HEADER TRANSLATION 15-OCT-02 1N0V
TITLE CRYSTAL STRUCTURE OF ELONGATION FACTOR 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR 2;
COMPND 3 CHAIN: C, D;
COMPND 4 SYNONYM: EF-2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS G-PROTEIN CIS-PROLINE, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.JOERGENSEN,P.A.ORTIZ,A.CARR-SCHMID,P.NISSEN,T.G.KINZY,G.R.ANDERSEN
REVDAT 6 03-APR-24 1N0V 1 REMARK
REVDAT 5 14-FEB-24 1N0V 1 REMARK
REVDAT 4 31-JAN-18 1N0V 1 REMARK
REVDAT 3 24-FEB-09 1N0V 1 VERSN
REVDAT 2 08-MAR-05 1N0V 1 JRNL REMARK MASTER
REVDAT 1 27-NOV-02 1N0V 0
JRNL AUTH R.JOERGENSEN,P.A.ORTIZ,A.CARR-SCHMID,P.NISSEN,T.G.KINZY,
JRNL AUTH 2 G.R.ANDERSEN
JRNL TITL TWO CRYSTAL STRUCTURES DEMONSTRATE LARGE CONFORMATIONAL
JRNL TITL 2 CHANGES IN THE EUKARYOTIC RIBOSOMAL TRANSLOCASE.
JRNL REF NAT.STRUCT.BIOL. V. 10 379 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12692531
JRNL DOI 10.1038/NSB923
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.JOERGENSEN,A.CARR-SCHMID,P.A.ORTIZ,T.G.KINZY,G.R.ANDERSEN
REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF THE YEAST ELONGATION
REMARK 1 TITL 2 FACTOR EEF2
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 712 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444902003001
REMARK 2
REMARK 2 RESOLUTION. 2.85 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) : 2.85
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 : 45917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1101
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 : 12838
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.420
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1N0V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-01
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 : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.038
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45917
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31600
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: AMORE
REMARK 200 STARTING MODEL: STRUCTURE OF EEF2-SORDARIN COMPLEX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, HEPES, ETHYLENE GLYCOL;
REMARK 280 MAGNESIUM CHLORIDE, GDP, EDTA, DTT, PH 7.2, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 100K
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 49.41750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.27300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.41750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.27300
