HEADER MEMBRANE PROTEIN 30-JUN-18 6GYN
TITLE STRUCTURE OF HUMAN HCN4 HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-
TITLE 2 GATED ION CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC
COMPND 3 NUCLEOTIDE-GATED CHANNEL 4;
COMPND 4 CHAIN: A, B, C, D;
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: HCN4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE
KEYWDS ION CHANNEL, PACEMAKER CURRENT, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.A.SHINTRE,A.C.W.PIKE,A.TESSITORE,M.YOUNG,S.R.BUSHELL,C.STRAIN-
AUTHOR 2 DAMERELL,S.MUKHOPADHYAY,N.A.BURGESS-BROWN,J.T.HUISKONEN,
AUTHOR 3 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,E.P.CARPENTER,STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (SGC)
REVDAT 2 11-DEC-19 6GYN 1 SCALE
REVDAT 1 08-MAY-19 6GYN 0
JRNL AUTH C.A.SHINTRE,A.C.W.PIKE,A.TESSITORE,M.YOUNG,S.R.BUSHELL,
JRNL AUTH 2 C.STRAIN-DAMERELL,S.MUKHOPADHYAY,N.A.BURGESS-BROWN,
JRNL AUTH 3 J.T.HUISKONEN,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
JRNL AUTH 4 E.P.CARPENTER
JRNL TITL STRUCTURE OF HUMAN HCN4 HYPERPOLARIZATION-ACTIVATED CYCLIC
JRNL TITL 2 NUCLEOTIDE-GATED ION CHANNEL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, EPU, CTFFIND, COOT, PHENIX,
REMARK 3 RELION, RELION, RELION, CRYOSPARC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : MODEL REFINED AGAINST THE CRYOSPARC B-FACTOR
REMARK 3 SHARPENED MAP USING DEFAULT RESTRAINTS
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.400
REMARK 3 NUMBER OF PARTICLES : 25764
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6GYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200010747.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : POTASSIUM/SODIUM
REMARK 245 HYPERPOLARIZATION-ACTIVATED
REMARK 245 CYCLIC NUCLEOTIDE-GATED ION
REMARK 245 CHANNEL 4
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOTTED FOR 5.5S BEFORE PLUNGE
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 1294
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 48.70
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 37313
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : EBIC TITAN KRIOS M02
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 54070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 87250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -416.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 199
REMARK 465 MET A 200
REMARK 465 LEU A 201
REMARK 465 PRO A 202
REMARK 465 GLU A 203
REMARK 465 ALA A 204
REMARK 465 GLU A 205
REMARK 465 VAL A 206
REMARK 465 ARG A 207
REMARK 465 LEU A 208
REMARK 465 GLY A 209
REMARK 465 GLN A 210
REMARK 465 ALA A 211
REMARK 465 GLY A 212
REMARK 465 PHE A 213
REMARK 465 ASP A 709
REMARK 465 ARG A 710
REMARK 465 LEU A 711
REMARK 465 ASP A 712
REMARK 465 ARG A 713
REMARK 465 ILE A 714
REMARK 465 GLY A 715
REMARK 465 LYS A 716
REMARK 465 LYS A 717
REMARK 465 ASN A 718
REMARK 465 SER A 719
REMARK 465 SER B 199
REMARK 465 MET B 200
REMARK 465 LEU B 201
REMARK 465 PRO B 202
REMARK 465 GLU B 203
REMARK 465 ALA B 204
REMARK 465 GLU B 205
REMARK 465 VAL B 206
REMARK 465 ARG B 207
REMARK 465 LEU B 208
REMARK 465 GLY B 209
REMARK 465 GLN B 210
REMARK 465 ALA B 211
REMARK 465 GLY B 212
REMARK 465 PHE B 213
REMARK 465 ASP B 709
REMARK 465 ARG B 710
REMARK 465 LEU B 711
REMARK 465 ASP B 712
REMARK 465 ARG B 713
REMARK 465 ILE B 714
REMARK 465 GLY B 715
REMARK 465 LYS B 716
REMARK 465 LYS B 717
REMARK 465 ASN B 718
REMARK 465 SER B 719
REMARK 465 SER C 199
REMARK 465 MET C 200
REMARK 465 LEU C 201
REMARK 465 PRO C 202
REMARK 465 GLU C 203
REMARK 465 ALA C 204
REMARK 465 GLU C 205
