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HEADER HYDROLASE 26-APR-21 7EP9
TITLE THE STRUCTURE OF CARBOXYPEPTIDASE FROM FUSOBACTERIUM NUCLEATUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S9 FAMILY PEPTIDASE;
COMPND 3 CHAIN: G, A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSOBACTERIUM NUCLEATUM;
SOURCE 3 ORGANISM_TAXID: 851;
SOURCE 4 GENE: BKN39_05345;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FUSOBACTERIUM NUCLEATUM; SERINE PEPTIDASE; CRYSTAL SCREENING,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WANG,Y.L.JIANG
REVDAT 1 27-OCT-21 7EP9 0
JRNL AUTH X.WANG,W.T.HOU,R.XIA,M.T.CHENG
JRNL TITL EXPRESSION ,PURIFICATION AND CRYSTALLIZATION OF A SERINE
JRNL TITL 2 PEPTIDASE FROM FUSOBACTERIUM NUCLEATUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3228
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 94966
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 4942
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.8300 - 8.0752 0.95 3082 172 0.1862 0.1917
REMARK 3 2 8.0752 - 6.4156 1.00 3082 179 0.2010 0.2148
REMARK 3 3 6.4156 - 5.6063 1.00 3089 162 0.1962 0.2001
REMARK 3 4 5.6063 - 5.0945 1.00 3057 183 0.1867 0.2234
REMARK 3 5 5.0945 - 4.7298 1.00 3021 186 0.1826 0.2320
REMARK 3 6 4.7298 - 4.4512 1.00 3009 173 0.1941 0.2394
REMARK 3 7 4.4512 - 4.2285 1.00 3038 183 0.1950 0.2342
REMARK 3 8 4.2285 - 4.0445 1.00 3006 164 0.2054 0.2338
REMARK 3 9 4.0445 - 3.8889 1.00 3014 159 0.2197 0.2628
REMARK 3 10 3.8889 - 3.7548 1.00 3030 148 0.2223 0.2721
REMARK 3 11 3.7548 - 3.6374 1.00 3026 164 0.2259 0.2956
REMARK 3 12 3.6374 - 3.5335 1.00 2977 176 0.2356 0.3180
REMARK 3 13 3.5335 - 3.4405 1.00 3005 166 0.2345 0.3043
REMARK 3 14 3.4405 - 3.3566 1.00 3007 155 0.2468 0.2720
REMARK 3 15 3.3566 - 3.2803 1.00 2981 162 0.2508 0.3197
REMARK 3 16 3.2803 - 3.2105 1.00 2988 167 0.2526 0.3313
REMARK 3 17 3.2105 - 3.1463 1.00 3003 164 0.2614 0.2973
REMARK 3 18 3.1463 - 3.0870 1.00 3026 129 0.2594 0.3212
REMARK 3 19 3.0870 - 3.0318 1.00 3005 145 0.2664 0.3342
REMARK 3 20 3.0318 - 2.9805 1.00 2996 163 0.2608 0.3308
REMARK 3 21 2.9805 - 2.9324 1.00 2959 174 0.2629 0.2877
REMARK 3 22 2.9324 - 2.8873 1.00 2964 182 0.2783 0.3684
REMARK 3 23 2.8873 - 2.8448 1.00 2969 172 0.2913 0.3282
REMARK 3 24 2.8448 - 2.8048 1.00 2974 170 0.2939 0.3511
REMARK 3 25 2.8048 - 2.7669 1.00 2957 168 0.2848 0.3606
REMARK 3 26 2.7669 - 2.7309 1.00 3002 166 0.2807 0.3401
REMARK 3 27 2.7309 - 2.6968 1.00 2994 144 0.2988 0.3221
REMARK 3 28 2.6968 - 2.6643 1.00 2993 158 0.2843 0.3667
REMARK 3 29 2.6643 - 2.6333 1.00 2939 165 0.2967 0.3737
REMARK 3 30 2.6333 - 2.6040 0.95 2831 143 0.3137 0.3662
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7EP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1300021945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95180
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21%PEG_2000 AND 0.1 M TRIS PH 7.9,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 96.00200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.39850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 96.00200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.39850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, A, B, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU C 146 NH2 ARG C 151 1.99
REMARK 500 OG1 THR A 74 OD1 ASP A 102 2.06
REMARK 500 OG SER A 61 OE2 GLU A 64 2.15
REMARK 500 OG SER B 61 OE2 GLU B 64 2.17
REMARK 500 OD1 ASP G 501 NH1 ARG G 535 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER G 40 -159.45 -147.16
REMARK 500 ASN G 71 -158.39 -150.99
REMARK 500 PRO G 116 36.23 -81.11
REMARK 500 ILE G 125 -61.06 -90.33
REMARK 500 ASP G 168 23.95 -150.66
REMARK 500 ILE G 200 -59.37 -122.80
REMARK 500 GLU G 214 -117.94 54.21
REMARK 500 GLU G 262 -114.20 49.75
REMARK 500 LYS G 264 -150.85 -128.75
REMARK 500 SER G 270 130.84 -178.36
