HEADER BIOSYNTHETIC PROTEIN/TRANSFERASE 10-MAY-05 1ZM2
TITLE STRUCTURE OF ADP-RIBOSYLATED EEF2 IN COMPLEX WITH CATALYTIC FRAGMENT
TITLE 2 OF ETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR 2;
COMPND 3 CHAIN: A, C, E;
COMPND 4 FRAGMENT: EEF2;
COMPND 5 SYNONYM: EF-2;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EXOTOXIN A;
COMPND 8 CHAIN: B, D, F;
COMPND 9 FRAGMENT: CATALYTIC DOMAIN;
COMPND 10 SYNONYM: NAD-DEPENDENT ADP-RIBOSYLTRANSFERASE;
COMPND 11 EC: 2.4.2.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 7 ORGANISM_TAXID: 287;
SOURCE 8 GENE: ETA;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ELONGATION FACTOR, TOXIN, ADP-RIBOSYLATION, BIOSYNTHETIC PROTEIN-
KEYWDS 2 TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.JOERGENSEN,A.R.MERRILL,S.P.YATES,V.E.MARQUEZ,A.L.SCHWAN,T.BOESEN,
AUTHOR 2 G.R.ANDERSEN
REVDAT 4 23-AUG-23 1ZM2 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1ZM2 1 VERSN
REVDAT 2 30-AUG-05 1ZM2 1 JRNL
REVDAT 1 24-MAY-05 1ZM2 0
JRNL AUTH R.JOERGENSEN,A.R.MERRILL,S.P.YATES,V.E.MARQUEZ,A.L.SCHWAN,
JRNL AUTH 2 T.BOESEN,G.R.ANDERSEN
JRNL TITL EXOTOXIN A-EEF2 COMPLEX STRUCTURE INDICATES ADP RIBOSYLATION
JRNL TITL 2 BY RIBOSOME MIMICRY.
JRNL REF NATURE V. 436 979 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 16107839
JRNL DOI 10.1038/NATURE03871
REMARK 2
REMARK 2 RESOLUTION. 3.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 75835
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1521
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 : 23989
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 0
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) : 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) : NULL
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.450
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1ZM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032878.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.952
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75835
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.070
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRIES 1N0V AND 1AER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, MPD, HEPES, PH 7.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 165.31500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.92000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 165.31500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.92000
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, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 400
REMARK 400 COMPOUND RESIDUE 699 IS AN ADP-RIBOSYLATED DIPHTHAMIDE WHICH IS
REMARK 400 COMPOSED OF DDE WITH A LINK TO APR LIGANDS. THE COMPLETE ADP-
REMARK 400 RIBOSYLATED DIPHTHAMIDE CAN ONLY BE OBSERVED IN CHAIN E.
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 ALA A 49
REMARK 465 LYS A 50
REMARK 465 ALA A 51
REMARK 465 GLY A 52
REMARK 465 GLU A 53
REMARK 465 ALA A 54
REMARK 465 ARG A 55
REMARK 465 PHE A 56
REMARK 465 THR A 57
REMARK 465 ASP A 58
REMARK 465 THR A 59
REMARK 465 ARG A 60
REMARK 465 LYS A 61
REMARK 465 ASP A 62
REMARK 465 GLU A 63
REMARK 465 GLN A 64
REMARK 465 GLU A 65
REMARK 465 ARG A 66
REMARK 465 MET C 1
REMARK 465 ALA C 49
REMARK 465 LYS C 50
REMARK 465 ALA C 51
REMARK 465 GLY C 52
REMARK 465 GLU C 53
REMARK 465 ALA C 54
REMARK 465 ARG C 55
REMARK 465 PHE C 56
REMARK 465 THR C 57
REMARK 465 ASP C 58
REMARK 465 THR C 59
REMARK 465 ARG C 60
REMARK 465 LYS C 61
REMARK 465 ASP C 62
REMARK 465 GLU C 63
REMARK 465 GLN C 64
REMARK 465 GLU C 65
REMARK 465 ARG C 66
REMARK 465 MET E 1
REMARK 465 ALA E 49
REMARK 465 LYS E 50
REMARK 465 ALA E 51
REMARK 465 GLY E 52
REMARK 465 GLU E 53
REMARK 465 ALA E 54
REMARK 465 ARG E 55
REMARK 465 PHE E 56
REMARK 465 THR E 57
REMARK 465 ASP E 58
REMARK 465 THR E 59
REMARK 465 ARG E 60
REMARK 465 LYS E 61
REMARK 465 ASP E 62
REMARK 465 GLU E 63
REMARK 465 GLN E 64
REMARK 465 GLU E 65
REMARK 465 ARG E 66
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 DDE A 699 NAD CBI OAG CBW NCB CAB CAC
REMARK 470 DDE A 699 CAA CAU CAT
REMARK 470 GLU B 399 CG CD OE1 OE2
REMARK 470 DDE C 699 NAD CBI OAG CBW NCB CAB CAC
REMARK 470 DDE C 699 CAA CAU CAT
REMARK 470 GLU D 399 CG CD OE1 OE2
REMARK 470 GLU F 399 CG CD OE1 OE2
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 PRO E 559 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 PRO E 559 C - N - CD ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG F 494 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 PRO F 521 C - N - CA ANGL. DEV. = 11.9 DEGREES
REMARK 500 PRO F 521 C - N - CD ANGL. DEV. = -13.8 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 GLN A 41 3.28 -63.56
REMARK 500 SER A 72 109.83 -51.65
REMARK 500 GLN A 91 132.56 -176.19
REMARK 500 LYS A 92 138.05 -37.97
REMARK 500 ASP A 94 104.86 -168.53
REMARK 500 PHE A 111 18.31 -68.02
REMARK 500 SER A 112 -66.83 -8.90
REMARK 500 ARG A 150 61.50 68.77
REMARK 500 LEU A 164 -71.47 -75.51
REMARK 500 LEU A 215 -74.57 -45.45
REMARK 500 ALA A 287 -76.11 -57.96
REMARK 500 PRO A 345 2.95 -62.66
REMARK 500 ALA A 361 -3.00 -59.70
REMARK 500 CYS A 372 51.61 38.55
REMARK 500 ASP A 390 80.99 -63.90
REMARK 500 LYS A 391 -154.09 74.93
REMARK 500 ALA A 402 149.82 -170.66
REMARK 500 LYS A 422 -172.98 -69.66
REMARK 500 ILE A 428 89.76 -66.78
REMARK 500 ASP A 446 -71.76 -55.12
REMARK 500 CYS A 448 107.79 -167.88
REMARK 500 ASP A 460 -33.59 -31.44
REMARK 500 LYS A 465 -55.57 -140.52
REMARK 500 THR A 471 -31.22 -138.14
REMARK 500 LYS A 479 99.44 -19.67
REMARK 500 PRO A 487 104.16 -58.97
REMARK 500 ALA A 498 -17.55 -37.84
REMARK 500 SER A 525 -8.02 -56.56
REMARK 500 ASP A 548 -77.43 -129.40
REMARK 500 SER A 579 170.85 -57.73
REMARK 500 LYS A 582 21.36 86.66
REMARK 500 ASP A 610 -173.88 -61.10
REMARK 500 ASP A 621 -72.54 -66.20
REMARK 500 ASP A 639 33.23 38.49
REMARK 500 ASN A 641 11.10 -163.39
REMARK 500 TYR A 655 -2.33 73.13
REMARK 500 PHE A 677 37.47 -163.97
REMARK 500 ALA A 720 36.73 -77.66
REMARK 500 ASP A 721 86.40 52.98
REMARK 500 PRO A 761 -78.85 -24.07
REMARK 500 PRO A 764 35.46 -96.52
REMARK 500 SER A 806 157.07 -46.06
REMARK 500 SER A 813 171.74 -55.88
REMARK 500 SER B 459 72.49 61.74
REMARK 500 SER B 506 4.01 -58.08
REMARK 500 LEU B 518 -19.67 -41.12
REMARK 500 ALA B 520 145.79 -39.54
REMARK 500 ARG B 538 -96.82 -134.91
REMARK 500 LEU B 539 37.53 -93.95
REMARK 500 GLU B 548 117.96 -39.00
REMARK 500
REMARK 500 THIS ENTRY HAS 174 RAMACHANDRAN OUTLIERS.
