HEADER DNA BINDING PROTEIN 20-MAR-17 5V7K
TITLE PCNA MUTANT D41A/D42A PROTEIN DEFECTIVE IN GENE SILENCING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PCNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: POL30, YBR088C, YBR0811;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CAF-1, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.KONDRATICK,J.M.LITMAN,M.T.WASHINGTON,L.M.DIECKMAN
REVDAT 3 06-MAR-24 5V7K 1 REMARK
REVDAT 2 01-JAN-20 5V7K 1 REMARK
REVDAT 1 14-MAR-18 5V7K 0
JRNL AUTH C.M.KONDRATICK,J.M.LITMAN,K.V.SHAFFER,M.T.WASHINGTON,
JRNL AUTH 2 L.M.DIECKMAN
JRNL TITL CRYSTAL STRUCTURES OF PCNA MUTANT PROTEINS DEFECTIVE IN GENE
JRNL TITL 2 SILENCING SUGGEST A NOVEL INTERACTION SITE ON THE FRONT FACE
JRNL TITL 3 OF THE PCNA RING.
JRNL REF PLOS ONE V. 13 93333 2018
JRNL REFN ESSN 1932-6203
JRNL PMID 29499038
JRNL DOI 10.1371/JOURNAL.PONE.0193333
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FORCE FIELD X
REMARK 3 AUTHORS : MICHAEL J. SCHNIEDERS,TIMOTHY D. FENN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.190
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22320
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 1062
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 14.8340 - 5.9819 1.00 2673 128 0.1426 0.1627
REMARK 3 2 5.9819 - 4.8009 1.00 2647 137 0.1552 0.2050
REMARK 3 3 4.8009 - 4.2099 1.00 2637 130 0.1293 0.1965
REMARK 3 4 4.2099 - 3.8323 1.00 2673 132 0.1999 0.2636
REMARK 3 5 3.8323 - 3.5617 1.00 2673 137 0.2128 0.2291
REMARK 3 6 3.5617 - 3.3542 1.00 2661 131 0.2673 0.3169
REMARK 3 7 3.3542 - 3.1880 1.00 2647 131 0.2964 0.3407
REMARK 3 8 3.1880 - 3.0505 1.00 2647 136 0.3330 0.3800
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.510
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.120
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 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 : 0.021 2028
REMARK 3 ANGLE : 1.927 2736
REMARK 3 CHIRALITY : 0.076 324
REMARK 3 PLANARITY : 0.009 350
REMARK 3 DIHEDRAL : 18.298 762
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 5V7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226909.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11773
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 14.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE, PH 5.43, 0.529
REMARK 280 AMMONIUM SULFATE, 0.729M LITHIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 61.16150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.16150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.16150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.16150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.16150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.16150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 61.16150
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 61.16150
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 61.16150
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 61.16150
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 61.16150
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 61.16150
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 61.16150
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 61.16150
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 61.16150
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 61.16150
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 61.16150
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 61.16150
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 ASP A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
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 ILE A 216 HG SER A 219 1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 146 CB LYS A 146 CG 0.183