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 300 REMARK: THE MOLECULE FUNCTIONS AS A MONOMER
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 APPLY THE FOLLOWING TO CHAINS: C
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 APPLY THE FOLLOWING TO CHAINS: 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 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 C 1
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 D 1
REMARK 465 ALA D 51
REMARK 465 GLY D 52
REMARK 465 GLU D 53
REMARK 465 ALA D 54
REMARK 465 ARG D 55
REMARK 465 PHE D 56
REMARK 465 THR D 57
REMARK 465 ASP D 58
REMARK 465 THR D 59
REMARK 465 ARG D 60
REMARK 465 LYS D 61
REMARK 465 ASP D 62
REMARK 465 GLU D 63
REMARK 465 GLN D 64
REMARK 465 GLU D 65
REMARK 465 ARG D 66
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 C 761 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 PRO C 761 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 ASP D 263 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 PRO D 268 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 THR C 5 -173.15 -66.32
REMARK 500 SER C 47 132.10 -36.58
REMARK 500 ALA C 49 170.87 66.72
REMARK 500 LYS C 90 50.76 -69.41
REMARK 500 SER C 112 -64.89 10.20
REMARK 500 ARG C 150 38.54 71.08
REMARK 500 LYS C 159 55.52 73.58
REMARK 500 GLU C 166 -79.20 -63.13
REMARK 500 VAL C 169 -172.21 -67.69
REMARK 500 ILE C 188 -75.90 -64.61
REMARK 500 VAL C 189 -39.11 -32.57
REMARK 500 ASP C 194 143.85 -35.95
REMARK 500 VAL C 200 22.98 -72.48
REMARK 500 LEU C 215 -73.51 -61.62
REMARK 500 ARG C 228 -77.38 -67.20
REMARK 500 LYS C 232 8.84 -61.09
REMARK 500 ALA C 264 -125.52 69.86
REMARK 500 GLU C 265 31.85 -89.54
REMARK 500 PHE C 291 52.90 37.22
REMARK 500 LYS C 293 -30.05 -37.81
REMARK 500 ILE C 296 -48.26 -25.37
REMARK 500 GLU C 304 39.48 81.81
REMARK 500 ASP C 310 -66.56 -27.78
REMARK 500 GLU C 311 -38.90 -36.65
REMARK 500 LYS C 321 6.05 -60.03
REMARK 500 PRO C 329 87.50 -48.01
REMARK 500 ALA C 330 -42.85 -29.46
REMARK 500 PRO C 360 130.70 -39.74
REMARK 500 ASP C 363 160.67 -47.38
REMARK 500 ASP C 390 66.74 -66.29
REMARK 500 LYS C 391 -152.00 74.37
REMARK 500 ASN C 417 35.62 -89.29
REMARK 500 MET C 437 71.13 -100.61
REMARK 500 GLN C 461 3.65 -69.64
REMARK 500 LYS C 465 -57.60 -147.11
REMARK 500 LYS C 479 105.89 -46.29
REMARK 500 ALA C 498 -65.34 -17.33
