HEADER CELL CYCLE 08-OCT-13 4N40
TITLE CRYSTAL STRUCTURE OF HUMAN EPITHELIAL CELL-TRANSFORMING SEQUENCE 2
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN ECT2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES, ISOFORM 4, 45-325;
COMPND 5 SYNONYM: EPITHELIAL CELL-TRANSFORMING SEQUENCE 2 ONCOGENE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ECT2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS TRIPLE BRCT DOMAINS, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZOU,Z.H.SHAO,F.D.LI,D.GONG,C.WANG,Q.GONG,Y.SHI
REVDAT 3 15-NOV-17 4N40 1 REMARK
REVDAT 2 31-DEC-14 4N40 1 JRNL
REVDAT 1 27-AUG-14 4N40 0
JRNL AUTH Y.ZOU,Z.H.SHAO,J.PENG,F.D.LI,D.GONG,C.WANG,X.ZUO,Z.ZHANG,
JRNL AUTH 2 J.WU,Y.SHI,Q.GONG
JRNL TITL CRYSTAL STRUCTURE OF TRIPLE-BRCT-DOMAIN OF ECT2 AND INSIGHTS
JRNL TITL 2 INTO THE BINDING CHARACTERISTICS TO CYK-4
JRNL REF FEBS LETT. V. 588 2911 2014
JRNL REFN ISSN 0014-5793
JRNL PMID 25068414
JRNL DOI 10.1016/J.FEBSLET.2014.07.019
REMARK 2
REMARK 2 RESOLUTION. 3.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
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) : 3.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 9156
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770
REMARK 3 FREE R VALUE TEST SET COUNT : 437
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 36.8753 - 4.4783 1.00 2909 141 0.1913 0.2634
REMARK 3 2 4.4783 - 3.5555 1.00 2899 145 0.2116 0.2620
REMARK 3 3 3.5555 - 3.1063 1.00 2911 151 0.3120 0.3901
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 69.93
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 106.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 112.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31770
REMARK 3 B22 (A**2) : -0.31770
REMARK 3 B33 (A**2) : 0.63530
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.012 2198
REMARK 3 ANGLE : 1.655 2988
REMARK 3 CHIRALITY : 0.101 337
REMARK 3 PLANARITY : 0.007 386
REMARK 3 DIHEDRAL : 15.811 782
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 4N40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082723.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-12; 06-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SSRF; SSRF
REMARK 200 BEAMLINE : BL17U; BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793; 0.9793
REMARK 200 MONOCHROMATOR : PLANE GRATING; PLANE GRATING
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R; ADSC QUANTUM
REMARK 200 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9161
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.95600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 14% MPEG 5000, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.85000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.70911
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.74800
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 61.85000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 35.70911
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.74800
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 61.85000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 35.70911
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.74800
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.41823
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 59.49600
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 71.41823
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 59.49600
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 71.41823
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 59.49600
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 GLU A 45 CG CD OE1 OE2
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 VAL A 82 CG1 CG2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 ASP A 89 CG OD1 OD2
REMARK 470 ASN A 108 CG OD1 ND2
REMARK 470 LYS A 129 CG CD CE NZ
REMARK 470 ARG A 156 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 157 CG CD CE NZ
REMARK 470 LYS A 158 CG CD CE NZ
REMARK 470 GLU A 159 CG CD OE1 OE2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 THR A 184 OG1 CG2
REMARK 470 HIS A 185 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 186 CG CD1 CD2
REMARK 470 ASN A 189 CG OD1 ND2
REMARK 470 GLN A 192 CG CD OE1 NE2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 GLN A 222 CG CD OE1 NE2
REMARK 470 GLU A 234 CG CD OE1 OE2
REMARK 470 ASP A 252 CG OD1 OD2
REMARK 470 GLU A 253 CG CD OE1 OE2
REMARK 470 GLU A 260 CG CD OE1 OE2
REMARK 470 GLU A 275 CD OE1 OE2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 PHE A 292 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 293 CD OE1 OE2
REMARK 470 LYS A 296 CG CD CE NZ
REMARK 470 LYS A 297 CE NZ
REMARK 470 GLN A 303 CG CD OE1 NE2
REMARK 470 LEU A 322 CG CD1 CD2
REMARK 470 GLU A 324 CG CD OE1 OE2
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 THR A 184 N LEU A 186 2.13
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 ASN A 189 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 THR A 191 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 PRO A 291 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 48 35.99 -86.52
REMARK 500 GLN A 57 -139.56 44.83
REMARK 500 GLU A 58 -5.16 -53.16
REMARK 500 LEU A 65 -71.16 -57.26
REMARK 500 CYS A 142 -146.60 -128.95
REMARK 500 THR A 143 11.60 -148.65
REMARK 500 ASN A 180 -153.26 -139.67
REMARK 500 HIS A 185 20.56 17.60
REMARK 500 LEU A 186 115.48 175.98
REMARK 500 ARG A 218 31.35 -96.93
REMARK 500 GLN A 265 32.29 -93.23
REMARK 500 LEU A 272 152.13 -39.95
REMARK 500 ASN A 285 -76.71 -79.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 186 VAL A 187 142.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE REFERENCE SEQUENCE OF THIS PROTEIN IS ISOFORM 4 OF Q9H8V3.