REMARK 500 MET G 272 46.67 -75.93
REMARK 500 LEU G 302 73.36 -64.02
REMARK 500 SER G 308 149.67 -176.50
REMARK 500 ALA G 332 -68.51 -172.87
REMARK 500 SER G 351 50.68 -145.27
REMARK 500 ALA G 362 -87.05 -124.56
REMARK 500 ASN G 363 74.09 -116.97
REMARK 500 ASN G 364 16.30 58.76
REMARK 500 SER G 392 44.58 -144.82
REMARK 500 LYS G 445 59.54 -108.00
REMARK 500 THR G 446 -165.29 -124.88
REMARK 500 TYR G 477 33.84 -150.39
REMARK 500 THR G 490 -92.66 -110.31
REMARK 500 ASP G 510 97.90 -62.83
REMARK 500 SER G 520 -123.11 57.15
REMARK 500 ARG G 543 50.67 31.34
REMARK 500 THR G 569 147.35 -172.14
REMARK 500 ASN G 632 -155.37 -132.21
REMARK 500 ASN A 17 61.61 62.58
REMARK 500 SER A 40 -156.53 -136.39
REMARK 500 LEU A 68 148.00 -173.94
REMARK 500 ASP A 168 27.84 -152.03
REMARK 500 LYS A 182 18.89 58.96
REMARK 500 LYS A 213 -66.01 -101.81
REMARK 500 GLU A 214 -68.19 -129.63
REMARK 500 LEU A 252 -60.27 -107.19
REMARK 500 GLU A 262 -125.40 58.05
REMARK 500 ALA A 332 -86.13 -148.22
REMARK 500 ALA A 362 -68.63 -130.18
REMARK 500 ASN A 364 19.56 56.91
REMARK 500 THR A 418 -166.83 -122.36
REMARK 500 THR A 446 -168.74 -128.47
REMARK 500 THR A 490 -88.71 -116.41
REMARK 500 SER A 520 -118.30 52.73
REMARK 500 ARG A 543 51.33 32.94
REMARK 500 PRO A 570 -9.28 -54.07
REMARK 500 ASN A 632 -150.95 -137.30
REMARK 500 GLU A 634 20.21 -79.68
REMARK 500 SER A 638 19.21 -150.83
REMARK 500 PRO B 116 38.70 -78.81
REMARK 500
REMARK 500 THIS ENTRY HAS 103 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH G 864 DISTANCE = 6.63 ANGSTROMS
DBREF1 7EP9 G 1 660 UNP A0A1S1MBE1_FUSNU
DBREF2 7EP9 G A0A1S1MBE1 1 660
DBREF1 7EP9 A 1 660 UNP A0A1S1MBE1_FUSNU
DBREF2 7EP9 A A0A1S1MBE1 1 660
DBREF1 7EP9 B 1 660 UNP A0A1S1MBE1_FUSNU
DBREF2 7EP9 B A0A1S1MBE1 1 660
DBREF1 7EP9 C 1 660 UNP A0A1S1MBE1_FUSNU
DBREF2 7EP9 C A0A1S1MBE1 1 660
SEQRES 1 G 660 MET GLU ASN LEU LYS LEU ASP SER PHE LEU GLU TYR LYS
SEQRES 2 G 660 PHE LEU SER ASN LEU ASP PHE ASN PRO ASP GLY SER ASN
SEQRES 3 G 660 LEU ALA PHE SER LEU SER GLU ALA ASP LEU GLU ASN ASN
SEQRES 4 G 660 SER TYR LYS HIS PHE ILE TYR ASN LEU ASP THR LYS ASN
SEQRES 5 G 660 LYS GLU ILE LYS LYS LEU THR HIS SER GLY LYS GLU LYS
SEQRES 6 G 660 ASN SER LEU TRP LEU ASN ASN ASN THR ILE LEU PHE SER
SEQRES 7 G 660 ALA ASP ARG ASP LYS ASP ILE GLU GLU LYS LYS LYS LEU
SEQRES 8 G 660 GLY GLU THR TRP THR ILE PHE TYR ALA LEU ASP ILE LYS
SEQRES 9 G 660 ASN GLY GLY GLU ALA TYR GLU TYR MET LYS LEU PRO VAL
SEQRES 10 G 660 ASN VAL THR GLU ILE LYS ILE ILE ASP GLU ASN ASN PHE
SEQRES 11 G 660 ILE LEU THR ALA ASP PHE ASP ASN ASN SER LEU ASN LEU
SEQRES 12 G 660 ASN ASP LEU LYS GLY GLY GLU ARG GLU LYS ALA ILE LYS
SEQRES 13 G 660 GLN ILE GLU GLU ASN LYS ASP TYR GLU VAL LEU ASP GLU
SEQRES 14 G 660 ILE PRO PHE TRP SER ASN GLY ASN GLY PHE ARG ASN LYS
SEQRES 15 G 660 LYS ARG ASN ARG LEU TYR HIS PHE ASP LYS SER ASN ASN
SEQRES 16 G 660 LYS LEU THR PRO ILE SER ASP GLU TYR THR ASN VAL GLU
SEQRES 17 G 660 SER PHE ASN ILE LYS GLU ASN LYS VAL ILE PHE VAL GLY
SEQRES 18 G 660 ARG THR TYR LYS ASP LYS GLN ALA LEU THR ALA GLY LEU
SEQRES 19 G 660 TYR THR TYR ASP VAL LYS SER ASN LYS LEU GLU ILE ILE
SEQRES 20 G 660 ILE SER ASP ASN LEU TYR ASP ILE SER TYR ALA ASN PHE
SEQRES 21 G 660 ILE GLU ASP LYS ILE ILE CYS ALA LEU SER ASP MET LYS
SEQRES 22 G 660 GLU TYR GLY ILE ASN GLU ASN HIS LYS ILE TYR LEU ILE
SEQRES 23 G 660 ASP SER ASN LYS ASN ILE ASN LEU LEU TYR GLU ASN ASP
SEQRES 24 G 660 THR TRP LEU ALA CYS THR VAL GLY SER ASP CYS ARG LEU
SEQRES 25 G 660 GLY GLY GLY LYS SER PHE LYS VAL ILE GLY ASN LYS LEU
SEQRES 26 G 660 TYR PHE LEU SER THR ILE ALA ASP SER VAL HIS LEU SER
SEQRES 27 G 660 SER LEU ASP THR ASN GLY LYS VAL GLU ILE LEU SER SER
SEQRES 28 G 660 GLU ASN GLY SER ILE ASP PHE PHE ASP ILE ALA ASN ASN
SEQRES 29 G 660 GLU ILE TYR TYR VAL GLY MET ARG ASP TYR THR LEU GLN
SEQRES 30 G 660 GLU ILE TYR LYS LEU GLU ASN ASN SER SER ILE LYS LEU
