HEADER SIGNALING PROTEIN 30-OCT-17 6EUB
TITLE THE FIBRINOGEN-LIKE DOMAIN OF HUMAN ANGPTL4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOPOIETIN-RELATED PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANGIOPOIETIN-LIKE PROTEIN 4,HEPATIC FIBRINOGEN/ANGIOPOIETIN-
COMPND 5 RELATED PROTEIN,HFARP;
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: ANGPTL4, ARP4, HFARP, PGAR, PP1158, PSEC0166, UNQ171/PRO197;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. MDS42;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1110693
KEYWDS LIPID METABOLISM, PLASMA TRIGLYCERIDE, ANGIOPOIETIN-LIKE, CORONARY
KEYWDS 2 ARTERY DISEASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.I.BITEROVA,M.ESMAEELI,H.I.ALANEN,M.SAARANEN,L.W.RUDDOCK
REVDAT 2 17-JAN-24 6EUB 1 REMARK
REVDAT 1 09-MAY-18 6EUB 0
JRNL AUTH E.BITEROVA,M.ESMAEELI,H.I.ALANEN,M.SAARANEN,L.W.RUDDOCK
JRNL TITL STRUCTURES OF ANGPTL3 AND ANGPTL4, MODULATORS OF
JRNL TITL 2 TRIGLYCERIDE LEVELS AND CORONARY ARTERY DISEASE.
JRNL REF SCI REP V. 8 6752 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29713054
JRNL DOI 10.1038/S41598-018-25237-7
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 16046
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 803
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 47.1716 - 4.1789 0.99 2695 142 0.1803 0.2374
REMARK 3 2 4.1789 - 3.3172 1.00 2550 135 0.1682 0.2293
REMARK 3 3 3.3172 - 2.8980 0.99 2561 134 0.2155 0.2669
REMARK 3 4 2.8980 - 2.6330 0.99 2492 132 0.2475 0.2595
REMARK 3 5 2.6330 - 2.4443 0.99 2507 132 0.2771 0.3388
REMARK 3 6 2.4443 - 2.3002 0.97 2438 128 0.3066 0.3491
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.82
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 1800
REMARK 3 ANGLE : 1.054 2437
REMARK 3 CHIRALITY : 0.058 243
REMARK 3 PLANARITY : 0.009 318
REMARK 3 DIHEDRAL : 5.223 1452
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3218 -29.4159 -4.7403
REMARK 3 T TENSOR
REMARK 3 T11: 0.5183 T22: 0.4305
REMARK 3 T33: 0.3479 T12: 0.0416
REMARK 3 T13: -0.0320 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 6.3128 L22: 4.3063
REMARK 3 L33: 6.5739 L12: -1.1530
REMARK 3 L13: -4.2185 L23: 0.3178
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.1474 S13: 0.3240
REMARK 3 S21: 0.0343 S22: -0.0223 S23: -0.1818
REMARK 3 S31: -0.9299 S32: 0.2060 S33: -0.0208
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 222 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8309 -42.2613 -8.9897
REMARK 3 T TENSOR
REMARK 3 T11: 0.3163 T22: 0.4218
REMARK 3 T33: 0.2891 T12: 0.0681
REMARK 3 T13: 0.0045 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 4.8180 L22: 8.3624
REMARK 3 L33: 2.7896 L12: 1.2284
REMARK 3 L13: 0.3820 L23: 1.2700
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: 0.1755 S13: 0.2138
REMARK 3 S21: -0.0095 S22: -0.0168 S23: 0.5596
REMARK 3 S31: 0.1063 S32: -0.1897 S33: -0.0730
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 359 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7257 -46.8947 -7.0841