DBREF 4N40 A 45 325 UNP Q9H8V3 ECT2_HUMAN 45 325
SEQRES 1 A 281 GLU MSE PRO GLN ILE GLU THR ARG VAL ILE LEU VAL GLN
SEQRES 2 A 281 GLU ALA GLY LYS GLN GLU GLU LEU ILE LYS ALA LEU LYS
SEQRES 3 A 281 ASP ILE LYS VAL GLY PHE VAL LYS MSE GLU SER VAL GLU
SEQRES 4 A 281 GLU PHE GLU GLY LEU ASP SER PRO GLU PHE GLU ASN VAL
SEQRES 5 A 281 PHE VAL VAL THR ASP PHE GLN ASP SER VAL PHE ASN ASP
SEQRES 6 A 281 LEU TYR LYS ALA ASP CYS ARG VAL ILE GLY PRO PRO VAL
SEQRES 7 A 281 VAL LEU ASN CYS SER GLN LYS GLY GLU PRO LEU PRO PHE
SEQRES 8 A 281 SER CYS ARG PRO LEU TYR CYS THR SER MSE MSE ASN LEU
SEQRES 9 A 281 VAL LEU CYS PHE THR GLY PHE ARG LYS LYS GLU GLU LEU
SEQRES 10 A 281 VAL ARG LEU VAL THR LEU VAL HIS HIS MSE GLY GLY VAL
SEQRES 11 A 281 ILE ARG LYS ASP PHE ASN SER LYS VAL THR HIS LEU VAL
SEQRES 12 A 281 ALA ASN CYS THR GLN GLY GLU LYS PHE ARG VAL ALA VAL
SEQRES 13 A 281 SER LEU GLY THR PRO ILE MSE LYS PRO GLU TRP ILE TYR
SEQRES 14 A 281 LYS ALA TRP GLU ARG ARG ASN GLU GLN ASP PHE TYR ALA
SEQRES 15 A 281 ALA VAL ASP ASP PHE ARG ASN GLU PHE LYS VAL PRO PRO
SEQRES 16 A 281 PHE GLN ASP CYS ILE LEU SER PHE LEU GLY PHE SER ASP
SEQRES 17 A 281 GLU GLU LYS THR ASN MSE GLU GLU MSE THR GLU MSE GLN
SEQRES 18 A 281 GLY GLY LYS TYR LEU PRO LEU GLY ASP GLU ARG CYS THR
SEQRES 19 A 281 HIS LEU VAL VAL GLU GLU ASN ILE VAL LYS ASP LEU PRO
SEQRES 20 A 281 PHE GLU PRO SER LYS LYS LEU TYR VAL VAL LYS GLN GLU
SEQRES 21 A 281 TRP PHE TRP GLY SER ILE GLN MSE ASP ALA ARG ALA GLY
SEQRES 22 A 281 GLU THR MSE TYR LEU TYR GLU LYS
MODRES 4N40 MSE A 46 MET SELENOMETHIONINE
MODRES 4N40 MSE A 79 MET SELENOMETHIONINE
MODRES 4N40 MSE A 145 MET SELENOMETHIONINE
MODRES 4N40 MSE A 146 MET SELENOMETHIONINE
MODRES 4N40 MSE A 171 MET SELENOMETHIONINE
MODRES 4N40 MSE A 207 MET SELENOMETHIONINE
MODRES 4N40 MSE A 258 MET SELENOMETHIONINE
MODRES 4N40 MSE A 261 MET SELENOMETHIONINE
MODRES 4N40 MSE A 264 MET SELENOMETHIONINE
MODRES 4N40 MSE A 312 MET SELENOMETHIONINE
MODRES 4N40 MSE A 320 MET SELENOMETHIONINE
HET MSE A 46 8
HET MSE A 79 8
HET MSE A 145 8
HET MSE A 146 8
HET MSE A 171 8
HET MSE A 207 8
HET MSE A 258 8
HET MSE A 261 8
HET MSE A 264 8
HET MSE A 312 8
HET MSE A 320 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 11(C5 H11 N O2 SE)
HELIX 1 1 GLU A 58 GLY A 60 5 3
HELIX 2 2 GLN A 62 ILE A 72 1 11