REMARK 500 LEU C 536 -74.72 -51.34
REMARK 500 ASP C 548 -75.94 -109.82
REMARK 500 SER C 579 171.31 -51.05
REMARK 500 LYS C 582 -13.55 105.32
REMARK 500 ASP C 610 165.88 -44.55
REMARK 500 VAL C 627 -25.34 -35.43
REMARK 500 CYS C 635 161.32 174.48
REMARK 500 ASP C 639 14.95 57.11
REMARK 500 ALA C 652 74.67 36.66
REMARK 500 ASP C 661 -70.21 -43.60
REMARK 500 PHE C 677 31.99 -158.35
REMARK 500 ALA C 720 41.78 -106.68
REMARK 500 ASP C 721 80.53 48.89
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FNM RELATED DB: PDB
REMARK 900 STRUCTURE OF EF-G
REMARK 900 RELATED ID: 1N0U RELATED DB: PDB
REMARK 900 STRUCTURE OF EEF2 IN COMPLEX WITH SORDARIN
DBREF 1N0V C 1 842 UNP P32324 EF2_YEAST 1 842
DBREF 1N0V D 1 842 UNP P32324 EF2_YEAST 1 842
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 HIS 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 842 MET VAL ALA PHE THR VAL ASP GLN MET ARG SER LEU MET
SEQRES 2 D 842 ASP LYS VAL THR ASN VAL ARG ASN MET SER VAL ILE ALA
SEQRES 3 D 842 HIS VAL ASP HIS GLY LYS SER THR LEU THR ASP SER LEU
SEQRES 4 D 842 VAL GLN ARG ALA GLY ILE ILE SER ALA ALA LYS ALA GLY
SEQRES 5 D 842 GLU ALA ARG PHE THR ASP THR ARG LYS ASP GLU GLN GLU
SEQRES 6 D 842 ARG GLY ILE THR ILE LYS SER THR ALA ILE SER LEU TYR
SEQRES 7 D 842 SER GLU MET SER ASP GLU ASP VAL LYS GLU ILE LYS GLN
SEQRES 8 D 842 LYS THR ASP GLY ASN SER PHE LEU ILE ASN LEU ILE ASP
SEQRES 9 D 842 SER PRO GLY HIS VAL ASP PHE SER SER GLU VAL THR ALA
SEQRES 10 D 842 ALA LEU ARG VAL THR ASP GLY ALA LEU VAL VAL VAL ASP
SEQRES 11 D 842 THR ILE GLU GLY VAL CYS VAL GLN THR GLU THR VAL LEU
SEQRES 12 D 842 ARG GLN ALA LEU GLY GLU ARG ILE LYS PRO VAL VAL VAL
SEQRES 13 D 842 ILE ASN LYS VAL ASP ARG ALA LEU LEU GLU LEU GLN VAL
SEQRES 14 D 842 SER LYS GLU ASP LEU TYR GLN THR PHE ALA ARG THR VAL
SEQRES 15 D 842 GLU SER VAL ASN VAL ILE VAL SER THR TYR ALA ASP GLU
SEQRES 16 D 842 VAL LEU GLY ASP VAL GLN VAL TYR PRO ALA ARG GLY THR
SEQRES 17 D 842 VAL ALA PHE GLY SER GLY LEU HIS GLY TRP ALA PHE THR
SEQRES 18 D 842 ILE ARG GLN PHE ALA THR ARG TYR ALA LYS LYS PHE GLY
SEQRES 19 D 842 VAL ASP LYS ALA LYS MET MET ASP ARG LEU TRP GLY ASP
SEQRES 20 D 842 SER PHE PHE ASN PRO LYS THR LYS LYS TRP THR ASN LYS
SEQRES 21 D 842 ASP THR ASP ALA GLU GLY LYS PRO LEU GLU ARG ALA PHE
SEQRES 22 D 842 ASN MET PHE ILE LEU ASP PRO ILE PHE ARG LEU PHE THR
SEQRES 23 D 842 ALA ILE MET ASN PHE LYS LYS ASP GLU ILE PRO VAL LEU
