HEADER IMMUNE SYSTEM 13-FEB-17 5URV
TITLE CRYSTAL STRUCTURE OF FRIZZLED 7 CRD IN COMPLEX WITH C24 FATTY ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRIZZLED-7;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HFZ7,FZE3;
COMPND 5 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: FZD7;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS FRIZZLED 7, CRD, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUKUND,A.H.NILE,K.STANGER,R.N.HANNOUSH,W.WANG
REVDAT 2 29-JUL-20 5URV 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 10-MAY-17 5URV 0
JRNL AUTH A.H.NILE,S.MUKUND,K.STANGER,W.WANG,R.N.HANNOUSH
JRNL TITL UNSATURATED FATTY ACYL RECOGNITION BY FRIZZLED RECEPTORS
JRNL TITL 2 MEDIATES DIMERIZATION UPON WNT LIGAND BINDING.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 4147 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28377511
JRNL DOI 10.1073/PNAS.1618293114
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 41459
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2120
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 41.3583 - 5.4221 0.99 2662 98 0.1718 0.1827
REMARK 3 2 5.4221 - 4.3052 1.00 2611 155 0.1303 0.1755
REMARK 3 3 4.3052 - 3.7614 0.99 2568 143 0.1240 0.1493
REMARK 3 4 3.7614 - 3.4176 1.00 2625 156 0.1382 0.1907
REMARK 3 5 3.4176 - 3.1728 1.00 2613 139 0.1522 0.2143
REMARK 3 6 3.1728 - 2.9858 1.00 2665 129 0.1647 0.2210
REMARK 3 7 2.9858 - 2.8363 1.00 2662 140 0.1608 0.2107
REMARK 3 8 2.8363 - 2.7128 0.99 2565 153 0.1628 0.2433
REMARK 3 9 2.7128 - 2.6084 1.00 2628 135 0.1682 0.2276
REMARK 3 10 2.6084 - 2.5184 1.00 2651 136 0.1777 0.2295
REMARK 3 11 2.5184 - 2.4397 1.00 2620 146 0.1868 0.2184
REMARK 3 12 2.4397 - 2.3700 1.00 2624 139 0.1863 0.2596
REMARK 3 13 2.3700 - 2.3076 1.00 2590 147 0.2030 0.2567
REMARK 3 14 2.3076 - 2.2513 1.00 2653 156 0.2503 0.3051
REMARK 3 15 2.2513 - 2.2001 0.99 2602 148 0.2715 0.3228
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.120
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 : 0.011 2126
REMARK 3 ANGLE : 1.325 2838
REMARK 3 CHIRALITY : 0.053 299
REMARK 3 PLANARITY : 0.006 365
REMARK 3 DIHEDRAL : 16.281 799
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR CHAIN B OR CHAIN L OR CHAIN S
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2689 40.2663 15.8466
REMARK 3 T TENSOR
REMARK 3 T11: 0.0720 T22: 0.0993
REMARK 3 T33: 0.0945 T12: 0.0053
REMARK 3 T13: -0.0199 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.1943 L22: 0.7467
REMARK 3 L33: 0.4088 L12: -0.1214
REMARK 3 L13: -0.1395 L23: -0.0367
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.0155 S13: 0.0155
REMARK 3 S21: -0.0472 S22: -0.0041 S23: 0.0500
REMARK 3 S31: 0.0580 S32: -0.0156 S33: -0.0031
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 5URV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22293
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
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: NULL
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 (%): 61.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES SODIUM SALT PH 6.5, 2.0M
REMARK 280 AMMONIUM SULFATE, 5%(W/V) PEG 400, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
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 48.78000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.45100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.78000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.45100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 B 208 LIES ON A SPECIAL POSITION.