HELIX 3 3 GLU A 83 ASP A 89 5 7
HELIX 4 4 ASP A 104 ALA A 113 1 10
HELIX 5 5 GLY A 119 LYS A 129 1 11
HELIX 6 6 LYS A 157 HIS A 170 1 14
HELIX 7 7 GLY A 193 GLY A 203 1 11
HELIX 8 8 PRO A 209 GLU A 217 1 9
HELIX 9 9 VAL A 228 LYS A 236 1 9
HELIX 10 10 SER A 251 GLU A 263 1 13
HELIX 11 11 GLN A 303 MSE A 312 1 10
HELIX 12 12 GLY A 317 LEU A 322 5 6
SHEET 1 A 4 PHE A 76 MSE A 79 0
SHEET 2 A 4 THR A 51 VAL A 56 1 N LEU A 55 O VAL A 77
SHEET 3 A 4 GLU A 94 VAL A 98 1 O VAL A 98 N ILE A 54
SHEET 4 A 4 ARG A 116 ILE A 118 1 O ARG A 116 N PHE A 97
SHEET 1 B 2 VAL A 149 LEU A 150 0
SHEET 2 B 2 VAL A 174 ILE A 175 1 O VAL A 174 N LEU A 150
SHEET 1 C 3 PHE A 152 THR A 153 0
SHEET 2 C 3 VAL A 187 ASN A 189 1 O ALA A 188 N THR A 153
SHEET 3 C 3 ILE A 206 MSE A 207 1 O MSE A 207 N VAL A 187
SHEET 1 D 2 ILE A 244 LEU A 245 0
SHEET 2 D 2 LYS A 268 TYR A 269 1 O LYS A 268 N LEU A 245
SHEET 1 E 3 PHE A 247 LEU A 248 0
SHEET 2 E 3 HIS A 279 VAL A 282 1 O VAL A 281 N LEU A 248
SHEET 3 E 3 TYR A 299 LYS A 302 1 O TYR A 299 N LEU A 280
LINK C GLU A 45 N MSE A 46 1555 1555 1.33
LINK C MSE A 46 N PRO A 47 1555 1555 1.35
LINK C LYS A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N GLU A 80 1555 1555 1.34
LINK C SER A 144 N MSE A 145 1555 1555 1.33
LINK C MSE A 145 N MSE A 146 1555 1555 1.32
LINK C MSE A 146 N ASN A 147 1555 1555 1.33
LINK C HIS A 170 N MSE A 171 1555 1555 1.33
LINK C MSE A 171 N GLY A 172 1555 1555 1.33
LINK C ILE A 206 N MSE A 207 1555 1555 1.33
LINK C MSE A 207 N LYS A 208 1555 1555 1.33
LINK C ASN A 257 N MSE A 258 1555 1555 1.33
LINK C MSE A 258 N GLU A 259 1555 1555 1.33
LINK C GLU A 260 N MSE A 261 1555 1555 1.33
LINK C MSE A 261 N THR A 262 1555 1555 1.33
LINK C GLU A 263 N MSE A 264 1555 1555 1.32
LINK C MSE A 264 N GLN A 265 1555 1555 1.32
LINK C GLN A 311 N MSE A 312 1555 1555 1.34
LINK C MSE A 312 N ASP A 313 1555 1555 1.33
LINK C THR A 319 N MSE A 320 1555 1555 1.33
LINK C MSE A 320 N TYR A 321 1555 1555 1.33
CISPEP 1 PHE A 102 GLN A 103 0 -0.26
CISPEP 2 MSE A 146 ASN A 147 0 1.46
CISPEP 3 MSE A 171 GLY A 172 0 -2.88
CRYST1 123.700 123.700 89.244 90.00 90.00 120.00 H 3 9
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 0.008084 0.004667 0.000000 0.00000
SCALE2 0.000000 0.009335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END