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 APR E 843
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U2R RELATED DB: PDB
REMARK 900 STRUCTURE OF ADP-RIBOSYLATED EEF2 IN COMPLEX WITH SORDARIN
REMARK 900 RELATED ID: 1AER RELATED DB: PDB
REMARK 900 STRUCTURE OF CATALYTIC FRAGMENT OF ETA
REMARK 900 RELATED ID: 1ZM3 RELATED DB: PDB
REMARK 900 RELATED ID: 1ZM4 RELATED DB: PDB
REMARK 900 RELATED ID: 1ZM9 RELATED DB: PDB
DBREF 1ZM2 A 1 842 UNP P32324 EF2_YEAST 1 842
DBREF 1ZM2 C 1 842 UNP P32324 EF2_YEAST 1 842
DBREF 1ZM2 E 1 842 UNP P32324 EF2_YEAST 1 842
DBREF 1ZM2 B 399 605 GB 151216 AAB59097 424 630
DBREF 1ZM2 D 399 605 GB 151216 AAB59097 424 630
DBREF 1ZM2 F 399 605 GB 151216 AAB59097 424 630
SEQADV 1ZM2 DDE A 699 UNP P32324 HIS 699 MODIFIED RESIDUE
SEQADV 1ZM2 DDE C 699 UNP P32324 HIS 699 MODIFIED RESIDUE
SEQADV 1ZM2 DDE E 699 UNP P32324 HIS 699 MODIFIED RESIDUE
SEQRES 1 A 842 MET VAL ALA PHE THR VAL ASP GLN MET ARG SER LEU MET
SEQRES 2 A 842 ASP LYS VAL THR ASN VAL ARG ASN MET SER VAL ILE ALA
SEQRES 3 A 842 HIS VAL ASP HIS GLY LYS SER THR LEU THR ASP SER LEU
SEQRES 4 A 842 VAL GLN ARG ALA GLY ILE ILE SER ALA ALA LYS ALA GLY
SEQRES 5 A 842 GLU ALA ARG PHE THR ASP THR ARG LYS ASP GLU GLN GLU
SEQRES 6 A 842 ARG GLY ILE THR ILE LYS SER THR ALA ILE SER LEU TYR
SEQRES 7 A 842 SER GLU MET SER ASP GLU ASP VAL LYS GLU ILE LYS GLN
SEQRES 8 A 842 LYS THR ASP GLY ASN SER PHE LEU ILE ASN LEU ILE ASP
SEQRES 9 A 842 SER PRO GLY HIS VAL ASP PHE SER SER GLU VAL THR ALA
SEQRES 10 A 842 ALA LEU ARG VAL THR ASP GLY ALA LEU VAL VAL VAL ASP
SEQRES 11 A 842 THR ILE GLU GLY VAL CYS VAL GLN THR GLU THR VAL LEU
SEQRES 12 A 842 ARG GLN ALA LEU GLY GLU ARG ILE LYS PRO VAL VAL VAL
SEQRES 13 A 842 ILE ASN LYS VAL ASP ARG ALA LEU LEU GLU LEU GLN VAL
SEQRES 14 A 842 SER LYS GLU ASP LEU TYR GLN THR PHE ALA ARG THR VAL
SEQRES 15 A 842 GLU SER VAL ASN VAL ILE VAL SER THR TYR ALA ASP GLU
SEQRES 16 A 842 VAL LEU GLY ASP VAL GLN VAL TYR PRO ALA ARG GLY THR
SEQRES 17 A 842 VAL ALA PHE GLY SER GLY LEU HIS GLY TRP ALA PHE THR
SEQRES 18 A 842 ILE ARG GLN PHE ALA THR ARG TYR ALA LYS LYS PHE GLY
SEQRES 19 A 842 VAL ASP LYS ALA LYS MET MET ASP ARG LEU TRP GLY ASP
SEQRES 20 A 842 SER PHE PHE ASN PRO LYS THR LYS LYS TRP THR ASN LYS
SEQRES 21 A 842 ASP THR ASP ALA GLU GLY LYS PRO LEU GLU ARG ALA PHE
SEQRES 22 A 842 ASN MET PHE ILE LEU ASP PRO ILE PHE ARG LEU PHE THR
SEQRES 23 A 842 ALA ILE MET ASN PHE LYS LYS ASP GLU ILE PRO VAL LEU
SEQRES 24 A 842 LEU GLU LYS LEU GLU ILE VAL LEU LYS GLY ASP GLU LYS
SEQRES 25 A 842 ASP LEU GLU GLY LYS ALA LEU LEU LYS VAL VAL MET ARG
SEQRES 26 A 842 LYS PHE LEU PRO ALA ALA ASP ALA LEU LEU GLU MET ILE
SEQRES 27 A 842 VAL LEU HIS LEU PRO SER PRO VAL THR ALA GLN ALA TYR
SEQRES 28 A 842 ARG ALA GLU GLN LEU TYR GLU GLY PRO ALA ASP ASP ALA
SEQRES 29 A 842 ASN CYS ILE ALA ILE LYS ASN CYS ASP PRO LYS ALA ASP
SEQRES 30 A 842 LEU MET LEU TYR VAL SER LYS MET VAL PRO THR SER ASP
SEQRES 31 A 842 LYS GLY ARG PHE TYR ALA PHE GLY ARG VAL PHE ALA GLY
SEQRES 32 A 842 THR VAL LYS SER GLY GLN LYS VAL ARG ILE GLN GLY PRO
SEQRES 33 A 842 ASN TYR VAL PRO GLY LYS LYS ASP ASP LEU PHE ILE LYS
SEQRES 34 A 842 ALA ILE GLN ARG VAL VAL LEU MET MET GLY ARG PHE VAL
SEQRES 35 A 842 GLU PRO ILE ASP ASP CYS PRO ALA GLY ASN ILE ILE GLY
SEQRES 36 A 842 LEU VAL GLY ILE ASP GLN PHE LEU LEU LYS THR GLY THR
SEQRES 37 A 842 LEU THR THR SER GLU THR ALA HIS ASN MET LYS VAL MET
SEQRES 38 A 842 LYS PHE SER VAL SER PRO VAL VAL GLN VAL ALA VAL GLU
SEQRES 39 A 842 VAL LYS ASN ALA ASN ASP LEU PRO LYS LEU VAL GLU GLY
SEQRES 40 A 842 LEU LYS ARG LEU SER LYS SER ASP PRO CYS VAL LEU THR
SEQRES 41 A 842 TYR MET SER GLU SER GLY GLU HIS ILE VAL ALA GLY THR
SEQRES 42 A 842 GLY GLU LEU HIS LEU GLU ILE CYS LEU GLN ASP LEU GLU
SEQRES 43 A 842 HIS ASP HIS ALA GLY VAL PRO LEU LYS ILE SER PRO PRO
SEQRES 44 A 842 VAL VAL ALA TYR ARG GLU THR VAL GLU SER GLU SER SER
SEQRES 45 A 842 GLN THR ALA LEU SER LYS SER PRO ASN LYS HIS ASN ARG
SEQRES 46 A 842 ILE TYR LEU LYS ALA GLU PRO ILE ASP GLU GLU VAL SER
SEQRES 47 A 842 LEU ALA ILE GLU ASN GLY ILE ILE ASN PRO ARG ASP ASP
SEQRES 48 A 842 PHE LYS ALA ARG ALA ARG ILE MET ALA ASP ASP TYR GLY
SEQRES 49 A 842 TRP ASP VAL THR ASP ALA ARG LYS ILE TRP CYS PHE GLY
SEQRES 50 A 842 PRO ASP GLY ASN GLY PRO ASN LEU VAL ILE ASP GLN THR
SEQRES 51 A 842 LYS ALA VAL GLN TYR LEU HIS GLU ILE LYS ASP SER VAL
SEQRES 52 A 842 VAL ALA ALA PHE GLN TRP ALA THR LYS GLU GLY PRO ILE