SEQRES 31 G 660 SER SER PHE ASN GLU GLU ILE ASN LYS LYS TYR LYS ILE
SEQRES 32 G 660 SER LYS PRO GLU VAL PHE ASP PHE ILE THR ASN GLY ASP
SEQRES 33 G 660 THR THR LYS GLY PHE VAL ILE TYR PRO ILE ASP TYR ASP
SEQRES 34 G 660 LYS ASN LYS THR TYR PRO ALA ILE LEU ASP ILE HIS GLY
SEQRES 35 G 660 GLY PRO LYS THR VAL TYR GLY ASP VAL TYR TYR HIS GLU
SEQRES 36 G 660 MET GLN VAL TRP ALA ASN MET GLY TYR PHE VAL ILE PHE
SEQRES 37 G 660 THR ASN PRO HIS GLY SER ASP GLY TYR GLY ASN LYS PHE
SEQRES 38 G 660 ALA ASP ILE ARG GLY LYS TYR GLY THR ILE ASP TYR GLU
SEQRES 39 G 660 ASP LEU MET ASN PHE THR ASP TYR VAL LEU GLU LYS TYR
SEQRES 40 G 660 PRO ILE ASP LYS SER ARG VAL GLY VAL THR GLY GLY SER
SEQRES 41 G 660 TYR GLY GLY TYR MET THR ASN TRP ILE ILE GLY HIS THR
SEQRES 42 G 660 ASP ARG PHE LYS CYS ALA ALA SER GLN ARG SER ILE SER
SEQRES 43 G 660 ASN TRP ILE SER LYS PHE GLY THR THR ASP ILE GLY TYR
SEQRES 44 G 660 TYR PHE ASN ALA ASP GLN ASN GLN ALA THR PRO TRP ILE
SEQRES 45 G 660 ASN HIS ASP LYS LEU TRP TRP HIS SER PRO LEU LYS TYR
SEQRES 46 G 660 ALA ASP LYS ALA LYS THR PRO THR LEU PHE ILE HIS SER
SEQRES 47 G 660 GLU GLU ASP TYR ARG CYS TRP LEU ALA GLU GLY LEU GLN
SEQRES 48 G 660 MET PHE THR ALA LEU LYS TYR HIS GLY ILE GLU ALA ARG
SEQRES 49 G 660 LEU CYS MET PHE ARG GLY GLU ASN HIS GLU LEU SER ARG
SEQRES 50 G 660 SER GLY LYS PRO LYS HIS ARG ILE ARG ARG LEU THR GLU
SEQRES 51 G 660 ILE THR ASN TRP PHE GLU LYS TYR LEU LYS
SEQRES 1 A 660 MET GLU ASN LEU LYS LEU ASP SER PHE LEU GLU TYR LYS
SEQRES 2 A 660 PHE LEU SER ASN LEU ASP PHE ASN PRO ASP GLY SER ASN
SEQRES 3 A 660 LEU ALA PHE SER LEU SER GLU ALA ASP LEU GLU ASN ASN
SEQRES 4 A 660 SER TYR LYS HIS PHE ILE TYR ASN LEU ASP THR LYS ASN
SEQRES 5 A 660 LYS GLU ILE LYS LYS LEU THR HIS SER GLY LYS GLU LYS
SEQRES 6 A 660 ASN SER LEU TRP LEU ASN ASN ASN THR ILE LEU PHE SER
SEQRES 7 A 660 ALA ASP ARG ASP LYS ASP ILE GLU GLU LYS LYS LYS LEU
SEQRES 8 A 660 GLY GLU THR TRP THR ILE PHE TYR ALA LEU ASP ILE LYS
SEQRES 9 A 660 ASN GLY GLY GLU ALA TYR GLU TYR MET LYS LEU PRO VAL
SEQRES 10 A 660 ASN VAL THR GLU ILE LYS ILE ILE ASP GLU ASN ASN PHE
SEQRES 11 A 660 ILE LEU THR ALA ASP PHE ASP ASN ASN SER LEU ASN LEU
SEQRES 12 A 660 ASN ASP LEU LYS GLY GLY GLU ARG GLU LYS ALA ILE LYS
SEQRES 13 A 660 GLN ILE GLU GLU ASN LYS ASP TYR GLU VAL LEU ASP GLU
SEQRES 14 A 660 ILE PRO PHE TRP SER ASN GLY ASN GLY PHE ARG ASN LYS
SEQRES 15 A 660 LYS ARG ASN ARG LEU TYR HIS PHE ASP LYS SER ASN ASN
SEQRES 16 A 660 LYS LEU THR PRO ILE SER ASP GLU TYR THR ASN VAL GLU
SEQRES 17 A 660 SER PHE ASN ILE LYS GLU ASN LYS VAL ILE PHE VAL GLY
SEQRES 18 A 660 ARG THR TYR LYS ASP LYS GLN ALA LEU THR ALA GLY LEU
SEQRES 19 A 660 TYR THR TYR ASP VAL LYS SER ASN LYS LEU GLU ILE ILE
SEQRES 20 A 660 ILE SER ASP ASN LEU TYR ASP ILE SER TYR ALA ASN PHE
SEQRES 21 A 660 ILE GLU ASP LYS ILE ILE CYS ALA LEU SER ASP MET LYS
SEQRES 22 A 660 GLU TYR GLY ILE ASN GLU ASN HIS LYS ILE TYR LEU ILE
SEQRES 23 A 660 ASP SER ASN LYS ASN ILE ASN LEU LEU TYR GLU ASN ASP
SEQRES 24 A 660 THR TRP LEU ALA CYS THR VAL GLY SER ASP CYS ARG LEU
SEQRES 25 A 660 GLY GLY GLY LYS SER PHE LYS VAL ILE GLY ASN LYS LEU
SEQRES 26 A 660 TYR PHE LEU SER THR ILE ALA ASP SER VAL HIS LEU SER
SEQRES 27 A 660 SER LEU ASP THR ASN GLY LYS VAL GLU ILE LEU SER SER
SEQRES 28 A 660 GLU ASN GLY SER ILE ASP PHE PHE ASP ILE ALA ASN ASN
SEQRES 29 A 660 GLU ILE TYR TYR VAL GLY MET ARG ASP TYR THR LEU GLN
SEQRES 30 A 660 GLU ILE TYR LYS LEU GLU ASN ASN SER SER ILE LYS LEU
SEQRES 31 A 660 SER SER PHE ASN GLU GLU ILE ASN LYS LYS TYR LYS ILE
SEQRES 32 A 660 SER LYS PRO GLU VAL PHE ASP PHE ILE THR ASN GLY ASP
SEQRES 33 A 660 THR THR LYS GLY PHE VAL ILE TYR PRO ILE ASP TYR ASP
SEQRES 34 A 660 LYS ASN LYS THR TYR PRO ALA ILE LEU ASP ILE HIS GLY
SEQRES 35 A 660 GLY PRO LYS THR VAL TYR GLY ASP VAL TYR TYR HIS GLU