REMARK 465 VAL C 206
REMARK 465 ARG C 207
REMARK 465 LEU C 208
REMARK 465 GLY C 209
REMARK 465 GLN C 210
REMARK 465 ALA C 211
REMARK 465 GLY C 212
REMARK 465 PHE C 213
REMARK 465 ASP C 709
REMARK 465 ARG C 710
REMARK 465 LEU C 711
REMARK 465 ASP C 712
REMARK 465 ARG C 713
REMARK 465 ILE C 714
REMARK 465 GLY C 715
REMARK 465 LYS C 716
REMARK 465 LYS C 717
REMARK 465 ASN C 718
REMARK 465 SER C 719
REMARK 465 SER D 199
REMARK 465 MET D 200
REMARK 465 LEU D 201
REMARK 465 PRO D 202
REMARK 465 GLU D 203
REMARK 465 ALA D 204
REMARK 465 GLU D 205
REMARK 465 VAL D 206
REMARK 465 ARG D 207
REMARK 465 LEU D 208
REMARK 465 GLY D 209
REMARK 465 GLN D 210
REMARK 465 ALA D 211
REMARK 465 GLY D 212
REMARK 465 PHE D 213
REMARK 465 ASP D 709
REMARK 465 ARG D 710
REMARK 465 LEU D 711
REMARK 465 ASP D 712
REMARK 465 ARG D 713
REMARK 465 ILE D 714
REMARK 465 GLY D 715
REMARK 465 LYS D 716
REMARK 465 LYS D 717
REMARK 465 ASN D 718
REMARK 465 SER D 719
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 ARG A 216 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 218 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 290 CG CD OE1 OE2
REMARK 470 ASN A 291 CG OD1 ND2
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 ASP A 322 CG OD1 OD2
REMARK 470 ASN A 323 CG OD1 ND2
REMARK 470 THR A 324 OG1 CG2
REMARK 470 GLU A 325 CD OE1 OE2
REMARK 470 LYS A 369 CG CD CE NZ
REMARK 470 GLU A 403 CD OE1 OE2
REMARK 470 GLN A 484 CG CD OE1 NE2
REMARK 470 GLU A 567 CD OE1 OE2
REMARK 470 ASN A 598 CG OD1 ND2
REMARK 470 LYS A 630 CD CE NZ
REMARK 470 ASN A 647 CG OD1 ND2
REMARK 470 ARG A 666 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 708 CG CD1 CD2
REMARK 470 ARG B 216 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 218 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 290 CG CD OE1 OE2
REMARK 470 ASN B 291 CG OD1 ND2
REMARK 470 GLU B 321 CG CD OE1 OE2
REMARK 470 ASP B 322 CG OD1 OD2
REMARK 470 ASN B 323 CG OD1 ND2
REMARK 470 THR B 324 OG1 CG2
REMARK 470 GLU B 325 CD OE1 OE2
REMARK 470 LYS B 369 CG CD CE NZ
REMARK 470 GLU B 403 CD OE1 OE2
REMARK 470 GLN B 484 CG CD OE1 NE2
REMARK 470 GLU B 567 CD OE1 OE2
REMARK 470 ASN B 598 CG OD1 ND2
REMARK 470 LYS B 630 CD CE NZ
REMARK 470 ASN B 647 CG OD1 ND2
REMARK 470 ARG B 666 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 708 CG CD1 CD2
REMARK 470 ARG C 216 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 218 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 290 CG CD OE1 OE2
REMARK 470 ASN C 291 CG OD1 ND2
REMARK 470 GLU C 321 CG CD OE1 OE2
REMARK 470 ASP C 322 CG OD1 OD2
REMARK 470 ASN C 323 CG OD1 ND2
REMARK 470 THR C 324 OG1 CG2
REMARK 470 GLU C 325 CD OE1 OE2
REMARK 470 LYS C 369 CG CD CE NZ
REMARK 470 GLU C 403 CD OE1 OE2
REMARK 470 GLN C 484 CG CD OE1 NE2
REMARK 470 GLU C 567 CD OE1 OE2
REMARK 470 ASN C 598 CG OD1 ND2
REMARK 470 LYS C 630 CD CE NZ
REMARK 470 ASN C 647 CG OD1 ND2
REMARK 470 ARG C 666 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 708 CG CD1 CD2
REMARK 470 ARG D 216 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 218 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 290 CG CD OE1 OE2
REMARK 470 ASN D 291 CG OD1 ND2
REMARK 470 GLU D 321 CG CD OE1 OE2
REMARK 470 ASP D 322 CG OD1 OD2
REMARK 470 ASN D 323 CG OD1 ND2
REMARK 470 THR D 324 OG1 CG2
REMARK 470 GLU D 325 CD OE1 OE2
REMARK 470 LYS D 369 CG CD CE NZ
REMARK 470 GLU D 403 CD OE1 OE2
REMARK 470 GLN D 484 CG CD OE1 NE2
REMARK 470 GLU D 567 CD OE1 OE2
REMARK 470 ASN D 598 CG OD1 ND2
REMARK 470 LYS D 630 CD CE NZ
REMARK 470 ASN D 647 CG OD1 ND2
REMARK 470 ARG D 666 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 708 CG CD1 CD2