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 A 44 NE - CZ - NH2 ANGL. DEV. = -3.1 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 GLU A 3 89.70 -153.61
REMARK 500 PHE A 19 21.78 -142.81
REMARK 500 TYR A 60 133.54 -170.58
REMARK 500 THR A 106 -3.05 -58.04
REMARK 500 ASP A 109 -62.18 -138.66
REMARK 500 LYS A 164 122.81 -26.81
REMARK 500 PHE A 185 130.68 -173.18
REMARK 500 PRO A 191 7.89 -61.83
REMARK 500 SER A 220 1.68 -58.71
REMARK 500 PHE A 254 -81.88 -80.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V7M RELATED DB: PDB
REMARK 900 RELATED ID: 5V7L RELATED DB: PDB
DBREF 5V7K A 1 258 UNP P15873 PCNA_YEAST 1 258
SEQADV 5V7K MET A -6 UNP P15873 INITIATING METHIONINE
SEQADV 5V7K HIS A -5 UNP P15873 EXPRESSION TAG
SEQADV 5V7K HIS A -4 UNP P15873 EXPRESSION TAG
SEQADV 5V7K HIS A -3 UNP P15873 EXPRESSION TAG
SEQADV 5V7K HIS A -2 UNP P15873 EXPRESSION TAG
SEQADV 5V7K HIS A -1 UNP P15873 EXPRESSION TAG
SEQADV 5V7K HIS A 0 UNP P15873 EXPRESSION TAG
SEQADV 5V7K ALA A 41 UNP P15873 ASP 41 ENGINEERED MUTATION
SEQADV 5V7K ALA A 42 UNP P15873 ASP 42 ENGINEERED MUTATION
SEQRES 1 A 265 MET HIS HIS HIS HIS HIS HIS MET LEU GLU ALA LYS PHE
SEQRES 2 A 265 GLU GLU ALA SER LEU PHE LYS ARG ILE ILE ASP GLY PHE
SEQRES 3 A 265 LYS ASP CYS VAL GLN LEU VAL ASN PHE GLN CYS LYS GLU
SEQRES 4 A 265 ASP GLY ILE ILE ALA GLN ALA VAL ALA ALA SER ARG VAL
SEQRES 5 A 265 LEU LEU VAL SER LEU GLU ILE GLY VAL GLU ALA PHE GLN
SEQRES 6 A 265 GLU TYR ARG CYS ASP HIS PRO VAL THR LEU GLY MET ASP
SEQRES 7 A 265 LEU THR SER LEU SER LYS ILE LEU ARG CYS GLY ASN ASN
SEQRES 8 A 265 THR ASP THR LEU THR LEU ILE ALA ASP ASN THR PRO ASP
SEQRES 9 A 265 SER ILE ILE LEU LEU PHE GLU ASP THR LYS LYS ASP ARG
SEQRES 10 A 265 ILE ALA GLU TYR SER LEU LYS LEU MET ASP ILE ASP ALA
SEQRES 11 A 265 ASP PHE LEU LYS ILE GLU GLU LEU GLN TYR ASP SER THR
SEQRES 12 A 265 LEU SER LEU PRO SER SER GLU PHE SER LYS ILE VAL ARG
SEQRES 13 A 265 ASP LEU SER GLN LEU SER ASP SER ILE ASN ILE MET ILE
SEQRES 14 A 265 THR LYS GLU THR ILE LYS PHE VAL ALA ASP GLY ASP ILE
SEQRES 15 A 265 GLY SER GLY SER VAL ILE ILE LYS PRO PHE VAL ASP MET
SEQRES 16 A 265 GLU HIS PRO GLU THR SER ILE LYS LEU GLU MET ASP GLN
SEQRES 17 A 265 PRO VAL ASP LEU THR PHE GLY ALA LYS TYR LEU LEU ASP
SEQRES 18 A 265 ILE ILE LYS GLY SER SER LEU SER ASP ARG VAL GLY ILE
SEQRES 19 A 265 ARG LEU SER SER GLU ALA PRO ALA LEU PHE GLN PHE ASP
SEQRES 20 A 265 LEU LYS SER GLY PHE LEU GLN PHE PHE LEU ALA PRO LYS
SEQRES 21 A 265 PHE ASN ASP GLU GLU
HELIX 1 AA1 GLU A 8 ASP A 21 1 14
HELIX 2 AA2 LEU A 72 ARG A 80 1 9
HELIX 3 AA3 SER A 141 SER A 152 1 12
HELIX 4 AA4 ALA A 209 LYS A 217 1 9
HELIX 5 AA5 GLY A 218 SER A 222 5 5
SHEET 1 AA1 5 PHE A 57 GLU A 59 0
SHEET 2 AA1 5 LEU A 2 PHE A 6 -1 N LYS A 5 O GLU A 59
SHEET 3 AA1 5 THR A 87 ALA A 92 -1 O LEU A 90 N ALA A 4
SHEET 4 AA1 5 SER A 98 GLU A 104 -1 O GLU A 104 N THR A 87
SHEET 5 AA1 5 ILE A 111 LYS A 117 -1 O LEU A 116 N ILE A 99
SHEET 1 AA2 9 VAL A 66 ASP A 71 0
SHEET 2 AA2 9 LEU A 25 LYS A 31 -1 N CYS A 30 O VAL A 66
SHEET 3 AA2 9 GLY A 34 VAL A 40 -1 O ILE A 36 N GLN A 29
SHEET 4 AA2 9 LEU A 46 GLY A 53 -1 O ILE A 52 N ILE A 35
SHEET 5 AA2 9 GLY A 244 LEU A 250 -1 O GLN A 247 N SER A 49
SHEET 6 AA2 9 ALA A 235 ASP A 240 -1 N ALA A 235 O LEU A 250
SHEET 7 AA2 9 ARG A 224 LEU A 229 -1 N GLY A 226 O GLN A 238
SHEET 8 AA2 9 SER A 135 PRO A 140 -1 N LEU A 139 O VAL A 225
SHEET 9 AA2 9 LYS A 196 MET A 199 -1 O GLU A 198 N THR A 136
SHEET 1 AA3 4 SER A 177 ILE A 182 0
SHEET 2 AA3 4 THR A 166 ASP A 172 -1 N PHE A 169 O VAL A 180
SHEET 3 AA3 4 SER A 157 THR A 163 -1 N ASN A 159 O VAL A 170
SHEET 4 AA3 4 VAL A 203 GLY A 208 -1 O PHE A 207 N ILE A 158
CRYST1 122.323 122.323 122.323 90.00 90.00 90.00 P 21 3 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 0.008175 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008175 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
