HEADER DNA BINDING PROTEIN, CELL CYCLE 05-APR-17 5XEI
TITLE CRYSTAL STRUCTURE OF THE SMC HEAD DOMAIN WITH A COILED COIL AND JOINT
TITLE 2 DERIVED FROM PYROCOCCUS YAYANOSII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHROMOSOME PARTITION PROTEIN SMC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-254 AND 907-1177;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS YAYANOSII (STRAIN CH1 / JCM 16557);
SOURCE 3 ORGANISM_TAXID: 529709;
SOURCE 4 STRAIN: CH1 / JCM 16557;
SOURCE 5 GENE: SMC, PYCH_01200;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CONDENSIN, SMC, HEAD DOMAIN, ABC-ATPASE, DNA BINDING PROTEIN, CELL
KEYWDS 2 CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LEE,H.NOH,B.-H.OH
REVDAT 4 22-NOV-23 5XEI 1 REMARK
REVDAT 3 30-AUG-17 5XEI 1 REMARK
REVDAT 2 02-AUG-17 5XEI 1 JRNL
REVDAT 1 07-JUN-17 5XEI 0
JRNL AUTH M.L.DIEBOLD-DURAND,H.LEE,L.B.RUIZ AVILA,H.NOH,H.C.SHIN,H.IM,
JRNL AUTH 2 F.P.BOCK,F.BURMANN,A.DURAND,A.BASFELD,S.HAM,J.BASQUIN,
JRNL AUTH 3 B.-H.OH,S.GRUBER
JRNL TITL STRUCTURE OF FULL-LENGTH SMC AND REARRANGEMENTS REQUIRED FOR
JRNL TITL 2 CHROMOSOME ORGANIZATION
JRNL REF MOL. CELL V. 67 334 2017
JRNL REFN ISSN 1097-4164
JRNL PMID 28689660
JRNL DOI 10.1016/J.MOLCEL.2017.06.010
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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) : 39.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 18871
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1903
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 39.6296 - 6.2572 0.99 1360 154 0.1794 0.2276
REMARK 3 2 6.2572 - 4.9696 0.99 1323 146 0.1968 0.2730
REMARK 3 3 4.9696 - 4.3423 1.00 1305 144 0.1594 0.2139
REMARK 3 4 4.3423 - 3.9457 0.99 1305 151 0.1877 0.2957
REMARK 3 5 3.9457 - 3.6631 0.99 1284 144 0.1978 0.2865
REMARK 3 6 3.6631 - 3.4473 0.98 1283 146 0.2061 0.2715
REMARK 3 7 3.4473 - 3.2747 0.98 1278 137 0.2147 0.3028
REMARK 3 8 3.2747 - 3.1322 0.95 1234 139 0.2322 0.3062
REMARK 3 9 3.1322 - 3.0117 0.91 1183 136 0.2494 0.3193
REMARK 3 10 3.0117 - 2.9078 0.90 1166 128 0.2617 0.3342
REMARK 3 11 2.9078 - 2.8169 0.89 1141 132 0.2873 0.3263
REMARK 3 12 2.8169 - 2.7364 0.89 1165 131 0.3027 0.3390
REMARK 3 13 2.7364 - 2.6644 0.81 1053 122 0.3013 0.4034
REMARK 3 14 2.6644 - 2.5994 0.70 888 93 0.3138 0.3532
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) : 29.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.96
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 : 0.010 4136
REMARK 3 ANGLE : 1.181 5539
REMARK 3 CHIRALITY : 0.056 622
REMARK 3 PLANARITY : 0.007 719
REMARK 3 DIHEDRAL : 21.165 2611
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 5XEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1300003337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-16
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 : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97941