REMARK 3 T TENSOR
REMARK 3 T11: 0.3681 T22: 0.3691
REMARK 3 T33: 0.2710 T12: 0.0463
REMARK 3 T13: -0.0238 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 2.8562 L22: 2.5887
REMARK 3 L33: 3.1481 L12: 1.2805
REMARK 3 L13: -0.6172 L23: -0.3126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: -0.0373 S13: -0.2078
REMARK 3 S21: 0.0330 S22: 0.1275 S23: -0.0706
REMARK 3 S31: 0.4064 S32: 0.1585 S33: -0.0848
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 360 THROUGH 400 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0577 -55.8573 -2.8898
REMARK 3 T TENSOR
REMARK 3 T11: 0.5481 T22: 0.3947
REMARK 3 T33: 0.3088 T12: 0.0352
REMARK 3 T13: -0.0107 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 6.1810 L22: 8.8378
REMARK 3 L33: 2.7925 L12: -1.5899
REMARK 3 L13: -0.4294 L23: -0.9828
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: -0.2322 S13: -0.5646
REMARK 3 S21: 0.5075 S22: -0.0290 S23: 0.0884
REMARK 3 S31: 0.7198 S32: 0.0603 S33: 0.0259
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 6EUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16070
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.162
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.396
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.86
REMARK 200 R MERGE FOR SHELL (I) : 1.13900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.310
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: 1Z3S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 7.5, 0.2 M
REMARK 280 SODIUM MALONATE, 20 % (W/V) PEG 3350, PH 7.4, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 19.81500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 19.81500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.88500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.88500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.81500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.88500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 19.81500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.88500
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 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 176
REMARK 465 HIS A 177
REMARK 465 HIS A 178
REMARK 465 HIS A 179
REMARK 465 HIS A 180
REMARK 465 HIS A 181
REMARK 465 HIS A 182
REMARK 465 MET A 183
REMARK 465 GLN A 370
REMARK 465 ALA A 401
REMARK 465 ALA A 402
REMARK 465 GLU A 403
REMARK 465 ALA A 404
REMARK 465 ALA A 405
REMARK 465 SER A 406
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 HIS A 231 -11.61 -160.82
REMARK 500 ASP A 232 -0.75 -148.11
REMARK 500 LEU A 345 -118.50 -98.94
REMARK 500 ASN A 358 102.13 -171.04
REMARK 500 TRP A 383 -73.71 -97.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EUA RELATED DB: PDB
DBREF 6EUB A 184 406 UNP Q9BY76 ANGL4_HUMAN 184 406
SEQADV 6EUB MET A 176 UNP Q9BY76 INITIATING METHIONINE
SEQADV 6EUB HIS A 177 UNP Q9BY76 EXPRESSION TAG
SEQADV 6EUB HIS A 178 UNP Q9BY76 EXPRESSION TAG
SEQADV 6EUB HIS A 179 UNP Q9BY76 EXPRESSION TAG