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 ALA A 0
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 4
REMARK 465 TYR A 5
REMARK 465 HIS A 6
REMARK 465 GLY A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 GLY A 10
REMARK 465 ILE A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 PRO A 14
REMARK 465 ASP A 15
REMARK 465 ASN A 134
REMARK 465 THR A 135
REMARK 465 SER A 136
REMARK 465 ASP A 137
REMARK 465 GLY A 138
REMARK 465 GLY A 139
REMARK 465 ASN A 140
REMARK 465 SER A 141
REMARK 465 HIS A 142
REMARK 465 HIS A 143
REMARK 465 HIS A 144
REMARK 465 HIS A 145
REMARK 465 HIS A 146
REMARK 465 HIS A 147
REMARK 465 ALA B 0
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 PRO B 4
REMARK 465 TYR B 5
REMARK 465 HIS B 6
REMARK 465 GLY B 7
REMARK 465 ASP B 137
REMARK 465 GLY B 138
REMARK 465 GLY B 139
REMARK 465 ASN B 140
REMARK 465 SER B 141
REMARK 465 HIS B 142
REMARK 465 HIS B 143
REMARK 465 HIS B 144
REMARK 465 HIS B 145
REMARK 465 HIS B 146
REMARK 465 HIS B 147
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 ND2 ASN A 33 O5 NAG A 202 1.95
REMARK 500 O2 SO4 B 208 O HOH B 301 2.08
REMARK 500 OE1 GLU B 128 O HOH B 302 2.18
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 O1 SO4 B 208 O HOH B 301 2565 2.08
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 ILE A 30 -168.51 -113.10
REMARK 500 ILE B 30 -166.59 -111.41
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 A 394 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A 395 DISTANCE = 8.07 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE AUTHOR INDICATES THAT THEY COULD NOT DISCERN THE DEGREE OF
REMARK 600 UNSATURATION FOR THE C24 LIPID
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PG B 202
REMARK 610 1PG B 203
REMARK 610 1PG B 204
DBREF 5URV A 0 138 UNP O75084 FZD7_HUMAN 30 168
DBREF 5URV B 0 138 UNP O75084 FZD7_HUMAN 30 168
SEQADV 5URV SER A 2 UNP O75084 ALA 32 CONFLICT
SEQADV 5URV GLY A 139 UNP O75084 EXPRESSION TAG
SEQADV 5URV ASN A 140 UNP O75084 EXPRESSION TAG
SEQADV 5URV SER A 141 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS A 142 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS A 143 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS A 144 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS A 145 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS A 146 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS A 147 UNP O75084 EXPRESSION TAG
SEQADV 5URV SER B 2 UNP O75084 ALA 32 CONFLICT
SEQADV 5URV GLY B 139 UNP O75084 EXPRESSION TAG
SEQADV 5URV ASN B 140 UNP O75084 EXPRESSION TAG
SEQADV 5URV SER B 141 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS B 142 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS B 143 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS B 144 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS B 145 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS B 146 UNP O75084 EXPRESSION TAG
SEQADV 5URV HIS B 147 UNP O75084 EXPRESSION TAG
SEQRES 1 A 148 ALA GLY SER GLN PRO TYR HIS GLY GLU LYS GLY ILE SER
SEQRES 2 A 148 VAL PRO ASP HIS GLY PHE CYS GLN PRO ILE SER ILE PRO
SEQRES 3 A 148 LEU CYS THR ASP ILE ALA TYR ASN GLN THR ILE LEU PRO
SEQRES 4 A 148 ASN LEU LEU GLY HIS THR ASN GLN GLU ASP ALA GLY LEU