SEQRES 36 A 660 MET GLN VAL TRP ALA ASN MET GLY TYR PHE VAL ILE PHE
SEQRES 37 A 660 THR ASN PRO HIS GLY SER ASP GLY TYR GLY ASN LYS PHE
SEQRES 38 A 660 ALA ASP ILE ARG GLY LYS TYR GLY THR ILE ASP TYR GLU
SEQRES 39 A 660 ASP LEU MET ASN PHE THR ASP TYR VAL LEU GLU LYS TYR
SEQRES 40 A 660 PRO ILE ASP LYS SER ARG VAL GLY VAL THR GLY GLY SER
SEQRES 41 A 660 TYR GLY GLY TYR MET THR ASN TRP ILE ILE GLY HIS THR
SEQRES 42 A 660 ASP ARG PHE LYS CYS ALA ALA SER GLN ARG SER ILE SER
SEQRES 43 A 660 ASN TRP ILE SER LYS PHE GLY THR THR ASP ILE GLY TYR
SEQRES 44 A 660 TYR PHE ASN ALA ASP GLN ASN GLN ALA THR PRO TRP ILE
SEQRES 45 A 660 ASN HIS ASP LYS LEU TRP TRP HIS SER PRO LEU LYS TYR
SEQRES 46 A 660 ALA ASP LYS ALA LYS THR PRO THR LEU PHE ILE HIS SER
SEQRES 47 A 660 GLU GLU ASP TYR ARG CYS TRP LEU ALA GLU GLY LEU GLN
SEQRES 48 A 660 MET PHE THR ALA LEU LYS TYR HIS GLY ILE GLU ALA ARG
SEQRES 49 A 660 LEU CYS MET PHE ARG GLY GLU ASN HIS GLU LEU SER ARG
SEQRES 50 A 660 SER GLY LYS PRO LYS HIS ARG ILE ARG ARG LEU THR GLU
SEQRES 51 A 660 ILE THR ASN TRP PHE GLU LYS TYR LEU LYS
SEQRES 1 B 660 MET GLU ASN LEU LYS LEU ASP SER PHE LEU GLU TYR LYS
SEQRES 2 B 660 PHE LEU SER ASN LEU ASP PHE ASN PRO ASP GLY SER ASN
SEQRES 3 B 660 LEU ALA PHE SER LEU SER GLU ALA ASP LEU GLU ASN ASN
SEQRES 4 B 660 SER TYR LYS HIS PHE ILE TYR ASN LEU ASP THR LYS ASN
SEQRES 5 B 660 LYS GLU ILE LYS LYS LEU THR HIS SER GLY LYS GLU LYS
SEQRES 6 B 660 ASN SER LEU TRP LEU ASN ASN ASN THR ILE LEU PHE SER
SEQRES 7 B 660 ALA ASP ARG ASP LYS ASP ILE GLU GLU LYS LYS LYS LEU
SEQRES 8 B 660 GLY GLU THR TRP THR ILE PHE TYR ALA LEU ASP ILE LYS
SEQRES 9 B 660 ASN GLY GLY GLU ALA TYR GLU TYR MET LYS LEU PRO VAL
SEQRES 10 B 660 ASN VAL THR GLU ILE LYS ILE ILE ASP GLU ASN ASN PHE
SEQRES 11 B 660 ILE LEU THR ALA ASP PHE ASP ASN ASN SER LEU ASN LEU
SEQRES 12 B 660 ASN ASP LEU LYS GLY GLY GLU ARG GLU LYS ALA ILE LYS
SEQRES 13 B 660 GLN ILE GLU GLU ASN LYS ASP TYR GLU VAL LEU ASP GLU
SEQRES 14 B 660 ILE PRO PHE TRP SER ASN GLY ASN GLY PHE ARG ASN LYS
SEQRES 15 B 660 LYS ARG ASN ARG LEU TYR HIS PHE ASP LYS SER ASN ASN
SEQRES 16 B 660 LYS LEU THR PRO ILE SER ASP GLU TYR THR ASN VAL GLU
SEQRES 17 B 660 SER PHE ASN ILE LYS GLU ASN LYS VAL ILE PHE VAL GLY
SEQRES 18 B 660 ARG THR TYR LYS ASP LYS GLN ALA LEU THR ALA GLY LEU
SEQRES 19 B 660 TYR THR TYR ASP VAL LYS SER ASN LYS LEU GLU ILE ILE
SEQRES 20 B 660 ILE SER ASP ASN LEU TYR ASP ILE SER TYR ALA ASN PHE
SEQRES 21 B 660 ILE GLU ASP LYS ILE ILE CYS ALA LEU SER ASP MET LYS
SEQRES 22 B 660 GLU TYR GLY ILE ASN GLU ASN HIS LYS ILE TYR LEU ILE
SEQRES 23 B 660 ASP SER ASN LYS ASN ILE ASN LEU LEU TYR GLU ASN ASP
SEQRES 24 B 660 THR TRP LEU ALA CYS THR VAL GLY SER ASP CYS ARG LEU
SEQRES 25 B 660 GLY GLY GLY LYS SER PHE LYS VAL ILE GLY ASN LYS LEU
SEQRES 26 B 660 TYR PHE LEU SER THR ILE ALA ASP SER VAL HIS LEU SER
SEQRES 27 B 660 SER LEU ASP THR ASN GLY LYS VAL GLU ILE LEU SER SER
SEQRES 28 B 660 GLU ASN GLY SER ILE ASP PHE PHE ASP ILE ALA ASN ASN
SEQRES 29 B 660 GLU ILE TYR TYR VAL GLY MET ARG ASP TYR THR LEU GLN
SEQRES 30 B 660 GLU ILE TYR LYS LEU GLU ASN ASN SER SER ILE LYS LEU
SEQRES 31 B 660 SER SER PHE ASN GLU GLU ILE ASN LYS LYS TYR LYS ILE
SEQRES 32 B 660 SER LYS PRO GLU VAL PHE ASP PHE ILE THR ASN GLY ASP
SEQRES 33 B 660 THR THR LYS GLY PHE VAL ILE TYR PRO ILE ASP TYR ASP
SEQRES 34 B 660 LYS ASN LYS THR TYR PRO ALA ILE LEU ASP ILE HIS GLY
SEQRES 35 B 660 GLY PRO LYS THR VAL TYR GLY ASP VAL TYR TYR HIS GLU
SEQRES 36 B 660 MET GLN VAL TRP ALA ASN MET GLY TYR PHE VAL ILE PHE
SEQRES 37 B 660 THR ASN PRO HIS GLY SER ASP GLY TYR GLY ASN LYS PHE
SEQRES 38 B 660 ALA ASP ILE ARG GLY LYS TYR GLY THR ILE ASP TYR GLU
SEQRES 39 B 660 ASP LEU MET ASN PHE THR ASP TYR VAL LEU GLU LYS TYR
SEQRES 40 B 660 PRO ILE ASP LYS SER ARG VAL GLY VAL THR GLY GLY SER
SEQRES 41 B 660 TYR GLY GLY TYR MET THR ASN TRP ILE ILE GLY HIS THR