SEQRES 24 D 842 LEU GLU LYS LEU GLU ILE VAL LEU LYS GLY ASP GLU LYS
SEQRES 25 D 842 ASP LEU GLU GLY LYS ALA LEU LEU LYS VAL VAL MET ARG
SEQRES 26 D 842 LYS PHE LEU PRO ALA ALA ASP ALA LEU LEU GLU MET ILE
SEQRES 27 D 842 VAL LEU HIS LEU PRO SER PRO VAL THR ALA GLN ALA TYR
SEQRES 28 D 842 ARG ALA GLU GLN LEU TYR GLU GLY PRO ALA ASP ASP ALA
SEQRES 29 D 842 ASN CYS ILE ALA ILE LYS ASN CYS ASP PRO LYS ALA ASP
SEQRES 30 D 842 LEU MET LEU TYR VAL SER LYS MET VAL PRO THR SER ASP
SEQRES 31 D 842 LYS GLY ARG PHE TYR ALA PHE GLY ARG VAL PHE ALA GLY
SEQRES 32 D 842 THR VAL LYS SER GLY GLN LYS VAL ARG ILE GLN GLY PRO
SEQRES 33 D 842 ASN TYR VAL PRO GLY LYS LYS ASP ASP LEU PHE ILE LYS
SEQRES 34 D 842 ALA ILE GLN ARG VAL VAL LEU MET MET GLY ARG PHE VAL
SEQRES 35 D 842 GLU PRO ILE ASP ASP CYS PRO ALA GLY ASN ILE ILE GLY
SEQRES 36 D 842 LEU VAL GLY ILE ASP GLN PHE LEU LEU LYS THR GLY THR
SEQRES 37 D 842 LEU THR THR SER GLU THR ALA HIS ASN MET LYS VAL MET
SEQRES 38 D 842 LYS PHE SER VAL SER PRO VAL VAL GLN VAL ALA VAL GLU
SEQRES 39 D 842 VAL LYS ASN ALA ASN ASP LEU PRO LYS LEU VAL GLU GLY
SEQRES 40 D 842 LEU LYS ARG LEU SER LYS SER ASP PRO CYS VAL LEU THR
SEQRES 41 D 842 TYR MET SER GLU SER GLY GLU HIS ILE VAL ALA GLY THR
SEQRES 42 D 842 GLY GLU LEU HIS LEU GLU ILE CYS LEU GLN ASP LEU GLU
SEQRES 43 D 842 HIS ASP HIS ALA GLY VAL PRO LEU LYS ILE SER PRO PRO
SEQRES 44 D 842 VAL VAL ALA TYR ARG GLU THR VAL GLU SER GLU SER SER
SEQRES 45 D 842 GLN THR ALA LEU SER LYS SER PRO ASN LYS HIS ASN ARG
SEQRES 46 D 842 ILE TYR LEU LYS ALA GLU PRO ILE ASP GLU GLU VAL SER
SEQRES 47 D 842 LEU ALA ILE GLU ASN GLY ILE ILE ASN PRO ARG ASP ASP
SEQRES 48 D 842 PHE LYS ALA ARG ALA ARG ILE MET ALA ASP ASP TYR GLY
SEQRES 49 D 842 TRP ASP VAL THR ASP ALA ARG LYS ILE TRP CYS PHE GLY
SEQRES 50 D 842 PRO ASP GLY ASN GLY PRO ASN LEU VAL ILE ASP GLN THR
SEQRES 51 D 842 LYS ALA VAL GLN TYR LEU HIS GLU ILE LYS ASP SER VAL
SEQRES 52 D 842 VAL ALA ALA PHE GLN TRP ALA THR LYS GLU GLY PRO ILE
SEQRES 53 D 842 PHE GLY GLU GLU MET ARG SER VAL ARG VAL ASN ILE LEU
SEQRES 54 D 842 ASP VAL THR LEU HIS ALA ASP ALA ILE HIS ARG GLY GLY
SEQRES 55 D 842 GLY GLN ILE ILE PRO THR MET ARG ARG ALA THR TYR ALA
SEQRES 56 D 842 GLY PHE LEU LEU ALA ASP PRO LYS ILE GLN GLU PRO VAL
SEQRES 57 D 842 PHE LEU VAL GLU ILE GLN CYS PRO GLU GLN ALA VAL GLY
SEQRES 58 D 842 GLY ILE TYR SER VAL LEU ASN LYS LYS ARG GLY GLN VAL
SEQRES 59 D 842 VAL SER GLU GLU GLN ARG PRO GLY THR PRO LEU PHE THR