SEQRES 53 A 842 PHE GLY GLU GLU MET ARG SER VAL ARG VAL ASN ILE LEU
SEQRES 54 A 842 ASP VAL THR LEU HIS ALA ASP ALA ILE DDE ARG GLY GLY
SEQRES 55 A 842 GLY GLN ILE ILE PRO THR MET ARG ARG ALA THR TYR ALA
SEQRES 56 A 842 GLY PHE LEU LEU ALA ASP PRO LYS ILE GLN GLU PRO VAL
SEQRES 57 A 842 PHE LEU VAL GLU ILE GLN CYS PRO GLU GLN ALA VAL GLY
SEQRES 58 A 842 GLY ILE TYR SER VAL LEU ASN LYS LYS ARG GLY GLN VAL
SEQRES 59 A 842 VAL SER GLU GLU GLN ARG PRO GLY THR PRO LEU PHE THR
SEQRES 60 A 842 VAL LYS ALA TYR LEU PRO VAL ASN GLU SER PHE GLY PHE
SEQRES 61 A 842 THR GLY GLU LEU ARG GLN ALA THR GLY GLY GLN ALA PHE
SEQRES 62 A 842 PRO GLN MET VAL PHE ASP HIS TRP SER THR LEU GLY SER
SEQRES 63 A 842 ASP PRO LEU ASP PRO THR SER LYS ALA GLY GLU ILE VAL
SEQRES 64 A 842 LEU ALA ALA ARG LYS ARG HIS GLY MET LYS GLU GLU VAL
SEQRES 65 A 842 PRO GLY TRP GLN GLU TYR TYR ASP LYS LEU
SEQRES 1 B 207 GLU PHE LEU GLY ASP GLY GLY ASP VAL SER PHE SER THR
SEQRES 2 B 207 ARG GLY THR GLN ASN TRP THR VAL GLU ARG LEU LEU GLN
SEQRES 3 B 207 ALA HIS ARG GLN LEU GLU GLU ARG GLY TYR VAL PHE VAL
SEQRES 4 B 207 GLY TYR HIS GLY THR PHE LEU GLU ALA ALA GLN SER ILE
SEQRES 5 B 207 VAL PHE GLY GLY VAL ARG ALA ARG SER GLN ASP LEU ASP
SEQRES 6 B 207 ALA ILE TRP ARG GLY PHE TYR ILE ALA GLY ASP PRO ALA
SEQRES 7 B 207 LEU ALA TYR GLY TYR ALA GLN ASP GLN GLU PRO ASP ALA
SEQRES 8 B 207 ARG GLY ARG ILE ARG ASN GLY ALA LEU LEU ARG VAL TYR
SEQRES 9 B 207 VAL PRO ARG SER SER LEU PRO GLY PHE TYR ARG THR SER
SEQRES 10 B 207 LEU THR LEU ALA ALA PRO GLU ALA ALA GLY GLU VAL GLU
SEQRES 11 B 207 ARG LEU ILE GLY HIS PRO LEU PRO LEU ARG LEU ASP ALA
SEQRES 12 B 207 ILE THR GLY PRO GLU GLU GLU GLY GLY ARG LEU GLU THR
SEQRES 13 B 207 ILE LEU GLY TRP PRO LEU ALA GLU ARG THR VAL VAL ILE
SEQRES 14 B 207 PRO SER ALA ILE PRO THR ASP PRO ARG ASN VAL GLY GLY
SEQRES 15 B 207 ASP LEU ASP PRO SER SER ILE PRO ASP LYS GLU GLN ALA
SEQRES 16 B 207 ILE SER ALA LEU PRO ASP TYR ALA SER GLN PRO GLY
SEQRES 1 C 842 MET VAL ALA PHE THR VAL ASP GLN MET ARG SER LEU MET
SEQRES 2 C 842 ASP LYS VAL THR ASN VAL ARG ASN MET SER VAL ILE ALA
SEQRES 3 C 842 HIS VAL ASP HIS GLY LYS SER THR LEU THR ASP SER LEU
SEQRES 4 C 842 VAL GLN ARG ALA GLY ILE ILE SER ALA ALA LYS ALA GLY
SEQRES 5 C 842 GLU ALA ARG PHE THR ASP THR ARG LYS ASP GLU GLN GLU
SEQRES 6 C 842 ARG GLY ILE THR ILE LYS SER THR ALA ILE SER LEU TYR
SEQRES 7 C 842 SER GLU MET SER ASP GLU ASP VAL LYS GLU ILE LYS GLN
SEQRES 8 C 842 LYS THR ASP GLY ASN SER PHE LEU ILE ASN LEU ILE ASP
SEQRES 9 C 842 SER PRO GLY HIS VAL ASP PHE SER SER GLU VAL THR ALA
SEQRES 10 C 842 ALA LEU ARG VAL THR ASP GLY ALA LEU VAL VAL VAL ASP
SEQRES 11 C 842 THR ILE GLU GLY VAL CYS VAL GLN THR GLU THR VAL LEU
SEQRES 12 C 842 ARG GLN ALA LEU GLY GLU ARG ILE LYS PRO VAL VAL VAL
SEQRES 13 C 842 ILE ASN LYS VAL ASP ARG ALA LEU LEU GLU LEU GLN VAL
SEQRES 14 C 842 SER LYS GLU ASP LEU TYR GLN THR PHE ALA ARG THR VAL
SEQRES 15 C 842 GLU SER VAL ASN VAL ILE VAL SER THR TYR ALA ASP GLU
SEQRES 16 C 842 VAL LEU GLY ASP VAL GLN VAL TYR PRO ALA ARG GLY THR
SEQRES 17 C 842 VAL ALA PHE GLY SER GLY LEU HIS GLY TRP ALA PHE THR
SEQRES 18 C 842 ILE ARG GLN PHE ALA THR ARG TYR ALA LYS LYS PHE GLY
SEQRES 19 C 842 VAL ASP LYS ALA LYS MET MET ASP ARG LEU TRP GLY ASP
SEQRES 20 C 842 SER PHE PHE ASN PRO LYS THR LYS LYS TRP THR ASN LYS
SEQRES 21 C 842 ASP THR ASP ALA GLU GLY LYS PRO LEU GLU ARG ALA PHE
SEQRES 22 C 842 ASN MET PHE ILE LEU ASP PRO ILE PHE ARG LEU PHE THR
SEQRES 23 C 842 ALA ILE MET ASN PHE LYS LYS ASP GLU ILE PRO VAL LEU
SEQRES 24 C 842 LEU GLU LYS LEU GLU ILE VAL LEU LYS GLY ASP GLU LYS
SEQRES 25 C 842 ASP LEU GLU GLY LYS ALA LEU LEU LYS VAL VAL MET ARG
SEQRES 26 C 842 LYS PHE LEU PRO ALA ALA ASP ALA LEU LEU GLU MET ILE
SEQRES 27 C 842 VAL LEU HIS LEU PRO SER PRO VAL THR ALA GLN ALA TYR
SEQRES 28 C 842 ARG ALA GLU GLN LEU TYR GLU GLY PRO ALA ASP ASP ALA
SEQRES 29 C 842 ASN CYS ILE ALA ILE LYS ASN CYS ASP PRO LYS ALA ASP
SEQRES 30 C 842 LEU MET LEU TYR VAL SER LYS MET VAL PRO THR SER ASP
SEQRES 31 C 842 LYS GLY ARG PHE TYR ALA PHE GLY ARG VAL PHE ALA GLY
SEQRES 32 C 842 THR VAL LYS SER GLY GLN LYS VAL ARG ILE GLN GLY PRO
SEQRES 33 C 842 ASN TYR VAL PRO GLY LYS LYS ASP ASP LEU PHE ILE LYS
SEQRES 34 C 842 ALA ILE GLN ARG VAL VAL LEU MET MET GLY ARG PHE VAL
SEQRES 35 C 842 GLU PRO ILE ASP ASP CYS PRO ALA GLY ASN ILE ILE GLY
SEQRES 36 C 842 LEU VAL GLY ILE ASP GLN PHE LEU LEU LYS THR GLY THR
SEQRES 37 C 842 LEU THR THR SER GLU THR ALA HIS ASN MET LYS VAL MET
