARK 500 HIS B 533 154.44 179.46
REMARK 500 ARG B 538 -114.56 -107.34
REMARK 500 LEU B 539 43.66 -86.07
REMARK 500 GLU B 546 40.11 138.48
REMARK 500 GLU B 548 -70.91 106.88
REMARK 500 LEU B 552 107.26 72.52
REMARK 500 PRO B 598 -85.24 -90.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN B 495 -16.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCA A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCA B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B 701
DBREF 1DMA A 400 613 UNP P11439 TOXA_PSEAE 425 638
DBREF 1DMA B 400 613 UNP P11439 TOXA_PSEAE 425 638
SEQRES 1 A 214 PHE LEU GLY ASP GLY GLY ASP VAL SER PHE SER THR ARG
SEQRES 2 A 214 GLY THR GLN ASN TRP THR VAL GLU ARG LEU LEU GLN ALA
SEQRES 3 A 214 HIS ARG GLN LEU GLU GLU ARG GLY TYR VAL PHE VAL GLY
SEQRES 4 A 214 TYR HIS GLY THR PHE LEU GLU ALA ALA GLN SER ILE VAL
SEQRES 5 A 214 PHE GLY GLY VAL ARG ALA ARG SER GLN ASP LEU ASP ALA
SEQRES 6 A 214 ILE TRP ARG GLY PHE TYR ILE ALA GLY ASP PRO ALA LEU
SEQRES 7 A 214 ALA TYR GLY TYR ALA GLN ASP GLN GLU PRO ASP ALA ARG
SEQRES 8 A 214 GLY ARG ILE ARG ASN GLY ALA LEU LEU ARG VAL TYR VAL
SEQRES 9 A 214 PRO ARG SER SER LEU PRO GLY PHE TYR ARG THR SER LEU
SEQRES 10 A 214 THR LEU ALA ALA PRO GLU ALA ALA GLY GLU VAL GLU ARG
SEQRES 11 A 214 LEU ILE GLY HIS PRO LEU PRO LEU ARG LEU ASP ALA ILE
SEQRES 12 A 214 THR GLY PRO GLU GLU GLU GLY GLY ARG LEU GLU THR ILE
SEQRES 13 A 214 LEU GLY TRP PRO LEU ALA GLU ARG THR VAL VAL ILE PRO
SEQRES 14 A 214 SER ALA ILE PRO THR ASP PRO ARG ASN VAL GLY GLY ASP
SEQRES 15 A 214 LEU ASP PRO SER SER ILE PRO ASP LYS GLU GLN ALA ILE
SEQRES 16 A 214 SER ALA LEU PRO ASP TYR ALA SER GLN PRO GLY LYS PRO
SEQRES 17 A 214 PRO ARG GLU ASP LEU LYS
SEQRES 1 B 214 PHE LEU GLY ASP GLY GLY ASP VAL SER PHE SER THR ARG
SEQRES 2 B 214 GLY THR GLN ASN TRP THR VAL GLU ARG LEU LEU GLN ALA
SEQRES 3 B 214 HIS ARG GLN LEU GLU GLU ARG GLY TYR VAL PHE VAL GLY
SEQRES 4 B 214 TYR HIS GLY THR PHE LEU GLU ALA ALA GLN SER ILE VAL
SEQRES 5 B 214 PHE GLY GLY VAL ARG ALA ARG SER GLN ASP LEU ASP ALA
SEQRES 6 B 214 ILE TRP ARG GLY PHE TYR ILE ALA GLY ASP PRO ALA LEU
SEQRES 7 B 214 ALA TYR GLY TYR ALA GLN ASP GLN GLU PRO ASP ALA ARG
SEQRES 8 B 214 GLY ARG ILE ARG ASN GLY ALA LEU LEU ARG VAL TYR VAL
SEQRES 9 B 214 PRO ARG SER SER LEU PRO GLY PHE TYR ARG THR SER LEU
SEQRES 10 B 214 THR LEU ALA ALA PRO GLU ALA ALA GLY GLU VAL GLU ARG
SEQRES 11 B 214 LEU ILE GLY HIS PRO LEU PRO LEU ARG LEU ASP ALA ILE
SEQRES 12 B 214 THR GLY PRO GLU GLU GLU GLY GLY ARG LEU GLU THR ILE
SEQRES 13 B 214 LEU GLY TRP PRO LEU ALA GLU ARG THR VAL VAL ILE PRO