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 TRP A 253 63.64 60.64
REMARK 500 GLU A 290 31.91 -94.42
REMARK 500 TRP A 341 30.72 -140.86
REMARK 500 PHE A 445 74.59 53.10
REMARK 500 TYR A 481 -154.34 -94.89
REMARK 500 TRP B 253 63.52 60.72
REMARK 500 GLU B 290 31.86 -94.38
REMARK 500 TRP B 341 30.72 -140.82
REMARK 500 PHE B 445 74.62 53.04
REMARK 500 TYR B 481 -154.31 -94.98
REMARK 500 TRP C 253 63.63 60.67
REMARK 500 GLU C 290 32.00 -94.43
REMARK 500 TRP C 341 30.69 -140.80
REMARK 500 PHE C 445 74.55 53.12
REMARK 500 TYR C 481 -154.35 -94.92
REMARK 500 TRP D 253 63.63 60.67
REMARK 500 GLU D 290 32.00 -94.43
REMARK 500 TRP D 341 30.69 -140.80
REMARK 500 PHE D 445 74.62 53.01
REMARK 500 TYR D 481 -154.35 -94.91
REMARK 500
REMARK 500 REMARK: NULL
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 PC1 A 801
REMARK 610 PC1 A 802
REMARK 610 PC1 A 803
REMARK 610 3PE A 804
REMARK 610 3PE A 805
REMARK 610 PC1 A 806
REMARK 610 PC1 A 807
REMARK 610 PC1 A 808
REMARK 610 PC1 A 809
REMARK 610 PC1 B 801
REMARK 610 PC1 B 802
REMARK 610 PC1 B 803
REMARK 610 PC1 B 804
REMARK 610 PC1 B 805
REMARK 610 3PE B 806
REMARK 610 3PE B 807
REMARK 610 PC1 B 808
REMARK 610 PC1 B 809
REMARK 610 PC1 C 801
REMARK 610 PC1 C 802
REMARK 610 PC1 C 803
REMARK 610 PC1 C 804
REMARK 610 PC1 C 805
REMARK 610 3PE C 806
REMARK 610 3PE C 807
REMARK 610 PC1 C 808
REMARK 610 PC1 C 809
REMARK 610 PC1 D 801
REMARK 610 PC1 D 802
REMARK 610 PC1 D 803
REMARK 610 PC1 D 804
REMARK 610 PC1 D 805
REMARK 610 PC1 D 806
REMARK 610 PC1 D 807
REMARK 610 3PE D 808
REMARK 610 3PE D 809
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-0093 RELATED DB: EMDB
REMARK 900 STRUCTURE OF HUMAN HCN4 HYPERPOLARIZATION-ACTIVATED CYCLIC
REMARK 900 NUCLEOTIDE-GATED ION CHANNEL
DBREF 6GYN A 201 719 UNP Q9Y3Q4 HCN4_HUMAN 201 719
DBREF 6GYN B 201 719 UNP Q9Y3Q4 HCN4_HUMAN 201 719
DBREF 6GYN C 201 719 UNP Q9Y3Q4 HCN4_HUMAN 201 719
DBREF 6GYN D 201 719 UNP Q9Y3Q4 HCN4_HUMAN 201 719
SEQADV 6GYN SER A 199 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN MET A 200 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN SER B 199 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN MET B 200 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN SER C 199 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN MET C 200 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN SER D 199 UNP Q9Y3Q4 EXPRESSION TAG
SEQADV 6GYN MET D 200 UNP Q9Y3Q4 EXPRESSION TAG
SEQRES 1 A 521 SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA
SEQRES 2 A 521 GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO
SEQRES 3 A 521 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 4 A 521 LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA
SEQRES 5 A 521 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 6 A 521 TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN
SEQRES 7 A 521 LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP
SEQRES 8 A 521 GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER
SEQRES 9 A 521 ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG
SEQRES 10 A 521 THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU
SEQRES 11 A 521 ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP
SEQRES 12 A 521 PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 13 A 521 ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL
SEQRES 14 A 521 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 15 A 521 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 16 A 521 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 17 A 521 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL
SEQRES 18 A 521 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 19 A 521 GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE
SEQRES 20 A 521 PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN
SEQRES 21 A 521 ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 22 A 521 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN
SEQRES 23 A 521 ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU
SEQRES 24 A 521 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE
SEQRES 25 A 521 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 26 A 521 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 27 A 521 TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN
SEQRES 28 A 521 ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 29 A 521 MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU
SEQRES 30 A 521 PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS
SEQRES 31 A 521 LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 32 A 521 ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU
SEQRES 33 A 521 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR
SEQRES 34 A 521 ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL
SEQRES 35 A 521 SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA
SEQRES 36 A 521 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG
SEQRES 37 A 521 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 38 A 521 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 39 A 521 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 40 A 521 VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 41 A 521 SER
SEQRES 1 B 521 SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA
SEQRES 2 B 521 GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO
SEQRES 3 B 521 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 4 B 521 LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA
SEQRES 5 B 521 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 6 B 521 TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN
SEQRES 7 B 521 LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP
SEQRES 8 B 521 GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER
SEQRES 9 B 521 ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG
SEQRES 10 B 521 THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU
SEQRES 11 B 521 ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP
SEQRES 12 B 521 PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 13 B 521 ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL
SEQRES 14 B 521 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 15 B 521 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 16 B 521 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 17 B 521 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL
SEQRES 18 B 521 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 19 B 521 GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE
SEQRES 20 B 521 PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN
SEQRES 21 B 521 ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 22 B 521 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN
SEQRES 23 B 521 ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU
SEQRES 24 B 521 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE
SEQRES 25 B 521 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 26 B 521 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 27 B 521 TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN
SEQRES 28 B 521 ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 29 B 521 MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU
SEQRES 30 B 521 PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS
SEQRES 31 B 521 LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 32 B 521 ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU
SEQRES 33 B 521 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR
SEQRES 34 B 521 ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL
SEQRES 35 B 521 SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA
SEQRES 36 B 521 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG
SEQRES 37 B 521 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 38 B 521 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 39 B 521 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 40 B 521 VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 41 B 521 SER
SEQRES 1 C 521 SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA
SEQRES 2 C 521 GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO
SEQRES 3 C 521 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 4 C 521 LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA
SEQRES 5 C 521 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 6 C 521 TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN
SEQRES 7 C 521 LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP
SEQRES 8 C 521 GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER
SEQRES 9 C 521 ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG
SEQRES 10 C 521 THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU
SEQRES 11 C 521 ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP
SEQRES 12 C 521 PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 13 C 521 ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL
SEQRES 14 C 521 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 15 C 521 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 16 C 521 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 17 C 521 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL
SEQRES 18 C 521 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 19 C 521 GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE
SEQRES 20 C 521 PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN
SEQRES 21 C 521 ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 22 C 521 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN
SEQRES 23 C 521 ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU
SEQRES 24 C 521 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE
SEQRES 25 C 521 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 26 C 521 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 27 C 521 TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN
SEQRES 28 C 521 ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 29 C 521 MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU
SEQRES 30 C 521 PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS
SEQRES 31 C 521 LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 32 C 521 ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU
SEQRES 33 C 521 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR
SEQRES 34 C 521 ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL
SEQRES 35 C 521 SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA
SEQRES 36 C 521 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG
SEQRES 37 C 521 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 38 C 521 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 39 C 521 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 40 C 521 VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 41 C 521 SER
SEQRES 1 D 521 SER MET LEU PRO GLU ALA GLU VAL ARG LEU GLY GLN ALA