SEQRES 38 C 842 LYS PHE SER VAL SER PRO VAL VAL GLN VAL ALA VAL GLU
SEQRES 39 C 842 VAL LYS ASN ALA ASN ASP LEU PRO LYS LEU VAL GLU GLY
SEQRES 40 C 842 LEU LYS ARG LEU SER LYS SER ASP PRO CYS VAL LEU THR
SEQRES 41 C 842 TYR MET SER GLU SER GLY GLU HIS ILE VAL ALA GLY THR
SEQRES 42 C 842 GLY GLU LEU HIS LEU GLU ILE CYS LEU GLN ASP LEU GLU
SEQRES 43 C 842 HIS ASP HIS ALA GLY VAL PRO LEU LYS ILE SER PRO PRO
SEQRES 44 C 842 VAL VAL ALA TYR ARG GLU THR VAL GLU SER GLU SER SER
SEQRES 45 C 842 GLN THR ALA LEU SER LYS SER PRO ASN LYS HIS ASN ARG
SEQRES 46 C 842 ILE TYR LEU LYS ALA GLU PRO ILE ASP GLU GLU VAL SER
SEQRES 47 C 842 LEU ALA ILE GLU ASN GLY ILE ILE ASN PRO ARG ASP ASP
SEQRES 48 C 842 PHE LYS ALA ARG ALA ARG ILE MET ALA ASP ASP TYR GLY
SEQRES 49 C 842 TRP ASP VAL THR ASP ALA ARG LYS ILE TRP CYS PHE GLY
SEQRES 50 C 842 PRO ASP GLY ASN GLY PRO ASN LEU VAL ILE ASP GLN THR
SEQRES 51 C 842 LYS ALA VAL GLN TYR LEU HIS GLU ILE LYS ASP SER VAL
SEQRES 52 C 842 VAL ALA ALA PHE GLN TRP ALA THR LYS GLU GLY PRO ILE
SEQRES 53 C 842 PHE GLY GLU GLU MET ARG SER VAL ARG VAL ASN ILE LEU
SEQRES 54 C 842 ASP VAL THR LEU HIS ALA ASP ALA ILE DDE ARG GLY GLY
SEQRES 55 C 842 GLY GLN ILE ILE PRO THR MET ARG ARG ALA THR TYR ALA
SEQRES 56 C 842 GLY PHE LEU LEU ALA ASP PRO LYS ILE GLN GLU PRO VAL
SEQRES 57 C 842 PHE LEU VAL GLU ILE GLN CYS PRO GLU GLN ALA VAL GLY
SEQRES 58 C 842 GLY ILE TYR SER VAL LEU ASN LYS LYS ARG GLY GLN VAL
SEQRES 59 C 842 VAL SER GLU GLU GLN ARG PRO GLY THR PRO LEU PHE THR
SEQRES 60 C 842 VAL LYS ALA TYR LEU PRO VAL ASN GLU SER PHE GLY PHE
SEQRES 61 C 842 THR GLY GLU LEU ARG GLN ALA THR GLY GLY GLN ALA PHE
SEQRES 62 C 842 PRO GLN MET VAL PHE ASP HIS TRP SER THR LEU GLY SER
SEQRES 63 C 842 ASP PRO LEU ASP PRO THR SER LYS ALA GLY GLU ILE VAL
SEQRES 64 C 842 LEU ALA ALA ARG LYS ARG HIS GLY MET LYS GLU GLU VAL
SEQRES 65 C 842 PRO GLY TRP GLN GLU TYR TYR ASP LYS LEU
SEQRES 1 D 207 GLU PHE LEU GLY ASP GLY GLY ASP VAL SER PHE SER THR
SEQRES 2 D 207 ARG GLY THR GLN ASN TRP THR VAL GLU ARG LEU LEU GLN
SEQRES 3 D 207 ALA HIS ARG GLN LEU GLU GLU ARG GLY TYR VAL PHE VAL
SEQRES 4 D 207 GLY TYR HIS GLY THR PHE LEU GLU ALA ALA GLN SER ILE
SEQRES 5 D 207 VAL PHE GLY GLY VAL ARG ALA ARG SER GLN ASP LEU ASP
SEQRES 6 D 207 ALA ILE TRP ARG GLY PHE TYR ILE ALA GLY ASP PRO ALA
SEQRES 7 D 207 LEU ALA TYR GLY TYR ALA GLN ASP GLN GLU PRO ASP ALA
SEQRES 8 D 207 ARG GLY ARG ILE ARG ASN GLY ALA LEU LEU ARG VAL TYR
SEQRES 9 D 207 VAL PRO ARG SER SER LEU PRO GLY PHE TYR ARG THR SER
SEQRES 10 D 207 LEU THR LEU ALA ALA PRO GLU ALA ALA GLY GLU VAL GLU
SEQRES 11 D 207 ARG LEU ILE GLY HIS PRO LEU PRO LEU ARG LEU ASP ALA
SEQRES 12 D 207 ILE THR GLY PRO GLU GLU GLU GLY GLY ARG LEU GLU THR
SEQRES 13 D 207 ILE LEU GLY TRP PRO LEU ALA GLU ARG THR VAL VAL ILE
SEQRES 14 D 207 PRO SER ALA ILE PRO THR ASP PRO ARG ASN VAL GLY GLY
SEQRES 15 D 207 ASP LEU ASP PRO SER SER ILE PRO ASP LYS GLU GLN ALA
SEQRES 16 D 207 ILE SER ALA LEU PRO ASP TYR ALA SER GLN PRO GLY
SEQRES 1 E 842 MET VAL ALA PHE THR VAL ASP GLN MET ARG SER LEU MET
SEQRES 2 E 842 ASP LYS VAL THR ASN VAL ARG ASN MET SER VAL ILE ALA
SEQRES 3 E 842 HIS VAL ASP HIS GLY LYS SER THR LEU THR ASP SER LEU
SEQRES 4 E 842 VAL GLN ARG ALA GLY ILE ILE SER ALA ALA LYS ALA GLY
SEQRES 5 E 842 GLU ALA ARG PHE THR ASP THR ARG LYS ASP GLU GLN GLU
SEQRES 6 E 842 ARG GLY ILE THR ILE LYS SER THR ALA ILE SER LEU TYR
SEQRES 7 E 842 SER GLU MET SER ASP GLU ASP VAL LYS GLU ILE LYS GLN
SEQRES 8 E 842 LYS THR ASP GLY ASN SER PHE LEU ILE ASN LEU ILE ASP
SEQRES 9 E 842 SER PRO GLY HIS VAL ASP PHE SER SER GLU VAL THR ALA
SEQRES 10 E 842 ALA LEU ARG VAL THR ASP GLY ALA LEU VAL VAL VAL ASP
SEQRES 11 E 842 THR ILE GLU GLY VAL CYS VAL GLN THR GLU THR VAL LEU
SEQRES 12 E 842 ARG GLN ALA LEU GLY GLU ARG ILE LYS PRO VAL VAL VAL
SEQRES 13 E 842 ILE ASN LYS VAL ASP ARG ALA LEU LEU GLU LEU GLN VAL
SEQRES 14 E 842 SER LYS GLU ASP LEU TYR GLN THR PHE ALA ARG THR VAL
SEQRES 15 E 842 GLU SER VAL ASN VAL ILE VAL SER THR TYR ALA ASP GLU
SEQRES 16 E 842 VAL LEU GLY ASP VAL GLN VAL TYR PRO ALA ARG GLY THR
SEQRES 17 E 842 VAL ALA PHE GLY SER GLY LEU HIS GLY TRP ALA PHE THR
SEQRES 18 E 842 ILE ARG GLN PHE ALA THR ARG TYR ALA LYS LYS PHE GLY
SEQRES 19 E 842 VAL ASP LYS ALA LYS MET MET ASP ARG LEU TRP GLY ASP
SEQRES 20 E 842 SER PHE PHE ASN PRO LYS THR LYS LYS TRP THR ASN LYS
SEQRES 21 E 842 ASP THR ASP ALA GLU GLY LYS PRO LEU GLU ARG ALA PHE
SEQRES 22 E 842 ASN MET PHE ILE LEU ASP PRO ILE PHE ARG LEU PHE THR