SEQRES 60 D 842 VAL LYS ALA TYR LEU PRO VAL ASN GLU SER PHE GLY PHE
SEQRES 61 D 842 THR GLY GLU LEU ARG GLN ALA THR GLY GLY GLN ALA PHE
SEQRES 62 D 842 PRO GLN MET VAL PHE ASP HIS TRP SER THR LEU GLY SER
SEQRES 63 D 842 ASP PRO LEU ASP PRO THR SER LYS ALA GLY GLU ILE VAL
SEQRES 64 D 842 LEU ALA ALA ARG LYS ARG HIS GLY MET LYS GLU GLU VAL
SEQRES 65 D 842 PRO GLY TRP GLN GLU TYR TYR ASP LYS LEU
HELIX 1 1 THR C 5 MET C 13 1 9
HELIX 2 2 LYS C 15 THR C 17 5 3
HELIX 3 3 HIS C 27 HIS C 30 5 4
HELIX 4 4 GLY C 31 GLY C 44 1 14
HELIX 5 5 SER C 82 LYS C 87 1 6
HELIX 6 6 HIS C 108 ASP C 110 5 3
HELIX 7 7 PHE C 111 VAL C 121 1 11
HELIX 8 8 CYS C 136 GLU C 149 1 14
HELIX 9 9 LYS C 159 GLU C 166 1 8
HELIX 10 10 SER C 170 TYR C 192 1 23
HELIX 11 11 THR C 221 LYS C 232 1 12
HELIX 12 12 ASP C 236 LEU C 244 1 9
HELIX 13 13 ARG C 271 ILE C 277 1 7
HELIX 14 14 ILE C 277 ASN C 290 1 14
HELIX 15 15 ASP C 294 GLU C 304 1 11
HELIX 16 16 LYS C 308 LEU C 314 5 7
HELIX 17 17 GLU C 315 LEU C 328 1 14
HELIX 18 18 PRO C 329 LEU C 342 1 14
HELIX 19 19 SER C 344 TYR C 357 1 14
HELIX 20 20 ASP C 363 ASN C 371 1 9
HELIX 21 21 ILE C 459 LEU C 463 5 5
HELIX 22 22 ASN C 497 ASN C 499 5 3
HELIX 23 23 ASP C 500 ASP C 515 1 16
HELIX 24 24 GLY C 534 ASP C 548 1 15
HELIX 25 25 ASP C 594 ASN C 603 1 10
HELIX 26 26 ASP C 611 GLY C 624 1 14
HELIX 27 27 ASP C 626 LYS C 632 1 7
HELIX 28 28 TYR C 655 GLU C 658 5 4
HELIX 29 29 ILE C 659 GLU C 673 1 15
HELIX 30 30 ASP C 696 ARG C 700 5 5
HELIX 31 31 GLY C 701 LEU C 719 1 19
HELIX 32 32 ALA C 739 LYS C 749 1 11
HELIX 33 33 ASN C 775 SER C 777 5 3
HELIX 34 34 GLY C 779 ALA C 787 1 9
HELIX 35 35 SER C 813 HIS C 826 1 14
HELIX 36 36 GLY C 834 TYR C 838 5 5
HELIX 37 37 THR D 5 LYS D 15 1 11
HELIX 38 38 HIS D 27 HIS D 30 5 4
HELIX 39 39 GLY D 31 GLY D 44 1 14
HELIX 40 40 SER D 82 GLU D 88 1 7
HELIX 41 41 HIS D 108 ASP D 110 5 3
HELIX 42 42 PHE D 111 ARG D 120 1 10
HELIX 43 43 CYS D 136 GLU D 149 1 14
HELIX 44 44 VAL D 160 GLU D 166 1 7
HELIX 45 45 SER D 170 ALA D 193 1 24
HELIX 46 46 TYR D 203 GLY D 207 5 5
HELIX 47 47 ILE D 222 PHE D 233 1 12
HELIX 48 48 ASP D 236 LEU D 244 1 9
HELIX 49 49 ARG D 271 ILE D 277 1 7
HELIX 50 50 ILE D 277 MET D 289 1 13
HELIX 51 51 GLU D 295 GLU D 304 1 10
HELIX 52 52 LYS D 308 ASP D 313 5 6
HELIX 53 53 GLY D 316 LEU D 328 1 13
HELIX 54 54 PRO D 329 LEU D 342 1 14
HELIX 55 55 SER D 344 TYR D 357 1 14
HELIX 56 56 ASP D 363 CYS D 372 1 10