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.599
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 (%) : 92.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5XNS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 3350, 4% TACSIMATE PH4.0, VAPOR
REMARK 280 DIFFUSION, HANGING 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 60.16000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.41800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.16000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.41800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 903
REMARK 465 GLY A 904
REMARK 465 GLY A 905
REMARK 465 SER A 906
REMARK 465 ARG A 1170
REMARK 465 ASN A 1171
REMARK 465 GLU A 1172
REMARK 465 ALA A 1173
REMARK 465 THR A 1174
REMARK 465 ILE A 1175
REMARK 465 GLY A 1176
REMARK 465 GLY A 1177
REMARK 465 VAL A 1178
REMARK 465 ASP A 1179
REMARK 465 ALA A 1180
REMARK 465 GLY A 1181
REMARK 465 SER A 1182
REMARK 465 SER A 1183
REMARK 465 SER A 1184
REMARK 465 ARG A 1185
REMARK 465 PRO A 1186
REMARK 465 GLY A 1187
REMARK 465 LEU A 1188
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 GLN A 916 CG CD OE1 NE2
REMARK 470 LEU A 917 CG CD1 CD2
REMARK 470 ARG A 918 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 919 CG1 CG2 CD1
REMARK 470 GLN A 920 CG CD OE1 NE2
REMARK 470 LYS A 951 CG CD CE NZ
REMARK 470 ASP A 955 CG OD1 OD2
REMARK 470 LYS A 961 CG CD CE NZ
REMARK 470 LEU A1157 CG CD1 CD2
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 ARG A 1146 NH2 ARG A 1151 1.81
REMARK 500 OE2 GLU A 923 NH1 ARG A 926 2.14
REMARK 500 NH1 ARG A 160 OD2 ASP A 164 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 65 OE2 GLU A 1018 1545 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A1146 CG - CD - NE ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG A1151 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A1151 NE - CZ - NH2 ANGL. DEV. = 3.3 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 PRO A 2 -174.62 -62.96
REMARK 500 LYS A 13 -132.37 40.64
REMARK 500 SER A 14 4.54 -67.99
REMARK 500 LEU A 50 32.06 -83.20
REMARK 500 ALA A 55 -82.44 62.43
REMARK 500 ASP A 65 34.76 -87.21
REMARK 500 PRO A 94 65.67 -66.39
REMARK 500 MET A 134 39.13 37.43
REMARK 500 SER A 136 70.15 57.86
REMARK 500 GLU A 138 19.32 53.84
REMARK 500 GLU A 235 -9.49 -58.33
REMARK 500 ALA A 251 37.26 -75.37
REMARK 500 GLU A 252 -21.66 -140.06
REMARK 500 SER A 938 4.25 -68.08
REMARK 500 LYS A 940 -5.55 -54.05
REMARK 500 VAL A 942 -138.44 -137.71
REMARK 500 LEU A 944 -142.12 -142.91
REMARK 500 ASP A 945 98.86 74.48
REMARK 500 ALA A 962 -73.21 -52.47
REMARK 500 ALA A1059 128.58 -37.90
REMARK 500 SER A1070 -70.26 -133.88
REMARK 500 GLU A1098 -116.42 37.35
REMARK 500 ILE A1099 -20.43 61.53
REMARK 500 ASP A1104 -177.38 -69.23
REMARK 500 LEU A1155 -135.66 -105.09