SEQRES 42 B 660 ASP ARG PHE LYS CYS ALA ALA SER GLN ARG SER ILE SER
SEQRES 43 B 660 ASN TRP ILE SER LYS PHE GLY THR THR ASP ILE GLY TYR
SEQRES 44 B 660 TYR PHE ASN ALA ASP GLN ASN GLN ALA THR PRO TRP ILE
SEQRES 45 B 660 ASN HIS ASP LYS LEU TRP TRP HIS SER PRO LEU LYS TYR
SEQRES 46 B 660 ALA ASP LYS ALA LYS THR PRO THR LEU PHE ILE HIS SER
SEQRES 47 B 660 GLU GLU ASP TYR ARG CYS TRP LEU ALA GLU GLY LEU GLN
SEQRES 48 B 660 MET PHE THR ALA LEU LYS TYR HIS GLY ILE GLU ALA ARG
SEQRES 49 B 660 LEU CYS MET PHE ARG GLY GLU ASN HIS GLU LEU SER ARG
SEQRES 50 B 660 SER GLY LYS PRO LYS HIS ARG ILE ARG ARG LEU THR GLU
SEQRES 51 B 660 ILE THR ASN TRP PHE GLU LYS TYR LEU LYS
SEQRES 1 C 660 MET GLU ASN LEU LYS LEU ASP SER PHE LEU GLU TYR LYS
SEQRES 2 C 660 PHE LEU SER ASN LEU ASP PHE ASN PRO ASP GLY SER ASN
SEQRES 3 C 660 LEU ALA PHE SER LEU SER GLU ALA ASP LEU GLU ASN ASN
SEQRES 4 C 660 SER TYR LYS HIS PHE ILE TYR ASN LEU ASP THR LYS ASN
SEQRES 5 C 660 LYS GLU ILE LYS LYS LEU THR HIS SER GLY LYS GLU LYS
SEQRES 6 C 660 ASN SER LEU TRP LEU ASN ASN ASN THR ILE LEU PHE SER
SEQRES 7 C 660 ALA ASP ARG ASP LYS ASP ILE GLU GLU LYS LYS LYS LEU
SEQRES 8 C 660 GLY GLU THR TRP THR ILE PHE TYR ALA LEU ASP ILE LYS
SEQRES 9 C 660 ASN GLY GLY GLU ALA TYR GLU TYR MET LYS LEU PRO VAL
SEQRES 10 C 660 ASN VAL THR GLU ILE LYS ILE ILE ASP GLU ASN ASN PHE
SEQRES 11 C 660 ILE LEU THR ALA ASP PHE ASP ASN ASN SER LEU ASN LEU
SEQRES 12 C 660 ASN ASP LEU LYS GLY GLY GLU ARG GLU LYS ALA ILE LYS
SEQRES 13 C 660 GLN ILE GLU GLU ASN LYS ASP TYR GLU VAL LEU ASP GLU
SEQRES 14 C 660 ILE PRO PHE TRP SER ASN GLY ASN GLY PHE ARG ASN LYS
SEQRES 15 C 660 LYS ARG ASN ARG LEU TYR HIS PHE ASP LYS SER ASN ASN
SEQRES 16 C 660 LYS LEU THR PRO ILE SER ASP GLU TYR THR ASN VAL GLU
SEQRES 17 C 660 SER PHE ASN ILE LYS GLU ASN LYS VAL ILE PHE VAL GLY
SEQRES 18 C 660 ARG THR TYR LYS ASP LYS GLN ALA LEU THR ALA GLY LEU
SEQRES 19 C 660 TYR THR TYR ASP VAL LYS SER ASN LYS LEU GLU ILE ILE
SEQRES 20 C 660 ILE SER ASP ASN LEU TYR ASP ILE SER TYR ALA ASN PHE
SEQRES 21 C 660 ILE GLU ASP LYS ILE ILE CYS ALA LEU SER ASP MET LYS
SEQRES 22 C 660 GLU TYR GLY ILE ASN GLU ASN HIS LYS ILE TYR LEU ILE
SEQRES 23 C 660 ASP SER ASN LYS ASN ILE ASN LEU LEU TYR GLU ASN ASP
SEQRES 24 C 660 THR TRP LEU ALA CYS THR VAL GLY SER ASP CYS ARG LEU
SEQRES 25 C 660 GLY GLY GLY LYS SER PHE LYS VAL ILE GLY ASN LYS LEU
SEQRES 26 C 660 TYR PHE LEU SER THR ILE ALA ASP SER VAL HIS LEU SER
SEQRES 27 C 660 SER LEU ASP THR ASN GLY LYS VAL GLU ILE LEU SER SER
SEQRES 28 C 660 GLU ASN GLY SER ILE ASP PHE PHE ASP ILE ALA ASN ASN
SEQRES 29 C 660 GLU ILE TYR TYR VAL GLY MET ARG ASP TYR THR LEU GLN
SEQRES 30 C 660 GLU ILE TYR LYS LEU GLU ASN ASN SER SER ILE LYS LEU
SEQRES 31 C 660 SER SER PHE ASN GLU GLU ILE ASN LYS LYS TYR LYS ILE
SEQRES 32 C 660 SER LYS PRO GLU VAL PHE ASP PHE ILE THR ASN GLY ASP
SEQRES 33 C 660 THR THR LYS GLY PHE VAL ILE TYR PRO ILE ASP TYR ASP
SEQRES 34 C 660 LYS ASN LYS THR TYR PRO ALA ILE LEU ASP ILE HIS GLY
SEQRES 35 C 660 GLY PRO LYS THR VAL TYR GLY ASP VAL TYR TYR HIS GLU
SEQRES 36 C 660 MET GLN VAL TRP ALA ASN MET GLY TYR PHE VAL ILE PHE
SEQRES 37 C 660 THR ASN PRO HIS GLY SER ASP GLY TYR GLY ASN LYS PHE
SEQRES 38 C 660 ALA ASP ILE ARG GLY LYS TYR GLY THR ILE ASP TYR GLU
SEQRES 39 C 660 ASP LEU MET ASN PHE THR ASP TYR VAL LEU GLU LYS TYR
SEQRES 40 C 660 PRO ILE ASP LYS SER ARG VAL GLY VAL THR GLY GLY SER
SEQRES 41 C 660 TYR GLY GLY TYR MET THR ASN TRP ILE ILE GLY HIS THR
SEQRES 42 C 660 ASP ARG PHE LYS CYS ALA ALA SER GLN ARG SER ILE SER
SEQRES 43 C 660 ASN TRP ILE SER LYS PHE GLY THR THR ASP ILE GLY TYR
SEQRES 44 C 660 TYR PHE ASN ALA ASP GLN ASN GLN ALA THR PRO TRP ILE
SEQRES 45 C 660 ASN HIS ASP LYS LEU TRP TRP HIS SER PRO LEU LYS TYR
SEQRES 46 C 660 ALA ASP LYS ALA LYS THR PRO THR LEU PHE ILE HIS SER