HELIX 57 57 ASN D 497 ASN D 499 5 3
HELIX 58 58 ASP D 500 ASP D 515 1 16
HELIX 59 59 GLY D 534 HIS D 547 1 14
HELIX 60 60 ASP D 594 ASN D 603 1 10
HELIX 61 61 ASP D 611 GLY D 624 1 14
HELIX 62 62 ASP D 626 LYS D 632 1 7
HELIX 63 63 TYR D 655 GLU D 658 5 4
HELIX 64 64 ILE D 659 GLU D 673 1 15
HELIX 65 65 ASP D 696 ARG D 700 5 5
HELIX 66 66 GLY D 701 LEU D 719 1 19
HELIX 67 67 ALA D 739 LYS D 749 1 11
HELIX 68 68 ASN D 775 SER D 777 5 3
HELIX 69 69 GLY D 779 GLY D 789 1 11
HELIX 70 70 SER D 813 HIS D 826 1 14
HELIX 71 71 GLY D 834 TYR D 839 5 6
SHEET 1 A 7 ALA C 74 GLU C 80 0
SHEET 2 A 7 SER C 97 ILE C 103 -1 N PHE C 98 O SER C 79
SHEET 3 A 7 VAL C 19 ILE C 25 1 O ARG C 20 N ASN C 101
SHEET 4 A 7 GLY C 124 ASP C 130 1 N GLY C 124 O ASN C 21
SHEET 5 A 7 LYS C 152 ASN C 158 1 O LYS C 152 N ALA C 125
SHEET 6 A 7 VAL C 209 SER C 213 1 O ALA C 210 N ILE C 157
SHEET 7 A 7 TRP C 218 PHE C 220 -1 O TRP C 218 N SER C 213
SHEET 1 B 2 PHE C 249 ASN C 251 0
SHEET 2 B 2 LYS C 256 THR C 258 -1 O LYS C 256 N ASN C 251
SHEET 1 C 2 THR C 262 ASP C 263 0
SHEET 2 C 2 LYS C 267 PRO C 268 -1 N LYS C 267 O ASP C 263
SHEET 1 D 8 PHE C 441 ILE C 445 0
SHEET 2 D 8 ARG C 433 MET C 438 -1 O VAL C 434 N ILE C 445
SHEET 3 D 8 ILE C 453 VAL C 457 -1 N GLY C 455 O VAL C 435
SHEET 4 D 8 PHE C 394 ALA C 402 -1 N ALA C 396 O LEU C 456
SHEET 5 D 8 MET C 379 PRO C 387 -1 O MET C 379 N PHE C 401
SHEET 6 D 8 GLY C 467 THR C 470 -1 O GLY C 467 N VAL C 382
SHEET 7 D 8 LYS C 410 GLN C 414 -1 N ARG C 412 O THR C 470
SHEET 8 D 8 LEU C 426 ALA C 430 -1 O PHE C 427 N ILE C 413
SHEET 1 E 2 THR C 404 LYS C 406 0
SHEET 2 E 2 ASP C 447 PRO C 449 -1 O CYS C 448 N VAL C 405
SHEET 1 F 6 LEU C 554 ILE C 556 0
SHEET 2 F 6 VAL C 489 VAL C 495 -1 O GLU C 494 N LYS C 555
SHEET 3 F 6 VAL C 560 VAL C 561 -1 N VAL C 560 O GLN C 490
SHEET 4 F 6 VAL C 489 VAL C 495 -1 O GLN C 490 N VAL C 560
SHEET 5 F 6 HIS C 528 GLY C 532 -1 O HIS C 528 N VAL C 493
SHEET 6 F 6 LEU C 519 MET C 522 -1 O LEU C 519 N ALA C 531
SHEET 1 G 6 ARG C 564 VAL C 567 0
SHEET 2 G 6 PRO C 722 PRO C 736 -1 O LYS C 723 N THR C 566
SHEET 3 G 6 MET C 796 THR C 803 -1 O VAL C 797 N LEU C 730
SHEET 4 G 6 PRO C 722 PRO C 736 -1 N GLU C 726 O SER C 802
SHEET 5 G 6 LEU C 765 PRO C 773 -1 O PHE C 766 N CYS C 735
SHEET 6 G 6 GLN C 753 GLN C 759 -1 O GLN C 753 N TYR C 771
SHEET 1 H 5 ALA C 575 LYS C 578 0
SHEET 2 H 5 ARG C 585 PRO C 592 -1 N ILE C 586 O SER C 577