SEQRES 14 B 214 SER ALA ILE PRO THR ASP PRO ARG ASN VAL GLY GLY ASP
SEQRES 15 B 214 LEU ASP PRO SER SER ILE PRO ASP LYS GLU GLN ALA ILE
SEQRES 16 B 214 SER ALA LEU PRO ASP TYR ALA SER GLN PRO GLY LYS PRO
SEQRES 17 B 214 PRO ARG GLU ASP LEU LYS
HET NCA A 700 9
HET NCA B 700 9
HET AMP B 701 23
HETNAM NCA NICOTINAMIDE
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 3 NCA 2(C6 H6 N2 O)
FORMUL 5 AMP C10 H14 N5 O7 P
FORMUL 6 HOH *33(H2 O)
HELIX 1 1 VAL A 419 GLU A 431 1 13
HELIX 2 2 LEU A 444 VAL A 451 1 8
HELIX 3 3 PRO A 475 TYR A 481 1 7
HELIX 4 4 ARG A 505 GLY A 510 5 6
HELIX 5 5 ALA A 523 ILE A 531 1 9
HELIX 6 6 TRP A 558 ARG A 563 1 6
HELIX 7 7 PRO A 584 SER A 586 5 3
HELIX 8 8 ASP A 589 ILE A 594 1 6
HELIX 9 9 VAL B 419 ARG B 432 1 14
HELIX 10 10 LEU B 444 GLY B 453 1 10
HELIX 11 11 PRO B 475 GLY B 480 1 6
HELIX 12 12 SER B 507 GLY B 510 5 4
HELIX 13 13 PRO B 521 ILE B 531 1 11
HELIX 14 14 TRP B 558 ARG B 563 1 6
HELIX 15 15 PRO B 584 SER B 586 5 3
HELIX 16 16 ASP B 589 ILE B 594 1 6
SHEET 1 A 2 SER A 408 SER A 410 0
SHEET 2 A 2 GLY A 413 GLN A 415 -1 N GLN A 415 O SER A 408
SHEET 1 B 4 GLY A 468 ALA A 472 0
SHEET 2 B 4 LEU A 552 GLY A 557 -1 N LEU A 556 O PHE A 469
SHEET 3 B 4 ALA A 541 PRO A 545 -1 N GLY A 544 O GLU A 553
SHEET 4 B 4 PHE A 511 ARG A 513 1 N TYR A 512 O ALA A 541
SHEET 1 C 3 VAL A 565 PRO A 568 0
SHEET 2 C 3 GLY A 496 PRO A 504 -1 N TYR A 502 O VAL A 565
SHEET 3 C 3 TYR A 434 PHE A 443 -1 N THR A 442 O ALA A 497
SHEET 1 D 4 PHE B 469 ILE B 471 0
SHEET 2 D 4 GLU B 553 LEU B 556 -1 N LEU B 556 O PHE B 469
SHEET 3 D 4 ALA B 541 GLY B 544 -1 N GLY B 544 O GLU B 553
SHEET 4 D 4 PHE B 511 ARG B 513 1 N TYR B 512 O ALA B 541
SHEET 1 E 3 VAL B 565 PRO B 568 0
SHEET 2 E 3 GLY B 496 PRO B 504 -1 N TYR B 502 O VAL B 565
SHEET 3 E 3 TYR B 434 PHE B 443 -1 N THR B 442 O ALA B 497
CISPEP 1 LEU A 535 PRO A 536 0 0.64
CISPEP 2 LEU B 535 PRO B 536 0 0.34
SITE 1 AC1 7 HIS A 440 GLY A 441 TYR A 470 ILE A 471
SITE 2 AC1 7 ALA A 478 TYR A 481 GLU A 553
SITE 1 AC2 7 HIS B 440 GLY B 441 TYR B 470 ILE B 471
SITE 2 AC2 7 ALA B 472 TYR B 481 GLU B 553
SITE 1 AC3 12 ARG A 609 HOH B 12 HIS B 440 THR B 442
SITE 2 AC3 12 ALA B 446 SER B 449 GLY B 454 VAL B 455
SITE 3 AC3 12 ARG B 456 ALA B 457 ARG B 458 PHE B 469
CRYST1 87.510 87.510 134.080 90.00 90.00 90.00 P 43 21 2 16
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 0.011427 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011427 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007458 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