SEQRES 23 E 842 ALA ILE MET ASN PHE LYS LYS ASP GLU ILE PRO VAL LEU
SEQRES 24 E 842 LEU GLU LYS LEU GLU ILE VAL LEU LYS GLY ASP GLU LYS
SEQRES 25 E 842 ASP LEU GLU GLY LYS ALA LEU LEU LYS VAL VAL MET ARG
SEQRES 26 E 842 LYS PHE LEU PRO ALA ALA ASP ALA LEU LEU GLU MET ILE
SEQRES 27 E 842 VAL LEU HIS LEU PRO SER PRO VAL THR ALA GLN ALA TYR
SEQRES 28 E 842 ARG ALA GLU GLN LEU TYR GLU GLY PRO ALA ASP ASP ALA
SEQRES 29 E 842 ASN CYS ILE ALA ILE LYS ASN CYS ASP PRO LYS ALA ASP
SEQRES 30 E 842 LEU MET LEU TYR VAL SER LYS MET VAL PRO THR SER ASP
SEQRES 31 E 842 LYS GLY ARG PHE TYR ALA PHE GLY ARG VAL PHE ALA GLY
SEQRES 32 E 842 THR VAL LYS SER GLY GLN LYS VAL ARG ILE GLN GLY PRO
SEQRES 33 E 842 ASN TYR VAL PRO GLY LYS LYS ASP ASP LEU PHE ILE LYS
SEQRES 34 E 842 ALA ILE GLN ARG VAL VAL LEU MET MET GLY ARG PHE VAL
SEQRES 35 E 842 GLU PRO ILE ASP ASP CYS PRO ALA GLY ASN ILE ILE GLY
SEQRES 36 E 842 LEU VAL GLY ILE ASP GLN PHE LEU LEU LYS THR GLY THR
SEQRES 37 E 842 LEU THR THR SER GLU THR ALA HIS ASN MET LYS VAL MET
SEQRES 38 E 842 LYS PHE SER VAL SER PRO VAL VAL GLN VAL ALA VAL GLU
SEQRES 39 E 842 VAL LYS ASN ALA ASN ASP LEU PRO LYS LEU VAL GLU GLY
SEQRES 40 E 842 LEU LYS ARG LEU SER LYS SER ASP PRO CYS VAL LEU THR
SEQRES 41 E 842 TYR MET SER GLU SER GLY GLU HIS ILE VAL ALA GLY THR
SEQRES 42 E 842 GLY GLU LEU HIS LEU GLU ILE CYS LEU GLN ASP LEU GLU
SEQRES 43 E 842 HIS ASP HIS ALA GLY VAL PRO LEU LYS ILE SER PRO PRO
SEQRES 44 E 842 VAL VAL ALA TYR ARG GLU THR VAL GLU SER GLU SER SER
SEQRES 45 E 842 GLN THR ALA LEU SER LYS SER PRO ASN LYS HIS ASN ARG
SEQRES 46 E 842 ILE TYR LEU LYS ALA GLU PRO ILE ASP GLU GLU VAL SER
SEQRES 47 E 842 LEU ALA ILE GLU ASN GLY ILE ILE ASN PRO ARG ASP ASP
SEQRES 48 E 842 PHE LYS ALA ARG ALA ARG ILE MET ALA ASP ASP TYR GLY
SEQRES 49 E 842 TRP ASP VAL THR ASP ALA ARG LYS ILE TRP CYS PHE GLY
SEQRES 50 E 842 PRO ASP GLY ASN GLY PRO ASN LEU VAL ILE ASP GLN THR
SEQRES 51 E 842 LYS ALA VAL GLN TYR LEU HIS GLU ILE LYS ASP SER VAL
SEQRES 52 E 842 VAL ALA ALA PHE GLN TRP ALA THR LYS GLU GLY PRO ILE
SEQRES 53 E 842 PHE GLY GLU GLU MET ARG SER VAL ARG VAL ASN ILE LEU
SEQRES 54 E 842 ASP VAL THR LEU HIS ALA ASP ALA ILE DDE ARG GLY GLY
SEQRES 55 E 842 GLY GLN ILE ILE PRO THR MET ARG ARG ALA THR TYR ALA
SEQRES 56 E 842 GLY PHE LEU LEU ALA ASP PRO LYS ILE GLN GLU PRO VAL
SEQRES 57 E 842 PHE LEU VAL GLU ILE GLN CYS PRO GLU GLN ALA VAL GLY
SEQRES 58 E 842 GLY ILE TYR SER VAL LEU ASN LYS LYS ARG GLY GLN VAL
SEQRES 59 E 842 VAL SER GLU GLU GLN ARG PRO GLY THR PRO LEU PHE THR
SEQRES 60 E 842 VAL LYS ALA TYR LEU PRO VAL ASN GLU SER PHE GLY PHE
SEQRES 61 E 842 THR GLY GLU LEU ARG GLN ALA THR GLY GLY GLN ALA PHE
SEQRES 62 E 842 PRO GLN MET VAL PHE ASP HIS TRP SER THR LEU GLY SER
SEQRES 63 E 842 ASP PRO LEU ASP PRO THR SER LYS ALA GLY GLU ILE VAL
SEQRES 64 E 842 LEU ALA ALA ARG LYS ARG HIS GLY MET LYS GLU GLU VAL
SEQRES 65 E 842 PRO GLY TRP GLN GLU TYR TYR ASP LYS LEU
SEQRES 1 F 207 GLU PHE LEU GLY ASP GLY GLY ASP VAL SER PHE SER THR
SEQRES 2 F 207 ARG GLY THR GLN ASN TRP THR VAL GLU ARG LEU LEU GLN
SEQRES 3 F 207 ALA HIS ARG GLN LEU GLU GLU ARG GLY TYR VAL PHE VAL
SEQRES 4 F 207 GLY TYR HIS GLY THR PHE LEU GLU ALA ALA GLN SER ILE
SEQRES 5 F 207 VAL PHE GLY GLY VAL ARG ALA ARG SER GLN ASP LEU ASP
SEQRES 6 F 207 ALA ILE TRP ARG GLY PHE TYR ILE ALA GLY ASP PRO ALA
SEQRES 7 F 207 LEU ALA TYR GLY TYR ALA GLN ASP GLN GLU PRO ASP ALA
SEQRES 8 F 207 ARG GLY ARG ILE ARG ASN GLY ALA LEU LEU ARG VAL TYR
SEQRES 9 F 207 VAL PRO ARG SER SER LEU PRO GLY PHE TYR ARG THR SER
SEQRES 10 F 207 LEU THR LEU ALA ALA PRO GLU ALA ALA GLY GLU VAL GLU
SEQRES 11 F 207 ARG LEU ILE GLY HIS PRO LEU PRO LEU ARG LEU ASP ALA
SEQRES 12 F 207 ILE THR GLY PRO GLU GLU GLU GLY GLY ARG LEU GLU THR
SEQRES 13 F 207 ILE LEU GLY TRP PRO LEU ALA GLU ARG THR VAL VAL ILE
SEQRES 14 F 207 PRO SER ALA ILE PRO THR ASP PRO ARG ASN VAL GLY GLY
SEQRES 15 F 207 ASP LEU ASP PRO SER SER ILE PRO ASP LYS GLU GLN ALA
SEQRES 16 F 207 ILE SER ALA LEU PRO ASP TYR ALA SER GLN PRO GLY
MODRES 1ZM2 DDE A 699 HIS
MODRES 1ZM2 DDE C 699 HIS
MODRES 1ZM2 DDE E 699 HIS
HET DDE A 699 10
HET DDE C 699 10
HET DDE E 699 20
HET APR E 843 35
HETNAM DDE {3-[4-(2-AMINO-2-CARBOXY-ETHYL)-1H-IMIDAZOL-2-YL]-1-
HETNAM 2 DDE CARBAMOYL-PROPYL}-TRIMETHYL-AMMONIUM
HETNAM APR ADENOSINE-5-DIPHOSPHORIBOSE
HETSYN DDE DIPHTHAMIDE; 2-(3-CARBOXYAMIDO-3-(TRIMETHYLAMMONIO)
HETSYN 2 DDE PROPYL)HISTIDINE
FORMUL 1 DDE 3(C13 H24 N5 O3 1+)