SHEET 3 H 5 VAL C 684 THR C 692 -1 N ARG C 685 O GLU C 591
SHEET 4 H 5 ASN C 644 ASP C 648 1 N LEU C 645 O VAL C 684
SHEET 5 H 5 ILE C 633 PHE C 636 -1 N TRP C 634 O VAL C 646
SHEET 1 I 2 ALA D 3 PHE D 4 0
SHEET 2 I 2 ILE D 46 SER D 47 1 O ILE D 46 N PHE D 4
SHEET 1 J 7 ALA D 74 GLU D 80 0
SHEET 2 J 7 SER D 97 ILE D 103 -1 N PHE D 98 O SER D 79
SHEET 3 J 7 VAL D 19 ILE D 25 1 O ARG D 20 N ASN D 101
SHEET 4 J 7 GLY D 124 ASP D 130 1 N GLY D 124 O ASN D 21
SHEET 5 J 7 LYS D 152 ASN D 158 1 O LYS D 152 N ALA D 125
SHEET 6 J 7 VAL D 209 SER D 213 1 O ALA D 210 N ILE D 157
SHEET 7 J 7 TRP D 218 THR D 221 -1 O TRP D 218 N SER D 213
SHEET 1 K 2 PHE D 249 ASN D 251 0
SHEET 2 K 2 LYS D 256 THR D 258 -1 O LYS D 256 N ASN D 251
SHEET 1 L 8 PHE D 441 PRO D 444 0
SHEET 2 L 8 ARG D 433 MET D 438 -1 N LEU D 436 O GLU D 443
SHEET 3 L 8 ILE D 453 VAL D 457 -1 O GLY D 455 N VAL D 435
SHEET 4 L 8 PHE D 394 ALA D 402 -1 N ALA D 396 O LEU D 456
SHEET 5 L 8 MET D 379 PRO D 387 -1 O MET D 379 N PHE D 401
SHEET 6 L 8 GLY D 467 THR D 470 -1 O GLY D 467 N VAL D 382
SHEET 7 L 8 LYS D 410 GLN D 414 -1 N ARG D 412 O THR D 470
SHEET 8 L 8 LEU D 426 ALA D 430 -1 O PHE D 427 N ILE D 413
SHEET 1 M 2 THR D 404 LYS D 406 0
SHEET 2 M 2 ASP D 447 PRO D 449 -1 N CYS D 448 O VAL D 405
SHEET 1 N 6 LEU D 519 MET D 522 0
SHEET 2 N 6 HIS D 528 GLY D 532 -1 N ILE D 529 O TYR D 521
SHEET 3 N 6 VAL D 489 VAL D 495 -1 O VAL D 489 N GLY D 532
SHEET 4 N 6 LEU D 554 ILE D 556 -1 N LYS D 555 O GLU D 494
SHEET 5 N 6 VAL D 489 VAL D 495 -1 O GLU D 494 N LYS D 555
SHEET 6 N 6 VAL D 560 VAL D 561 -1 N VAL D 560 O GLN D 490
SHEET 1 O 6 ARG D 564 VAL D 567 0
SHEET 2 O 6 PRO D 722 PRO D 736 -1 O LYS D 723 N THR D 566
SHEET 3 O 6 MET D 796 THR D 803 -1 O VAL D 797 N LEU D 730
SHEET 4 O 6 PRO D 722 PRO D 736 -1 O GLU D 726 N SER D 802
SHEET 5 O 6 LEU D 765 PRO D 773 -1 O PHE D 766 N CYS D 735
SHEET 6 O 6 GLN D 753 GLN D 759 -1 O GLN D 753 N TYR D 771
SHEET 1 P 5 ALA D 575 LYS D 578 0
SHEET 2 P 5 ARG D 585 PRO D 592 -1 N ILE D 586 O SER D 577
SHEET 3 P 5 VAL D 684 THR D 692 -1 N ARG D 685 O GLU D 591
SHEET 4 P 5 ASN D 644 ASP D 648 1 O LEU D 645 N VAL D 686
SHEET 5 P 5 ILE D 633 PHE D 636 -1 N TRP D 634 O VAL D 646
CISPEP 1 GLY C 637 PRO C 638 0 -0.02
CISPEP 2 GLY D 637 PRO D 638 0 0.32
CRYST1 98.835 114.546 177.310 90.00 90.00 90.00 P 21 21 21 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 0.010118 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