SEQRES 2 D 521 GLY PHE MET GLN ARG GLN PHE GLY ALA MET LEU GLN PRO
SEQRES 3 D 521 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 4 D 521 LYS ALA VAL GLU ARG GLU GLN GLU ARG VAL LYS SER ALA
SEQRES 5 D 521 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 6 D 521 TYR TRP ASP LEU THR MET LEU LEU LEU MET VAL GLY ASN
SEQRES 7 D 521 LEU ILE ILE ILE PRO VAL GLY ILE THR PHE PHE LYS ASP
SEQRES 8 D 521 GLU ASN THR THR PRO TRP ILE VAL PHE ASN VAL VAL SER
SEQRES 9 D 521 ASP THR PHE PHE LEU ILE ASP LEU VAL LEU ASN PHE ARG
SEQRES 10 D 521 THR GLY ILE VAL VAL GLU ASP ASN THR GLU ILE ILE LEU
SEQRES 11 D 521 ASP PRO GLN ARG ILE LYS MET LYS TYR LEU LYS SER TRP
SEQRES 12 D 521 PHE MET VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 13 D 521 ILE PHE LEU ILE VAL GLU THR ARG ILE ASP SER GLU VAL
SEQRES 14 D 521 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 15 D 521 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 16 D 521 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 17 D 521 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE VAL
SEQRES 18 D 521 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 19 D 521 GLY CYS LEU GLN PHE LEU VAL PRO MET LEU GLN ASP PHE
SEQRES 20 D 521 PRO ASP ASP CYS TRP VAL SER ILE ASN ASN MET VAL ASN
SEQRES 21 D 521 ASN SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 22 D 521 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ARG GLN
SEQRES 23 D 521 ALA PRO VAL GLY MET SER ASP VAL TRP LEU THR MET LEU
SEQRES 24 D 521 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE ILE
SEQRES 25 D 521 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 26 D 521 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 27 D 521 TYR MET SER PHE HIS LYS LEU PRO PRO ASP THR ARG GLN
SEQRES 28 D 521 ARG ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 29 D 521 MET PHE ASP GLU GLU SER ILE LEU GLY GLU LEU SER GLU
SEQRES 30 D 521 PRO LEU ARG GLU GLU ILE ILE ASN PHE ASN CYS ARG LYS
SEQRES 31 D 521 LEU VAL ALA SER MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 32 D 521 ASN PHE VAL THR SER MET LEU THR LYS LEU ARG PHE GLU
SEQRES 33 D 521 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY THR
SEQRES 34 D 521 ILE GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL VAL
SEQRES 35 D 521 SER VAL LEU THR LYS GLY ASN LYS GLU THR LYS LEU ALA
SEQRES 36 D 521 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR ARG
SEQRES 37 D 521 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 38 D 521 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 39 D 521 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 40 D 521 VAL ALA LEU ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 41 D 521 SER
HET PC1 A 801 36
HET PC1 A 802 29
HET PC1 A 803 14
HET 3PE A 804 30
HET 3PE A 805 32
HET PC1 A 806 23
HET PC1 A 807 15
HET PC1 A 808 35
HET PC1 A 809 15
HET PC1 B 801 35
HET PC1 B 802 15
HET PC1 B 803 36
HET PC1 B 804 29
HET PC1 B 805 14
HET 3PE B 806 30
HET 3PE B 807 32
HET PC1 B 808 23
HET PC1 B 809 15
HET PC1 C 801 35
HET PC1 C 802 15
HET PC1 C 803 36
HET PC1 C 804 29
HET PC1 C 805 14
HET 3PE C 806 30
HET 3PE C 807 32
HET PC1 C 808 23
HET PC1 C 809 15
HET PC1 D 801 23
HET PC1 D 802 15
HET PC1 D 803 35
HET PC1 D 804 15
HET PC1 D 805 36
HET PC1 D 806 29
HET PC1 D 807 14
HET 3PE D 808 30
HET 3PE D 809 32
HETNAM PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
HETNAM 3PE 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
HETSYN PC1 3-SN-PHOSPHATIDYLCHOLINE
HETSYN 3PE 3-SN-PHOSPHATIDYLETHANOLAMINE
FORMUL 5 PC1 28(C44 H88 N O8 P)
FORMUL 8 3PE 8(C41 H82 N O8 P)
HELIX 1 AA1 ARG A 216 LEU A 222 1 7