FORMUL 7 APR C15 H23 N5 O14 P2
HELIX 1 1 THR A 5 MET A 13 1 9
HELIX 2 2 LYS A 15 THR A 17 5 3
HELIX 3 3 HIS A 27 HIS A 30 5 4
HELIX 4 4 GLY A 31 GLY A 44 1 14
HELIX 5 5 SER A 82 GLU A 88 1 7
HELIX 6 6 HIS A 108 ASP A 110 5 3
HELIX 7 7 PHE A 111 THR A 122 1 12
HELIX 8 8 CYS A 136 GLU A 149 1 14
HELIX 9 9 LYS A 159 GLU A 166 1 8
HELIX 10 10 SER A 170 ALA A 193 1 24
HELIX 11 11 TYR A 203 GLY A 207 5 5
HELIX 12 12 ILE A 222 PHE A 233 1 12
HELIX 13 13 ASP A 236 LEU A 244 1 9
HELIX 14 14 ARG A 271 ILE A 277 1 7
HELIX 15 15 ILE A 277 ASN A 290 1 14
HELIX 16 16 ASP A 294 LEU A 303 1 10
HELIX 17 17 LYS A 308 GLU A 315 5 8
HELIX 18 18 GLY A 316 LEU A 328 1 13
HELIX 19 19 PRO A 329 LEU A 342 1 14
HELIX 20 20 ALA A 348 TYR A 357 1 10
HELIX 21 21 ASP A 363 ASN A 371 1 9
HELIX 22 22 ASN A 497 ASN A 499 5 3
HELIX 23 23 ASP A 500 ASP A 515 1 16
HELIX 24 24 GLY A 534 ASP A 548 1 15
HELIX 25 25 ASP A 594 ASN A 603 1 10
HELIX 26 26 ASP A 611 GLY A 624 1 14
HELIX 27 27 ASP A 626 ARG A 631 1 6
HELIX 28 28 TYR A 655 GLU A 658 5 4
HELIX 29 29 ILE A 659 THR A 671 1 13
HELIX 30 30 ASP A 696 ARG A 700 5 5
HELIX 31 31 GLY A 701 ALA A 720 1 20
HELIX 32 32 ALA A 739 ASN A 748 1 10
HELIX 33 33 ASN A 775 SER A 777 5 3
HELIX 34 34 GLY A 779 THR A 788 1 10
HELIX 35 35 SER A 813 HIS A 826 1 14
HELIX 36 36 GLY A 834 TYR A 839 1 6
HELIX 37 37 THR B 418 ARG B 432 1 15
HELIX 38 38 PHE B 443 PHE B 452 1 10
HELIX 39 39 ASP B 474 GLY B 480 1 7
HELIX 40 40 SER B 506 PRO B 509 5 4
HELIX 41 41 ALA B 520 GLY B 532 1 13
HELIX 42 42 GLY B 557 GLU B 562 1 6
HELIX 43 43 ASP B 583 ILE B 587 5 5
HELIX 44 44 PRO B 588 ILE B 594 1 7
HELIX 45 45 THR C 5 MET C 13 1 9
HELIX 46 46 ASP C 14 THR C 17 5 4
HELIX 47 47 HIS C 27 HIS C 30 5 4
HELIX 48 48 GLY C 31 GLY C 44 1 14
HELIX 49 49 SER C 82 GLU C 88 1 7
HELIX 50 50 HIS C 108 ASP C 110 5 3
HELIX 51 51 PHE C 111 ARG C 120 1 10
HELIX 52 52 CYS C 136 GLU C 149 1 14
HELIX 53 53 VAL C 160 GLU C 166 1 7
HELIX 54 54 SER C 170 ALA C 193 1 24
HELIX 55 55 TYR C 203 GLY C 207 5 5
HELIX 56 56 THR C 221 LYS C 232 1 12
HELIX 57 57 ASP C 236 LEU C 244 1 9
HELIX 58 58 ARG C 271 ILE C 277 1 7
HELIX 59 59 ILE C 277 ASN C 290 1 14
HELIX 60 60 ASP C 294 LEU C 303 1 10
HELIX 61 61 LYS C 308 LEU C 314 5 7
HELIX 62 62 ALA C 318 LEU C 328 1 11
HELIX 63 63 PRO C 329 LEU C 342 1 14
HELIX 64 64 SER C 344 TYR C 357 1 14
HELIX 65 65 ASP C 363 ASN C 371 1 9
HELIX 66 66 LEU C 501 ASP C 515 1 15
HELIX 67 67 GLY C 534 ASP C 548 1 15
HELIX 68 68 ASP C 594 ASN C 603 1 10
HELIX 69 69 ASP C 611 GLY C 624 1 14
HELIX 70 70 ASP C 626 LYS C 632 1 7
HELIX 71 71 TYR C 655 GLU C 658 5 4
HELIX 72 72 ILE C 659 GLU C 673 1 15
HELIX 73 73 ASP C 696 ARG C 700 5 5
HELIX 74 74 GLY C 701 ALA C 720 1 20
HELIX 75 75 ALA C 739 ASN C 748 1 10
HELIX 76 76 ASN C 775 SER C 777 5 3
HELIX 77 77 GLY C 779 THR C 788 1 10
HELIX 78 78 SER C 813 HIS C 826 1 14
HELIX 79 79 GLY C 834 TYR C 838 5 5
HELIX 80 80 THR D 418 ARG D 432 1 15
HELIX 81 81 PHE D 443 PHE D 452 1 10
HELIX 82 82 ASP D 474 GLY D 480 1 7
HELIX 83 83 SER D 506 PRO D 509 5 4
HELIX 84 84 GLU D 522 GLY D 532 1 11
HELIX 85 85 GLY D 557 GLU D 562 1 6
HELIX 86 86 ASP D 583 ILE D 587 5 5
HELIX 87 87 PRO D 588 ILE D 594 1 7
HELIX 88 88 THR E 5 MET E 13 1 9
HELIX 89 89 ASP E 14 THR E 17 5 4
HELIX 90 90 HIS E 27 HIS E 30 5 4
HELIX 91 91 GLY E 31 GLY E 44 1 14
HELIX 92 92 GLU E 84 ILE E 89 1 6
HELIX 93 93 HIS E 108 ASP E 110 5 3
HELIX 94 94 PHE E 111 THR E 122 1 12
HELIX 95 95 CYS E 136 GLU E 149 1 14
HELIX 96 96 VAL E 160 GLU E 166 1 7
HELIX 97 97 SER E 170 ALA E 193 1 24
HELIX 98 98 TYR E 203 GLY E 207 5 5
HELIX 99 99 GLN E 224 PHE E 233 1 10
HELIX 100 100 ASP E 236 TRP E 245 1 10
HELIX 101 101 ARG E 271 ILE E 277 1 7
HELIX 102 102 ILE E 277 ASN E 290 1 14
HELIX 103 103 ASP E 294 GLU E 304 1 11
HELIX 104 104 GLY E 316 LEU E 328 1 13
HELIX 105 105 PRO E 329 HIS E 341 1 13
HELIX 106 106 THR E 347 TYR E 357 1 11
HELIX 107 107 ASP E 363 ASN E 371 1 9
HELIX 108 108 ASP E 500 ASP E 515 1 16
HELIX 109 109 GLY E 534 ASP E 548 1 15
HELIX 110 110 ASP E 594 ASN E 603 1 10
HELIX 111 111 ASP E 611 GLY E 624 1 14
HELIX 112 112 ASP E 626 ARG E 631 1 6
HELIX 113 113 TYR E 655 GLU E 658 5 4
HELIX 114 114 ILE E 659 GLU E 673 1 15
HELIX 115 115 ASP E 696 ARG E 700 5 5
HELIX 116 116 GLY E 701 ALA E 720 1 20
HELIX 117 117 ALA E 739 ASN E 748 1 10
HELIX 118 118 ASN E 775 SER E 777 5 3
HELIX 119 119 GLY E 779 THR E 788 1 10
HELIX 120 120 SER E 813 HIS E 826 1 14
HELIX 121 121 GLY E 834 TYR E 838 5 5