SEQRES 47 C 660 GLU GLU ASP TYR ARG CYS TRP LEU ALA GLU GLY LEU GLN
SEQRES 48 C 660 MET PHE THR ALA LEU LYS TYR HIS GLY ILE GLU ALA ARG
SEQRES 49 C 660 LEU CYS MET PHE ARG GLY GLU ASN HIS GLU LEU SER ARG
SEQRES 50 C 660 SER GLY LYS PRO LYS HIS ARG ILE ARG ARG LEU THR GLU
SEQRES 51 C 660 ILE THR ASN TRP PHE GLU LYS TYR LEU LYS
FORMUL 5 HOH *490(H2 O)
HELIX 1 AA1 LYS G 5 TYR G 12 5 8
HELIX 2 AA2 ASP G 82 GLY G 92 1 11
HELIX 3 AA3 ASN G 142 LEU G 146 5 5
HELIX 4 AA4 GLY G 148 LYS G 162 1 15
HELIX 5 AA5 ASN G 394 TYR G 401 1 8
HELIX 6 AA6 TYR G 453 ASN G 461 1 9
HELIX 7 AA7 TYR G 477 ALA G 482 1 6
HELIX 8 AA8 THR G 490 TYR G 507 1 18
HELIX 9 AA9 SER G 520 THR G 533 1 14
HELIX 10 AB1 ASN G 547 THR G 554 1 8
HELIX 11 AB2 ILE G 557 GLN G 567 1 11
HELIX 12 AB3 ASN G 573 HIS G 580 1 8
HELIX 13 AB4 SER G 581 ALA G 589 5 9
HELIX 14 AB5 TRP G 605 HIS G 619 1 15
HELIX 15 AB6 GLU G 634 GLY G 639 1 6
HELIX 16 AB7 LYS G 640 LYS G 660 1 21
HELIX 17 AB8 ASP A 7 TYR A 12 5 6
HELIX 18 AB9 ASP A 82 GLY A 92 1 11
HELIX 19 AC1 LYS A 147 ASN A 161 1 15
HELIX 20 AC2 ASN A 394 TYR A 401 1 8
HELIX 21 AC3 TYR A 453 ASN A 461 1 9
HELIX 22 AC4 TYR A 477 ASP A 483 1 7
HELIX 23 AC5 THR A 490 TYR A 507 1 18
HELIX 24 AC6 SER A 520 GLY A 531 1 12
HELIX 25 AC7 ASN A 547 GLY A 553 1 7
HELIX 26 AC8 ILE A 557 GLN A 567 1 11
HELIX 27 AC9 ASN A 573 HIS A 580 1 8
HELIX 28 AD1 SER A 581 ALA A 589 5 9
HELIX 29 AD2 TRP A 605 HIS A 619 1 15
HELIX 30 AD3 GLU A 634 GLY A 639 1 6
HELIX 31 AD4 LYS A 640 LYS A 660 1 21
HELIX 32 AD5 LYS B 5 TYR B 12 5 8
HELIX 33 AD6 ASP B 82 GLY B 92 1 11
HELIX 34 AD7 ASN B 142 LEU B 146 5 5
HELIX 35 AD8 GLU B 150 LYS B 162 1 13
HELIX 36 AD9 GLU B 396 TYR B 401 1 6
HELIX 37 AE1 TYR B 453 ASN B 461 1 9
HELIX 38 AE2 GLY B 478 ASP B 483 1 6
HELIX 39 AE3 THR B 490 TYR B 507 1 18
HELIX 40 AE4 SER B 520 GLY B 531 1 12
HELIX 41 AE5 ASN B 547 GLY B 553 1 7
HELIX 42 AE6 ILE B 557 GLN B 567 1 11
HELIX 43 AE7 ASN B 573 HIS B 580 1 8
HELIX 44 AE8 SER B 581 ALA B 586 5 6
HELIX 45 AE9 LEU B 606 HIS B 619 1 14
HELIX 46 AF1 GLU B 634 GLY B 639 1 6
HELIX 47 AF2 LYS B 640 LYS B 660 1 21
HELIX 48 AF3 ASP C 7 TYR C 12 5 6
HELIX 49 AF4 ASP C 82 LEU C 91 1 10
HELIX 50 AF5 ASN C 142 LEU C 146 5 5
HELIX 51 AF6 GLY C 148 LYS C 162 1 15
HELIX 52 AF7 ASN C 394 TYR C 401 1 8
HELIX 53 AF8 TYR C 453 ASN C 461 1 9
HELIX 54 AF9 TYR C 477 ASP C 483 1 7
HELIX 55 AG1 THR C 490 TYR C 507 1 18
HELIX 56 AG2 GLY C 519 GLY C 531 1 13
HELIX 57 AG3 ASN C 547 GLY C 553 1 7
HELIX 58 AG4 ILE C 557 GLN C 567 1 11
HELIX 59 AG5 ASN C 573 HIS C 580 1 8
HELIX 60 AG6 SER C 581 ALA C 586 5 6
HELIX 61 AG7 TRP C 605 HIS C 619 1 15
HELIX 62 AG8 GLU C 634 GLY C 639 1 6
HELIX 63 AG9 LYS C 640 LYS C 660 1 21
SHEET 1 AA1 4 PHE G 14 PHE G 20 0
SHEET 2 AA1 4 ASN G 26 ASP G 35 -1 O SER G 30 N SER G 16
SHEET 3 AA1 4 SER G 40 ASP G 49 -1 O TYR G 46 N PHE G 29
SHEET 4 AA1 4 GLU G 54 LYS G 57 -1 O LYS G 56 N ASN G 47
SHEET 1 AA2 4 LYS G 65 ASN G 71 0
SHEET 2 AA2 4 THR G 74 ALA G 79 -1 O LEU G 76 N LEU G 68
SHEET 3 AA2 4 THR G 96 ASP G 102 -1 O TYR G 99 N PHE G 77
SHEET 4 AA2 4 TYR G 110 LEU G 115 -1 O TYR G 110 N ALA G 100
SHEET 1 AA3 4 VAL G 119 ASP G 126 0
SHEET 2 AA3 4 ASN G 129 ASP G 137 -1 O ASN G 129 N ILE G 125
SHEET 3 AA3 4 LYS G 183 ASP G 191 -1 O TYR G 188 N LEU G 132
SHEET 4 AA3 4 LYS G 196 PRO G 199 -1 O THR G 198 N HIS G 189
SHEET 1 AA4 9 TYR G 164 LEU G 167 0
SHEET 2 AA4 9 ALA A 623 PHE A 628 -1 O MET A 627 N GLU G 165
SHEET 3 AA4 9 THR A 593 SER A 598 1 N PHE A 595 O ARG A 624
SHEET 4 AA4 9 CYS A 538 GLN A 542 1 N SER A 541 O LEU A 594
SHEET 5 AA4 9 ILE A 509 GLY A 519 1 N VAL A 516 O ALA A 540
SHEET 6 AA4 9 TYR A 434 ILE A 440 1 N TYR A 434 O ASP A 510
SHEET 7 AA4 9 PHE A 465 THR A 469 1 O PHE A 465 N PRO A 435
SHEET 8 AA4 9 ASP A 416 ILE A 423 -1 N PHE A 421 O PHE A 468
SHEET 9 AA4 9 GLU A 407 THR A 413 -1 N PHE A 411 O THR A 418
SHEET 1 AA5 2 TRP G 173 SER G 174 0