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5XEI A 1 254 UNP F8AFS8 F8AFS8_PYRYC 1 254
DBREF 5XEI A 907 1177 UNP F8AFS8 F8AFS8_PYRYC 907 1177
SEQADV 5XEI SER A 903 UNP F8AFS8 LINKER
SEQADV 5XEI GLY A 904 UNP F8AFS8 LINKER
SEQADV 5XEI GLY A 905 UNP F8AFS8 LINKER
SEQADV 5XEI SER A 906 UNP F8AFS8 LINKER
SEQADV 5XEI VAL A 1178 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI ASP A 1179 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI ALA A 1180 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI GLY A 1181 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI SER A 1182 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI SER A 1183 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI SER A 1184 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI ARG A 1185 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI PRO A 1186 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI GLY A 1187 UNP F8AFS8 EXPRESSION TAG
SEQADV 5XEI LEU A 1188 UNP F8AFS8 EXPRESSION TAG
SEQRES 1 A 540 MET PRO TYR ILE GLU LYS LEU GLU LEU LYS GLY PHE LYS
SEQRES 2 A 540 SER TYR GLY ASN ARG LYS VAL VAL ILE PRO PHE SER LYS
SEQRES 3 A 540 GLY PHE THR ALA ILE VAL GLY ALA ASN GLY SER GLY LYS
SEQRES 4 A 540 SER ASN ILE GLY ASP ALA ILE LEU PHE VAL LEU GLY GLY
SEQRES 5 A 540 LEU SER ALA LYS ALA MET ARG ALA THR ARG ILE SER ASP
SEQRES 6 A 540 LEU ILE PHE ALA GLY SER LYS GLY GLU PRO PRO ALA LYS
SEQRES 7 A 540 TYR ALA GLU VAL ALA ILE TYR PHE ASN ASN GLU ASP ARG
SEQRES 8 A 540 GLY PHE PRO ILE ASP GLU ASP GLU VAL VAL ILE LYS ARG
SEQRES 9 A 540 ARG VAL TYR PRO ASP GLY ARG SER ALA TYR TRP LEU ASN
SEQRES 10 A 540 GLY ARG ARG ALA THR ARG SER GLU ILE LEU ASP LEU LEU
SEQRES 11 A 540 SER ALA ALA MET ILE SER PRO GLU GLY TYR ASN LEU VAL
SEQRES 12 A 540 LEU GLN GLY ASP ILE THR LYS PHE ILE LYS MET SER PRO
SEQRES 13 A 540 LEU GLU ARG ARG GLN LEU ILE ASP GLU ILE SER GLY ILE
SEQRES 14 A 540 ALA GLU TYR ASP ALA LYS LYS GLU LYS ALA LEU GLU GLU
SEQRES 15 A 540 LEU LYS GLN ALA GLU GLU ASN LEU ALA ARG VAL ASP LEU
SEQRES 16 A 540 LEU ILE LYS GLU VAL LYS LYS GLN LEU ASP LYS LEU GLU
SEQRES 17 A 540 LYS GLU ARG ASN ASP ALA LEU ARG TYR LEU ASP LEU LYS
SEQRES 18 A 540 GLU ARG LEU GLU ARG ALA ARG VAL ALA LEU LEU LEU GLY
SEQRES 19 A 540 GLU ILE LYS ARG LEU GLU SER MET ILE ASP GLU GLY GLU
SEQRES 20 A 540 ARG LYS ARG ALA GLU ILE GLU SER GLY GLY SER GLU ASN
SEQRES 21 A 540 THR ILE LYS VAL LYS SER ALA GLN LEU ARG ILE GLN LEU
SEQRES 22 A 540 GLU GLU LYS ARG ARG GLU LEU LYS HIS PHE ASP ALA ALA
SEQRES 23 A 540 LEU ILE ARG SER VAL LYS GLU VAL SER LEU ASP LEU GLU
SEQRES 24 A 540 VAL LEU ARG LYS GLU ILE GLU ASP MET GLU ALA GLU ILE
SEQRES 25 A 540 LYS ALA LEU GLU PRO VAL ASN MET LYS ALA ILE GLU ASP
SEQRES 26 A 540 PHE GLU VAL VAL GLU ARG ARG TYR LEU GLU LEU LYS SER
SEQRES 27 A 540 LYS ARG GLU LYS LEU GLU ALA GLU LYS GLU SER ILE ILE