HELIX 122 122 THR F 418 GLU F 431 1 14
HELIX 123 123 PHE F 443 PHE F 452 1 10
HELIX 124 124 ASP F 474 GLY F 480 1 7
HELIX 125 125 SER F 506 PRO F 509 5 4
HELIX 126 126 GLU F 522 GLY F 532 1 11
HELIX 127 127 GLY F 557 GLU F 562 1 6
HELIX 128 128 ASP F 583 ILE F 587 5 5
HELIX 129 129 PRO F 588 SER F 595 1 8
SHEET 1 A 2 ALA A 3 PHE A 4 0
SHEET 2 A 2 ILE A 46 SER A 47 1 O ILE A 46 N PHE A 4
SHEET 1 B 7 ALA A 74 GLU A 80 0
SHEET 2 B 7 SER A 97 ILE A 103 -1 O ILE A 100 N LEU A 77
SHEET 3 B 7 VAL A 19 SER A 23 1 N ARG A 20 O LEU A 99
SHEET 4 B 7 GLY A 124 ASP A 130 1 N GLY A 124 O ASN A 21
SHEET 5 B 7 LYS A 152 ASN A 158 1 O VAL A 156 N VAL A 129
SHEET 6 B 7 VAL A 209 SER A 213 1 O ALA A 210 N ILE A 157
SHEET 7 B 7 TRP A 218 THR A 221 -1 O TRP A 218 N SER A 213
SHEET 1 C 2 PHE A 249 PHE A 250 0
SHEET 2 C 2 TRP A 257 THR A 258 -1 O THR A 258 N PHE A 249
SHEET 1 D 8 LEU A 426 ALA A 430 0
SHEET 2 D 8 LYS A 410 GLN A 414 -1 N VAL A 411 O LYS A 429
SHEET 3 D 8 GLY A 467 THR A 470 -1 O THR A 468 N GLN A 414
SHEET 4 D 8 MET A 379 PRO A 387 -1 N LEU A 380 O LEU A 469
SHEET 5 D 8 PHE A 394 ALA A 402 -1 O ARG A 399 N TYR A 381
SHEET 6 D 8 ILE A 453 VAL A 457 -1 O LEU A 456 N ALA A 396
SHEET 7 D 8 ARG A 433 MET A 438 -1 N VAL A 435 O GLY A 455
SHEET 8 D 8 PHE A 441 PRO A 444 -1 O GLU A 443 N LEU A 436
SHEET 1 E 2 THR A 404 LYS A 406 0
SHEET 2 E 2 ASP A 447 PRO A 449 -1 O CYS A 448 N VAL A 405
SHEET 1 F 4 LEU A 519 MET A 522 0
SHEET 2 F 4 HIS A 528 GLY A 532 -1 O ILE A 529 N TYR A 521
SHEET 3 F 4 VAL A 489 VAL A 495 -1 N VAL A 489 O GLY A 532
SHEET 4 F 4 LEU A 554 ILE A 556 -1 O LYS A 555 N GLU A 494
SHEET 1 G 4 LEU A 519 MET A 522 0
SHEET 2 G 4 HIS A 528 GLY A 532 -1 O ILE A 529 N TYR A 521
SHEET 3 G 4 VAL A 489 VAL A 495 -1 N VAL A 489 O GLY A 532
SHEET 4 G 4 VAL A 560 VAL A 561 -1 O VAL A 560 N GLN A 490
SHEET 1 H 5 GLU A 680 MET A 681 0
SHEET 2 H 5 ARG A 564 VAL A 567 1 N GLU A 565 O GLU A 680
SHEET 3 H 5 PRO A 722 PRO A 736 -1 O GLN A 725 N ARG A 564
SHEET 4 H 5 LEU A 765 PRO A 773 -1 O LEU A 772 N PHE A 729
SHEET 5 H 5 GLN A 753 GLN A 759 -1 N VAL A 755 O LYS A 769
SHEET 1 I 4 GLU A 680 MET A 681 0
SHEET 2 I 4 ARG A 564 VAL A 567 1 N GLU A 565 O GLU A 680
SHEET 3 I 4 PRO A 722 PRO A 736 -1 O GLN A 725 N ARG A 564
SHEET 4 I 4 PHE A 793 THR A 803 -1 O SER A 802 N GLU A 726
SHEET 1 J 5 ALA A 575 LYS A 578 0
SHEET 2 J 5 ARG A 585 PRO A 592 -1 O LEU A 588 N ALA A 575
SHEET 3 J 5 VAL A 684 THR A 692 -1 O ASN A 687 N LYS A 589
SHEET 4 J 5 ASN A 644 ILE A 647 1 N ILE A 647 O VAL A 686
SHEET 5 J 5 ILE A 633 PHE A 636 -1 N TRP A 634 O VAL A 646
SHEET 1 K 3 TYR B 434 THR B 442 0
SHEET 2 K 3 ALA B 497 PRO B 504 -1 O LEU B 499 N HIS B 440
SHEET 3 K 3 VAL B 565 PRO B 568 -1 O ILE B 567 N ARG B 500
SHEET 1 L 4 PHE B 469 ILE B 471 0
SHEET 2 L 4 LEU B 552 LEU B 556 -1 O LEU B 556 N PHE B 469
SHEET 3 L 4 ALA B 541 PRO B 545 -1 N ILE B 542 O ILE B 555
SHEET 4 L 4 PHE B 511 ARG B 513 1 N TYR B 512 O ALA B 541
SHEET 1 M 2 ALA C 3 PHE C 4 0
SHEET 2 M 2 ILE C 46 SER C 47 1 O ILE C 46 N PHE C 4
SHEET 1 N 7 ALA C 74 GLU C 80 0
SHEET 2 N 7 SER C 97 ILE C 103 -1 O ILE C 100 N LEU C 77
SHEET 3 N 7 VAL C 19 SER C 23 1 N ARG C 20 O ASN C 101
SHEET 4 N 7 GLY C 124 ASP C 130 1 N GLY C 124 O ASN C 21
SHEET 5 N 7 LYS C 152 ASN C 158 1 O ASN C 158 N VAL C 129
SHEET 6 N 7 VAL C 209 SER C 213 1 O ALA C 210 N ILE C 157
SHEET 7 N 7 TRP C 218 PHE C 220 -1 O TRP C 218 N SER C 213
SHEET 1 O 2 PHE C 249 PHE C 250 0
SHEET 2 O 2 TRP C 257 THR C 258 -1 O THR C 258 N PHE C 249
SHEET 1 P 8 LEU C 426 ALA C 430 0
SHEET 2 P 8 LYS C 410 GLN C 414 -1 N VAL C 411 O LYS C 429
SHEET 3 P 8 GLY C 467 THR C 470 -1 O THR C 468 N GLN C 414
SHEET 4 P 8 MET C 379 PRO C 387 -1 N VAL C 382 O GLY C 467
SHEET 5 P 8 PHE C 394 ALA C 402 -1 O PHE C 397 N LYS C 384
SHEET 6 P 8 ILE C 453 VAL C 457 -1 O LEU C 456 N ALA C 396
SHEET 7 P 8 ARG C 433 MET C 438 -1 N VAL C 435 O GLY C 455
SHEET 8 P 8 PHE C 441 PRO C 444 -1 O GLU C 443 N LEU C 436
SHEET 1 Q 2 THR C 404 LYS C 406 0
SHEET 2 Q 2 ASP C 447 PRO C 449 -1 O CYS C 448 N VAL C 405
SHEET 1 R 2 VAL C 489 GLN C 490 0
SHEET 2 R 2 VAL C 560 VAL C 561 -1 O VAL C 560 N GLN C 490
SHEET 1 S 2 LEU C 519 SER C 523 0
SHEET 2 S 2 GLU C 527 ALA C 531 -1 O ILE C 529 N TYR C 521
SHEET 1 T 5 GLU C 680 MET C 681 0
SHEET 2 T 5 ARG C 564 VAL C 567 1 N GLU C 565 O GLU C 680
SHEET 3 T 5 PRO C 722 PRO C 736 -1 O LYS C 723 N THR C 566
SHEET 4 T 5 LEU C 765 PRO C 773 -1 O VAL C 768 N ILE C 733