SHEET 2 AA5 2 GLY G 178 PHE G 179 -1 O GLY G 178 N SER G 174
SHEET 1 AA6 4 THR G 205 LYS G 213 0
SHEET 2 AA6 4 LYS G 216 THR G 223 -1 O ARG G 222 N ASN G 206
SHEET 3 AA6 4 ALA G 232 ASP G 238 -1 O GLY G 233 N GLY G 221
SHEET 4 AA6 4 LYS G 243 TYR G 253 -1 O TYR G 253 N ALA G 232
SHEET 1 AA7 4 TYR G 257 ILE G 261 0
SHEET 2 AA7 4 LYS G 264 LEU G 269 -1 O LYS G 264 N ILE G 261
SHEET 3 AA7 4 LYS G 282 ILE G 286 -1 O TYR G 284 N CYS G 267
SHEET 4 AA7 4 ILE G 292 TYR G 296 -1 O ASN G 293 N LEU G 285
SHEET 1 AA8 4 PHE G 318 ILE G 321 0
SHEET 2 AA8 4 LYS G 324 THR G 330 -1 O TYR G 326 N LYS G 319
SHEET 3 AA8 4 VAL G 335 LEU G 340 -1 O HIS G 336 N SER G 329
SHEET 4 AA8 4 VAL G 346 SER G 350 -1 O LEU G 349 N LEU G 337
SHEET 1 AA9 4 SER G 355 ILE G 361 0
SHEET 2 AA9 4 ILE G 366 MET G 371 -1 O VAL G 369 N PHE G 358
SHEET 3 AA9 4 GLU G 378 LEU G 382 -1 O TYR G 380 N TYR G 368
SHEET 4 AA9 4 SER G 387 LYS G 389 -1 O ILE G 388 N LYS G 381
SHEET 1 AB1 9 GLU G 407 THR G 413 0
SHEET 2 AB1 9 ASP G 416 ILE G 423 -1 O ASP G 416 N THR G 413
SHEET 3 AB1 9 PHE G 465 THR G 469 -1 O VAL G 466 N ILE G 423
SHEET 4 AB1 9 TYR G 434 ILE G 440 1 N PRO G 435 O PHE G 465
SHEET 5 AB1 9 ILE G 509 GLY G 519 1 O GLY G 515 N ALA G 436
SHEET 6 AB1 9 CYS G 538 GLN G 542 1 O GLN G 542 N GLY G 518
SHEET 7 AB1 9 THR G 593 SER G 598 1 O LEU G 594 N SER G 541
SHEET 8 AB1 9 ALA G 623 PHE G 628 1 O ARG G 624 N PHE G 595
SHEET 9 AB1 9 TYR A 164 LEU A 167 -1 O GLU A 165 N MET G 627
SHEET 1 AB2 4 PHE A 14 PHE A 20 0
SHEET 2 AB2 4 ASN A 26 ASP A 35 -1 O SER A 30 N SER A 16
SHEET 3 AB2 4 SER A 40 ASP A 49 -1 O TYR A 46 N PHE A 29
SHEET 4 AB2 4 ILE A 55 LYS A 57 -1 O LYS A 56 N ASN A 47
SHEET 1 AB3 4 ASN A 66 ASN A 71 0
SHEET 2 AB3 4 THR A 74 ALA A 79 -1 O LEU A 76 N LEU A 68
SHEET 3 AB3 4 THR A 96 ASP A 102 -1 O TYR A 99 N PHE A 77
SHEET 4 AB3 4 TYR A 110 LEU A 115 -1 O TYR A 112 N PHE A 98
SHEET 1 AB4 4 VAL A 119 ASP A 126 0
SHEET 2 AB4 4 ASN A 129 ASP A 137 -1 O THR A 133 N THR A 120
SHEET 3 AB4 4 LYS A 183 ASP A 191 -1 O TYR A 188 N LEU A 132
SHEET 4 AB4 4 LYS A 196 PRO A 199 -1 O THR A 198 N HIS A 189
SHEET 1 AB5 2 TRP A 173 SER A 174 0
SHEET 2 AB5 2 GLY A 178 PHE A 179 -1 O GLY A 178 N SER A 174
SHEET 1 AB6 4 THR A 205 ILE A 212 0
SHEET 2 AB6 4 LYS A 216 THR A 223 -1 O ARG A 222 N ASN A 206
SHEET 3 AB6 4 GLY A 233 ASP A 238 -1 O TYR A 237 N VAL A 217
SHEET 4 AB6 4 LEU A 244 ILE A 248 -1 O ILE A 247 N LEU A 234
SHEET 1 AB7 4 TYR A 257 ILE A 261 0
SHEET 2 AB7 4 LYS A 264 LEU A 269 -1 O LYS A 264 N ILE A 261
SHEET 3 AB7 4 LYS A 282 ILE A 286 -1 O ILE A 286 N ILE A 265
SHEET 4 AB7 4 ILE A 292 TYR A 296 -1 O ASN A 293 N LEU A 285
SHEET 1 AB8 4 LYS A 319 ILE A 321 0
SHEET 2 AB8 4 LYS A 324 THR A 330 -1 O TYR A 326 N LYS A 319
SHEET 3 AB8 4 VAL A 335 SER A 338 -1 O HIS A 336 N SER A 329
SHEET 4 AB8 4 ILE A 348 SER A 350 -1 O LEU A 349 N LEU A 337
SHEET 1 AB9 4 SER A 355 ILE A 361 0
SHEET 2 AB9 4 ILE A 366 MET A 371 -1 O VAL A 369 N PHE A 358
SHEET 3 AB9 4 GLU A 378 GLU A 383 -1 O LEU A 382 N ILE A 366
SHEET 4 AB9 4 SER A 386 LYS A 389 -1 O SER A 386 N GLU A 383
SHEET 1 AC1 4 PHE B 14 PHE B 20 0
SHEET 2 AC1 4 ASN B 26 ASP B 35 -1 O ALA B 28 N ASP B 19
SHEET 3 AC1 4 SER B 40 ASP B 49 -1 O TYR B 46 N PHE B 29
SHEET 4 AC1 4 ILE B 55 LYS B 57 -1 O LYS B 56 N ASN B 47
SHEET 1 AC2 4 LYS B 65 TRP B 69 0
SHEET 2 AC2 4 THR B 74 ALA B 79 -1 O LEU B 76 N SER B 67
SHEET 3 AC2 4 THR B 96 ASP B 102 -1 O TYR B 99 N PHE B 77
SHEET 4 AC2 4 TYR B 110 LEU B 115 -1 O TYR B 110 N ALA B 100
SHEET 1 AC3 4 ASN B 118 ASP B 126 0
SHEET 2 AC3 4 ASN B 129 ASP B 137 -1 O ASP B 135 N ASN B 118
SHEET 3 AC3 4 LYS B 183 ASP B 191 -1 O TYR B 188 N LEU B 132
SHEET 4 AC3 4 LYS B 196 PRO B 199 -1 O THR B 198 N HIS B 189
SHEET 1 AC4 9 TYR B 164 LEU B 167 0
SHEET 2 AC4 9 ALA C 623 PHE C 628 -1 O MET C 627 N GLU B 165