SEQADV 6EUB HIS A 180 UNP Q9BY76 EXPRESSION TAG
SEQADV 6EUB HIS A 181 UNP Q9BY76 EXPRESSION TAG
SEQADV 6EUB HIS A 182 UNP Q9BY76 EXPRESSION TAG
SEQADV 6EUB MET A 183 UNP Q9BY76 EXPRESSION TAG
SEQRES 1 A 231 MET HIS HIS HIS HIS HIS HIS MET LEU PRO ARG ASP CYS
SEQRES 2 A 231 GLN GLU LEU PHE GLN VAL GLY GLU ARG GLN SER GLY LEU
SEQRES 3 A 231 PHE GLU ILE GLN PRO GLN GLY SER PRO PRO PHE LEU VAL
SEQRES 4 A 231 ASN CYS LYS MET THR SER ASP GLY GLY TRP THR VAL ILE
SEQRES 5 A 231 GLN ARG ARG HIS ASP GLY SER VAL ASP PHE ASN ARG PRO
SEQRES 6 A 231 TRP GLU ALA TYR LYS ALA GLY PHE GLY ASP PRO HIS GLY
SEQRES 7 A 231 GLU PHE TRP LEU GLY LEU GLU LYS VAL HIS SER ILE THR
SEQRES 8 A 231 GLY ASP ARG ASN SER ARG LEU ALA VAL GLN LEU ARG ASP
SEQRES 9 A 231 TRP ASP GLY ASN ALA GLU LEU LEU GLN PHE SER VAL HIS
SEQRES 10 A 231 LEU GLY GLY GLU ASP THR ALA TYR SER LEU GLN LEU THR
SEQRES 11 A 231 ALA PRO VAL ALA GLY GLN LEU GLY ALA THR THR VAL PRO
SEQRES 12 A 231 PRO SER GLY LEU SER VAL PRO PHE SER THR TRP ASP GLN
SEQRES 13 A 231 ASP HIS ASP LEU ARG ARG ASP LYS ASN CYS ALA LYS SER
SEQRES 14 A 231 LEU SER GLY GLY TRP TRP PHE GLY THR CYS SER HIS SER
SEQRES 15 A 231 ASN LEU ASN GLY GLN TYR PHE ARG SER ILE PRO GLN GLN
SEQRES 16 A 231 ARG GLN LYS LEU LYS LYS GLY ILE PHE TRP LYS THR TRP
SEQRES 17 A 231 ARG GLY ARG TYR TYR PRO LEU GLN ALA THR THR MET LEU
SEQRES 18 A 231 ILE GLN PRO MET ALA ALA GLU ALA ALA SER
HET 1PE A 501 16
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 2 1PE C10 H22 O6
FORMUL 3 HOH *43(H2 O)
HELIX 1 AA1 ASP A 187 VAL A 194 1 8
HELIX 2 AA2 PRO A 240 GLY A 247 1 8
HELIX 3 AA3 GLY A 258 GLY A 267 1 10
HELIX 4 AA4 GLY A 295 ALA A 299 5 5
HELIX 5 AA5 THR A 305 LEU A 312 1 8
HELIX 6 AA6 ASN A 340 LEU A 345 1 6
HELIX 7 AA7 LYS A 373 GLY A 377 5 5
HELIX 8 AA8 LYS A 381 GLY A 385 1 5
SHEET 1 AA1 5 GLY A 200 ILE A 204 0
SHEET 2 AA1 5 PHE A 212 THR A 219 -1 O CYS A 216 N GLY A 200
SHEET 3 AA1 5 GLY A 222 ARG A 230 -1 O TRP A 224 N LYS A 217
SHEET 4 AA1 5 PHE A 255 TRP A 256 -1 O PHE A 255 N ARG A 229
SHEET 5 AA1 5 PHE A 248 GLY A 249 -1 N PHE A 248 O TRP A 256
SHEET 1 AA2 8 GLY A 200 ILE A 204 0
SHEET 2 AA2 8 PHE A 212 THR A 219 -1 O CYS A 216 N GLY A 200
SHEET 3 AA2 8 GLY A 222 ARG A 230 -1 O TRP A 224 N LYS A 217
SHEET 4 AA2 8 ALA A 392 PRO A 399 -1 O ILE A 397 N THR A 225
SHEET 5 AA2 8 SER A 271 ARG A 278 -1 N ARG A 272 O GLN A 398
SHEET 6 AA2 8 ALA A 284 LEU A 293 -1 O PHE A 289 N LEU A 273
SHEET 7 AA2 8 LEU A 302 LEU A 304 -1 O GLN A 303 N HIS A 292
SHEET 8 AA2 8 LEU A 322 VAL A 324 -1 O LEU A 322 N LEU A 304
SHEET 1 AA3 2 SER A 357 ASN A 358 0
SHEET 2 AA3 2 PHE A 379 TRP A 380 -1 O PHE A 379 N ASN A 358
SSBOND 1 CYS A 188 CYS A 216 1555 1555 2.05
SSBOND 2 CYS A 341 CYS A 354 1555 1555 2.23
SITE 1 AC1 5 LEU A 335 ARG A 337 TRP A 350 THR A 353
SITE 2 AC1 5 LYS A 381
CRYST1 133.020 133.770 39.630 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007518 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025233 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