SEQRES 5 A 148 GLU VAL HIS GLN PHE TYR PRO LEU VAL LYS VAL GLN CYS
SEQRES 6 A 148 SER PRO GLU LEU ARG PHE PHE LEU CYS SER MET TYR ALA
SEQRES 7 A 148 PRO VAL CYS THR VAL LEU ASP GLN ALA ILE PRO PRO CYS
SEQRES 8 A 148 ARG SER LEU CYS GLU ARG ALA ARG GLN GLY CYS GLU ALA
SEQRES 9 A 148 LEU MET ASN LYS PHE GLY PHE GLN TRP PRO GLU ARG LEU
SEQRES 10 A 148 ARG CYS GLU ASN PHE PRO VAL HIS GLY ALA GLY GLU ILE
SEQRES 11 A 148 CYS VAL GLY GLN ASN THR SER ASP GLY GLY ASN SER HIS
SEQRES 12 A 148 HIS HIS HIS HIS HIS
SEQRES 1 B 148 ALA GLY SER GLN PRO TYR HIS GLY GLU LYS GLY ILE SER
SEQRES 2 B 148 VAL PRO ASP HIS GLY PHE CYS GLN PRO ILE SER ILE PRO
SEQRES 3 B 148 LEU CYS THR ASP ILE ALA TYR ASN GLN THR ILE LEU PRO
SEQRES 4 B 148 ASN LEU LEU GLY HIS THR ASN GLN GLU ASP ALA GLY LEU
SEQRES 5 B 148 GLU VAL HIS GLN PHE TYR PRO LEU VAL LYS VAL GLN CYS
SEQRES 6 B 148 SER PRO GLU LEU ARG PHE PHE LEU CYS SER MET TYR ALA
SEQRES 7 B 148 PRO VAL CYS THR VAL LEU ASP GLN ALA ILE PRO PRO CYS
SEQRES 8 B 148 ARG SER LEU CYS GLU ARG ALA ARG GLN GLY CYS GLU ALA
SEQRES 9 B 148 LEU MET ASN LYS PHE GLY PHE GLN TRP PRO GLU ARG LEU
SEQRES 10 B 148 ARG CYS GLU ASN PHE PRO VAL HIS GLY ALA GLY GLU ILE
SEQRES 11 B 148 CYS VAL GLY GLN ASN THR SER ASP GLY GLY ASN SER HIS
SEQRES 12 B 148 HIS HIS HIS HIS HIS
HET NER A 201 26
HET NAG A 202 14
HET SO4 A 203 5
HET SO4 A 204 5
HET SO4 A 205 5
HET NAG B 201 14
HET 1PG B 202 14
HET 1PG B 203 15
HET 1PG B 204 15
HET SO4 B 205 5
HET SO4 B 206 5
HET SO4 B 207 5
HET SO4 B 208 5
HET SO4 B 209 5
HETNAM NER (15E)-TETRACOS-15-ENOIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETSYN NER CIS-15-TETRACOSENOIC ACID
FORMUL 3 NER C24 H46 O2
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 5 SO4 8(O4 S 2-)
FORMUL 9 1PG 3(C11 H24 O6)
FORMUL 17 HOH *239(H2 O)
HELIX 1 AA1 ILE A 24 THR A 28 5 5
HELIX 2 AA2 ASN A 45 HIS A 54 1 10
HELIX 3 AA3 PHE A 56 GLN A 63 1 8
HELIX 4 AA4 GLU A 67 ALA A 77 1 11
HELIX 5 AA5 CYS A 90 PHE A 108 1 19
HELIX 6 AA6 PRO A 113 PHE A 121 5 9
HELIX 7 AA7 ILE B 24 THR B 28 5 5
HELIX 8 AA8 ASN B 45 HIS B 54 1 10
HELIX 9 AA9 PHE B 56 VAL B 62 1 7
HELIX 10 AB1 GLU B 67 ALA B 77 1 11
HELIX 11 AB2 CYS B 90 GLY B 109 1 20
HELIX 12 AB3 PRO B 113 PHE B 121 5 9
SHEET 1 AA1 2 CYS A 19 PRO A 21 0
SHEET 2 AA1 2 GLN A 34 ILE A 36 -1 O THR A 35 N GLN A 20
SHEET 1 AA2 2 CYS B 19 PRO B 21 0
SHEET 2 AA2 2 GLN B 34 ILE B 36 -1 O THR B 35 N GLN B 20
SSBOND 1 CYS A 19 CYS A 80 1555 1555 2.02
SSBOND 2 CYS A 27 CYS A 73 1555 1555 2.06
SSBOND 3 CYS A 64 CYS A 101 1555 1555 2.07
SSBOND 4 CYS A 90 CYS A 130 1555 1555 2.03
SSBOND 5 CYS A 94 CYS A 118 1555 1555 2.08
SSBOND 6 CYS B 19 CYS B 80 1555 1555 2.01
SSBOND 7 CYS B 27 CYS B 73 1555 1555 2.08
SSBOND 8 CYS B 64 CYS B 101 1555 1555 2.07
SSBOND 9 CYS B 90 CYS B 130 1555 1555 2.03
SSBOND 10 CYS B 94 CYS B 118 1555 1555 2.08
LINK ND2 ASN A 33 C1 NAG A 202 1555 1555 1.53
LINK ND2 ASN B 33 C1 NAG B 201 1555 1555 1.57
CISPEP 1 LEU A 37 PRO A 38 0 -3.87
CISPEP 2 LEU B 37 PRO B 38 0 -1.33
CRYST1 97.560 104.902 41.351 90.00 90.00 90.00 P 21 21 2 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 0.010250 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009533 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024183 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