SEQRES 28 A 540 GLU PHE ILE ASN GLU ILE GLU LYS GLU LYS LYS ASN VAL
SEQRES 29 A 540 PHE MET ARG THR LEU GLU ALA ILE ALA LYS ASN PHE SER
SEQRES 30 A 540 GLU LEU PHE ALA LYS LEU SER PRO GLY GLY SER ALA ARG
SEQRES 31 A 540 LEU ILE LEU GLU ASN PRO GLU ASP PRO PHE SER GLY GLY
SEQRES 32 A 540 LEU GLU ILE GLU ALA LYS PRO ALA GLY LYS ASP VAL LYS
SEQRES 33 A 540 ARG ILE GLU ALA MET SER GLY GLY GLU LYS ALA LEU THR
SEQRES 34 A 540 ALA LEU ALA PHE ILE PHE ALA ILE GLN ARG PHE LYS PRO
SEQRES 35 A 540 ALA PRO PHE TYR LEU PHE ASP GLU ILE ASP ALA HIS LEU
SEQRES 36 A 540 ASP ASP ALA ASN VAL LYS ARG VAL ALA ASP LEU ILE LYS
SEQRES 37 A 540 GLU SER SER ARG GLU SER GLN PHE ILE VAL ILE THR LEU
SEQRES 38 A 540 ARG ASP VAL MET MET ALA ASN ALA ASP LYS ILE ILE GLY
SEQRES 39 A 540 VAL SER MET ARG ASP GLY VAL SER ARG VAL VAL SER LEU
SEQRES 40 A 540 SER LEU GLU LYS ALA MET LYS ILE LEU GLU GLU ALA LYS
SEQRES 41 A 540 LYS ARG ASN GLU ALA THR ILE GLY GLY VAL ASP ALA GLY
SEQRES 42 A 540 SER SER SER ARG PRO GLY LEU
FORMUL 2 HOH *13(H2 O)
HELIX 1 AA1 SER A 40 LEU A 50 1 11
HELIX 2 AA2 ARG A 62 ILE A 67 5 6
HELIX 3 AA3 THR A 122 ALA A 133 1 12
HELIX 4 AA4 SER A 136 TYR A 140 5 5
HELIX 5 AA5 GLY A 146 LYS A 153 1 8
HELIX 6 AA6 SER A 155 GLY A 168 1 14
HELIX 7 AA7 ILE A 169 GLU A 247 1 79
HELIX 8 AA8 LYS A 249 ILE A 253 5 5
HELIX 9 AA9 ASN A 908 GLU A 927 1 20
HELIX 10 AB1 LEU A 928 PHE A 931 5 4
HELIX 11 AB2 ASP A 932 SER A 938 1 7
HELIX 12 AB3 ASP A 945 GLU A 964 1 20
HELIX 13 AB4 MET A 968 SER A 1032 1 65
HELIX 14 AB5 ASP A 1046 GLY A 1050 5 5
HELIX 15 AB6 GLU A 1067 MET A 1069 5 3
HELIX 16 AB7 GLY A 1071 LYS A 1089 1 19
HELIX 17 AB8 ASP A 1104 SER A 1119 1 16
HELIX 18 AB9 ARG A 1130 ALA A 1137 1 8
HELIX 19 AC1 SER A 1156 ALA A 1167 1 12
SHEET 1 AA1 6 VAL A 20 PRO A 23 0
SHEET 2 AA1 6 TYR A 3 LYS A 10 -1 N LEU A 7 O ILE A 22
SHEET 3 AA1 6 ALA A 80 ASN A 87 -1 O ASN A 87 N TYR A 3
SHEET 4 AA1 6 GLU A 99 VAL A 106 -1 O ILE A 102 N ILE A 84
SHEET 5 AA1 6 SER A 112 LEU A 116 -1 O TRP A 115 N LYS A 103
SHEET 6 AA1 6 ARG A 119 ALA A 121 -1 O ARG A 119 N LEU A 116
SHEET 1 AA2 6 LEU A 142 VAL A 143 0
SHEET 2 AA2 6 PHE A1093 ASP A1097 1 O LEU A1095 N VAL A 143
SHEET 3 AA2 6 GLN A1123 THR A1128 1 O ILE A1127 N PHE A1096
SHEET 4 AA2 6 PHE A 28 VAL A 32 1 N THR A 29 O PHE A1124
SHEET 5 AA2 6 LYS A1139 ARG A1146 1 O ILE A1141 N ALA A 30
SHEET 6 AA2 6 VAL A1149 SER A1154 -1 O VAL A1153 N GLY A1142
SHEET 1 AA3 3 SER A1036 LEU A1041 0
SHEET 2 AA3 3 LEU A1052 LYS A1057 -1 O LYS A1057 N SER A1036
SHEET 3 AA3 3 LYS A1064 ARG A1065 -1 O LYS A1064 N ALA A1056
CISPEP 1 GLU A 964 PRO A 965 0 -0.77
CRYST1 120.320 50.836 122.057 90.00 118.09 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008311 0.000000 0.004435 0.00000
SCALE2 0.000000 0.019671 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009286 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