SHEET 3 AC4 9 THR C 593 SER C 598 1 N PHE C 595 O ARG C 624
SHEET 4 AC4 9 CYS C 538 GLN C 542 1 N SER C 541 O ILE C 596
SHEET 5 AC4 9 ILE C 509 GLY C 518 1 N VAL C 516 O ALA C 540
SHEET 6 AC4 9 TYR C 434 ILE C 440 1 N LEU C 438 O GLY C 515
SHEET 7 AC4 9 PHE C 465 THR C 469 1 O ILE C 467 N ASP C 439
SHEET 8 AC4 9 ASP C 416 ILE C 423 -1 N PHE C 421 O PHE C 468
SHEET 9 AC4 9 GLU C 407 THR C 413 -1 N GLU C 407 O VAL C 422
SHEET 1 AC5 2 TRP B 173 SER B 174 0
SHEET 2 AC5 2 GLY B 178 PHE B 179 -1 O GLY B 178 N SER B 174
SHEET 1 AC6 7 THR B 205 ILE B 212 0
SHEET 2 AC6 7 LYS B 216 THR B 223 -1 O ILE B 218 N ASN B 211
SHEET 3 AC6 7 ALA B 232 ASP B 238 -1 O TYR B 237 N VAL B 217
SHEET 4 AC6 7 LYS B 243 ILE B 261 -1 O TYR B 253 N ALA B 232
SHEET 5 AC6 7 LYS B 264 SER B 270 -1 O SER B 270 N ASP B 254
SHEET 6 AC6 7 LYS B 282 ILE B 286 -1 O TYR B 284 N CYS B 267
SHEET 7 AC6 7 ILE B 292 TYR B 296 -1 O ASN B 293 N LEU B 285
SHEET 1 AC7 4 PHE B 318 ILE B 321 0
SHEET 2 AC7 4 LYS B 324 THR B 330 -1 O TYR B 326 N LYS B 319
SHEET 3 AC7 4 VAL B 335 ASP B 341 -1 O HIS B 336 N SER B 329
SHEET 4 AC7 4 VAL B 346 SER B 350 -1 O LEU B 349 N LEU B 337
SHEET 1 AC8 4 SER B 355 ILE B 361 0
SHEET 2 AC8 4 ILE B 366 MET B 371 -1 O VAL B 369 N PHE B 358
SHEET 3 AC8 4 GLU B 378 GLU B 383 -1 O LEU B 382 N ILE B 366
SHEET 4 AC8 4 SER B 386 LYS B 389 -1 O SER B 386 N GLU B 383
SHEET 1 AC9 9 GLU B 407 THR B 413 0
SHEET 2 AC9 9 ASP B 416 ILE B 423 -1 O GLY B 420 N PHE B 409
SHEET 3 AC9 9 PHE B 465 THR B 469 -1 O VAL B 466 N ILE B 423
SHEET 4 AC9 9 TYR B 434 ILE B 440 1 N ILE B 437 O ILE B 467
SHEET 5 AC9 9 ILE B 509 GLY B 519 1 O ASP B 510 N TYR B 434
SHEET 6 AC9 9 CYS B 538 GLN B 542 1 O GLN B 542 N GLY B 518
SHEET 7 AC9 9 THR B 593 SER B 598 1 O LEU B 594 N SER B 541
SHEET 8 AC9 9 ALA B 623 PHE B 628 1 O ARG B 624 N PHE B 595
SHEET 9 AC9 9 TYR C 164 LEU C 167 -1 O GLU C 165 N MET B 627
SHEET 1 AD1 4 PHE C 14 PHE C 20 0
SHEET 2 AD1 4 ASN C 26 ASP C 35 -1 O SER C 30 N SER C 16
SHEET 3 AD1 4 SER C 40 ASP C 49 -1 O TYR C 46 N PHE C 29
SHEET 4 AD1 4 ILE C 55 LYS C 57 -1 O LYS C 56 N ASN C 47
SHEET 1 AD2 4 LYS C 65 ASN C 71 0
SHEET 2 AD2 4 THR C 74 ALA C 79 -1 O THR C 74 N LEU C 70
SHEET 3 AD2 4 THR C 96 ASP C 102 -1 O TYR C 99 N PHE C 77
SHEET 4 AD2 4 TYR C 110 LEU C 115 -1 O TYR C 112 N PHE C 98
SHEET 1 AD3 4 ASN C 118 ILE C 124 0
SHEET 2 AD3 4 PHE C 130 ASP C 137 -1 O ASP C 135 N ASN C 118
SHEET 3 AD3 4 LYS C 183 ASP C 191 -1 O TYR C 188 N LEU C 132
SHEET 4 AD3 4 LYS C 196 PRO C 199 -1 O THR C 198 N HIS C 189
SHEET 1 AD4 3 THR C 205 ASN C 206 0
SHEET 2 AD4 3 LYS C 216 THR C 223 -1 O ARG C 222 N ASN C 206
SHEET 3 AD4 3 PHE C 210 ILE C 212 -1 N ASN C 211 O ILE C 218
SHEET 1 AD5 4 THR C 205 ASN C 206 0
SHEET 2 AD5 4 LYS C 216 THR C 223 -1 O ARG C 222 N ASN C 206
SHEET 3 AD5 4 GLY C 233 ASP C 238 -1 O GLY C 233 N GLY C 221
SHEET 4 AD5 4 LYS C 243 ILE C 248 -1 O ILE C 247 N LEU C 234
SHEET 1 AD6 4 ASN C 259 PHE C 260 0
SHEET 2 AD6 4 ILE C 265 LEU C 269 -1 O ILE C 266 N ASN C 259
SHEET 3 AD6 4 LYS C 282 ILE C 286 -1 O TYR C 284 N CYS C 267
SHEET 4 AD6 4 LEU C 294 TYR C 296 -1 O TYR C 296 N ILE C 283
SHEET 1 AD7 4 PHE C 318 ILE C 321 0
SHEET 2 AD7 4 LYS C 324 THR C 330 -1 O TYR C 326 N LYS C 319
SHEET 3 AD7 4 VAL C 335 LEU C 340 -1 O HIS C 336 N SER C 329
SHEET 4 AD7 4 VAL C 346 SER C 350 -1 O LEU C 349 N LEU C 337
SHEET 1 AD8 4 SER C 355 ILE C 361 0
SHEET 2 AD8 4 ILE C 366 MET C 371 -1 O TYR C 367 N ASP C 360
SHEET 3 AD8 4 GLU C 378 GLU C 383 -1 O TYR C 380 N TYR C 368
SHEET 4 AD8 4 SER C 386 LYS C 389 -1 O ILE C 388 N LYS C 381
CRYST1 192.004 124.797 128.898 90.00 90.00 90.00 P 21 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 0.005208 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007758 0.00000
TER 5410 LYS G 660
TER 10820 LYS A 660
TER 16230 LYS B 660
TER 21640 LYS C 660
MASTER 312 0 0 63 156 0 0 622126 4 0 204
END |