SHEET 5 T 5 GLN C 753 GLN C 759 -1 N SER C 756 O LYS C 769
SHEET 1 U 4 GLU C 680 MET C 681 0
SHEET 2 U 4 ARG C 564 VAL C 567 1 N GLU C 565 O GLU C 680
SHEET 3 U 4 PRO C 722 PRO C 736 -1 O LYS C 723 N THR C 566
SHEET 4 U 4 MET C 796 THR C 803 -1 O SER C 802 N GLU C 726
SHEET 1 V 5 ALA C 575 LYS C 578 0
SHEET 2 V 5 ARG C 585 PRO C 592 -1 O LEU C 588 N ALA C 575
SHEET 3 V 5 VAL C 684 THR C 692 -1 O ASP C 690 N TYR C 587
SHEET 4 V 5 ASN C 644 ASP C 648 1 N ILE C 647 O VAL C 686
SHEET 5 V 5 ILE C 633 PHE C 636 -1 N TRP C 634 O VAL C 646
SHEET 1 W 3 TYR D 434 THR D 442 0
SHEET 2 W 3 ALA D 497 PRO D 504 -1 O VAL D 501 N GLY D 438
SHEET 3 W 3 VAL D 565 PRO D 568 -1 O ILE D 567 N ARG D 500
SHEET 1 X 4 PHE D 469 ILE D 471 0
SHEET 2 X 4 LEU D 552 LEU D 556 -1 O LEU D 556 N PHE D 469
SHEET 3 X 4 ALA D 541 PRO D 545 -1 N ILE D 542 O ILE D 555
SHEET 4 X 4 PHE D 511 ARG D 513 1 N TYR D 512 O ALA D 541
SHEET 1 Y 2 ALA E 3 PHE E 4 0
SHEET 2 Y 2 ILE E 46 SER E 47 1 O ILE E 46 N PHE E 4
SHEET 1 Z 7 ALA E 74 GLU E 80 0
SHEET 2 Z 7 SER E 97 ILE E 103 -1 O LEU E 102 N ILE E 75
SHEET 3 Z 7 VAL E 19 SER E 23 1 N ARG E 20 O LEU E 99
SHEET 4 Z 7 GLY E 124 ASP E 130 1 O LEU E 126 N SER E 23
SHEET 5 Z 7 LYS E 152 ASN E 158 1 O ASN E 158 N VAL E 129
SHEET 6 Z 7 VAL E 209 SER E 213 1 O ALA E 210 N ILE E 157
SHEET 7 Z 7 TRP E 218 THR E 221 -1 O PHE E 220 N PHE E 211
SHEET 1 AA 2 PHE E 249 ASN E 251 0
SHEET 2 AA 2 LYS E 256 THR E 258 -1 O THR E 258 N PHE E 249
SHEET 1 AB 8 LYS E 429 ALA E 430 0
SHEET 2 AB 8 LYS E 410 GLN E 414 -1 N VAL E 411 O LYS E 429
SHEET 3 AB 8 GLY E 467 THR E 470 -1 O THR E 468 N GLN E 414
SHEET 4 AB 8 MET E 379 PRO E 387 -1 N LEU E 380 O LEU E 469
SHEET 5 AB 8 PHE E 394 ALA E 402 -1 O ARG E 399 N TYR E 381
SHEET 6 AB 8 ILE E 453 VAL E 457 -1 O LEU E 456 N ALA E 396
SHEET 7 AB 8 ARG E 433 MET E 438 -1 N VAL E 435 O GLY E 455
SHEET 8 AB 8 PHE E 441 PRO E 444 -1 O GLU E 443 N LEU E 436
SHEET 1 AC 2 THR E 404 LYS E 406 0
SHEET 2 AC 2 ASP E 447 PRO E 449 -1 O CYS E 448 N VAL E 405
SHEET 1 AD 4 LEU E 519 MET E 522 0
SHEET 2 AD 4 HIS E 528 GLY E 532 -1 O ALA E 531 N LEU E 519
SHEET 3 AD 4 VAL E 489 VAL E 495 -1 N VAL E 489 O GLY E 532
SHEET 4 AD 4 LEU E 554 ILE E 556 -1 O LYS E 555 N GLU E 494
SHEET 1 AE 4 LEU E 519 MET E 522 0
SHEET 2 AE 4 HIS E 528 GLY E 532 -1 O ALA E 531 N LEU E 519
SHEET 3 AE 4 VAL E 489 VAL E 495 -1 N VAL E 489 O GLY E 532
SHEET 4 AE 4 VAL E 560 VAL E 561 -1 O VAL E 560 N GLN E 490
SHEET 1 AF 5 GLU E 680 MET E 681 0
SHEET 2 AF 5 ARG E 564 VAL E 567 1 N GLU E 565 O GLU E 680
SHEET 3 AF 5 PRO E 722 PRO E 736 -1 O GLN E 725 N ARG E 564
SHEET 4 AF 5 LEU E 765 PRO E 773 -1 O LEU E 772 N PHE E 729
SHEET 5 AF 5 GLN E 753 GLN E 759 -1 N SER E 756 O LYS E 769
SHEET 1 AG 4 GLU E 680 MET E 681 0
SHEET 2 AG 4 ARG E 564 VAL E 567 1 N GLU E 565 O GLU E 680
SHEET 3 AG 4 PRO E 722 PRO E 736 -1 O GLN E 725 N ARG E 564
SHEET 4 AG 4 MET E 796 THR E 803 -1 O SER E 802 N GLU E 726
SHEET 1 AH 5 ALA E 575 LYS E 578 0
SHEET 2 AH 5 ARG E 585 PRO E 592 -1 O LEU E 588 N ALA E 575
SHEET 3 AH 5 VAL E 684 THR E 692 -1 O ARG E 685 N GLU E 591
SHEET 4 AH 5 ASN E 644 ASP E 648 1 N ILE E 647 O VAL E 686
SHEET 5 AH 5 ILE E 633 PHE E 636 -1 N TRP E 634 O VAL E 646
SHEET 1 AI 3 TYR F 434 THR F 442 0
SHEET 2 AI 3 ALA F 497 PRO F 504 -1 O LEU F 499 N HIS F 440
SHEET 3 AI 3 VAL F 565 PRO F 568 -1 O ILE F 567 N ARG F 500
SHEET 1 AJ 4 PHE F 469 ILE F 471 0
SHEET 2 AJ 4 LEU F 552 LEU F 556 -1 O THR F 554 N ILE F 471
SHEET 3 AJ 4 ALA F 541 PRO F 545 -1 N GLY F 544 O GLU F 553
SHEET 4 AJ 4 PHE F 511 ARG F 513 1 N TYR F 512 O ALA F 541
LINK C ILE A 698 N DDE A 699 1555 1555 1.33
LINK C DDE A 699 N ARG A 700 1555 1555 1.34
LINK C ILE C 698 N DDE C 699 1555 1555 1.32
LINK C DDE C 699 N ARG C 700 1555 1555 1.33
LINK C ILE E 698 N DDE E 699 1555 1555 1.34
LINK C DDE E 699 N ARG E 700 1555 1555 1.32
LINK NE2 DDE E 699 C1D APR E 843 1555 1555 1.38
CISPEP 1 GLY A 637 PRO A 638 0 0.12
CISPEP 2 LEU B 535 PRO B 536 0 0.47
CISPEP 3 GLY C 637 PRO C 638 0 -1.91
CISPEP 4 LEU D 535 PRO D 536 0 0.51
CISPEP 5 GLY E 637 PRO E 638 0 0.20
CISPEP 6 LEU F 535 PRO F 536 0 0.51
SITE 1 AC1 6 HIS E 694 ASP E 696 DDE E 699 ALA F 464
SITE 2 AC1 6 TYR F 470 TYR F 481
CRYST1 330.630 67.840 191.500 90.00 103.30 90.00 C 1 2 1 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 0.003025 0.000000 0.000715 0.00000
SCALE2 0.000000 0.014741 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005366 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