HELIX 2 AA2 ASN A 227 PHE A 234 1 8
HELIX 3 AA3 SER A 236 SER A 249 1 14
HELIX 4 AA4 SER A 259 PHE A 286 1 28
HELIX 5 AA5 THR A 292 ASN A 313 1 22
HELIX 6 AA6 PHE A 314 THR A 316 5 3
HELIX 7 AA7 ASP A 329 TRP A 341 1 13
HELIX 8 AA8 TRP A 341 ILE A 350 1 10
HELIX 9 AA9 PRO A 351 ASP A 364 1 14
HELIX 10 AB1 ALA A 371 SER A 384 1 14
HELIX 11 AB2 LEU A 385 LEU A 389 5 5
HELIX 12 AB3 ARG A 390 ASP A 410 1 21
HELIX 13 AB4 ALA A 412 GLN A 443 1 32
HELIX 14 AB5 CYS A 449 ASN A 454 1 6
HELIX 15 AB6 SER A 460 HIS A 475 1 16
HELIX 16 AB7 GLY A 488 GLN A 518 1 31
HELIX 17 AB8 ASP A 521 HIS A 541 1 21
HELIX 18 AB9 PRO A 544 TYR A 559 1 16
HELIX 19 AC1 ASP A 565 LEU A 573 1 9
HELIX 20 AC2 SER A 574 ALA A 591 1 18
HELIX 21 AC3 ASP A 600 LEU A 608 1 9
HELIX 22 AC4 THR A 609 LEU A 611 5 3
HELIX 23 AC5 GLU A 660 ARG A 666 1 7
HELIX 24 AC6 VAL A 686 TYR A 696 1 11
HELIX 25 AC7 TYR A 696 LEU A 708 1 13
HELIX 26 AC8 ARG B 216 LEU B 222 1 7
HELIX 27 AC9 ASN B 227 PHE B 234 1 8
HELIX 28 AD1 SER B 236 SER B 249 1 14
HELIX 29 AD2 SER B 259 PHE B 286 1 28
HELIX 30 AD3 THR B 292 ASN B 313 1 22
HELIX 31 AD4 PHE B 314 THR B 316 5 3
HELIX 32 AD5 ASP B 329 TRP B 341 1 13
HELIX 33 AD6 TRP B 341 ILE B 350 1 10
HELIX 34 AD7 PRO B 351 ASP B 364 1 14
HELIX 35 AD8 ALA B 371 SER B 384 1 14
HELIX 36 AD9 LEU B 385 LEU B 389 5 5
HELIX 37 AE1 ARG B 390 ASP B 410 1 21
HELIX 38 AE2 ALA B 412 GLN B 443 1 32
HELIX 39 AE3 CYS B 449 ASN B 454 1 6
HELIX 40 AE4 SER B 460 HIS B 475 1 16
HELIX 41 AE5 GLY B 488 GLN B 518 1 31
HELIX 42 AE6 ASP B 521 HIS B 541 1 21
HELIX 43 AE7 PRO B 544 TYR B 559 1 16
HELIX 44 AE8 ASP B 565 LEU B 573 1 9
HELIX 45 AE9 SER B 574 ALA B 591 1 18
HELIX 46 AF1 ASP B 600 LEU B 608 1 9
HELIX 47 AF2 THR B 609 LEU B 611 5 3
HELIX 48 AF3 GLU B 660 ARG B 666 1 7
HELIX 49 AF4 VAL B 686 TYR B 696 1 11
HELIX 50 AF5 TYR B 696 LEU B 708 1 13
HELIX 51 AF6 ARG C 216 LEU C 222 1 7
HELIX 52 AF7 ASN C 227 PHE C 234 1 8
HELIX 53 AF8 SER C 236 SER C 249 1 14
HELIX 54 AF9 SER C 259 PHE C 286 1 28
HELIX 55 AG1 THR C 292 ASN C 313 1 22
HELIX 56 AG2 PHE C 314 THR C 316 5 3
HELIX 57 AG3 ASP C 329 TRP C 341 1 13
HELIX 58 AG4 TRP C 341 ILE C 350 1 10
HELIX 59 AG5 PRO C 351 ASP C 364 1 14
HELIX 60 AG6 ALA C 371 SER C 384 1 14
HELIX 61 AG7 LEU C 385 LEU C 389 5 5
HELIX 62 AG8 ARG C 390 ASP C 410 1 21
HELIX 63 AG9 ALA C 412 GLN C 443 1 32
HELIX 64 AH1 CYS C 449 ASN C 454 1 6
HELIX 65 AH2 SER C 460 HIS C 475 1 16
HELIX 66 AH3 GLY C 488 GLN C 518 1 31
HELIX 67 AH4 ASP C 521 HIS C 541 1 21
HELIX 68 AH5 PRO C 544 TYR C 559 1 16
HELIX 69 AH6 ASP C 565 LEU C 573 1 9
HELIX 70 AH7 SER C 574 ALA C 591 1 18
HELIX 71 AH8 ASP C 600 LEU C 608 1 9
HELIX 72 AH9 THR C 609 LEU C 611 5 3
HELIX 73 AI1 GLU C 660 ARG C 666 1 7
HELIX 74 AI2 VAL C 686 TYR C 696 1 11
HELIX 75 AI3 TYR C 696 LEU C 708 1 13
HELIX 76 AI4 ARG D 216 LEU D 222 1 7
HELIX 77 AI5 ASN D 227 PHE D 234 1 8
HELIX 78 AI6 SER D 236 SER D 249 1 14
HELIX 79 AI7 SER D 259 PHE D 286 1 28
HELIX 80 AI8 THR D 292 ASN D 313 1 22
HELIX 81 AI9 PHE D 314 THR D 316 5 3
HELIX 82 AJ1 ASP D 329 TRP D 341 1 13
HELIX 83 AJ2 TRP D 341 ILE D 350 1 10
HELIX 84 AJ3 PRO D 351 ASP D 364 1 14
HELIX 85 AJ4 ALA D 371 SER D 384 1 14
HELIX 86 AJ5 LEU D 385 LEU D 389 5 5
HELIX 87 AJ6 ARG D 390 ASP D 410 1 21
HELIX 88 AJ7 ALA D 412 GLN D 443 1 32
HELIX 89 AJ8 CYS D 449 ASN D 454 1 6
HELIX 90 AJ9 SER D 460 HIS D 475 1 16
HELIX 91 AK1 GLY D 488 GLN D 518 1 31
HELIX 92 AK2 ASP D 521 HIS D 541 1 21
HELIX 93 AK3 PRO D 544 TYR D 559 1 16
HELIX 94 AK4 ASP D 565 LEU D 573 1 9
HELIX 95 AK5 SER D 574 ALA D 591 1 18
HELIX 96 AK6 ASP D 600 LEU D 608 1 9
HELIX 97 AK7 THR D 609 LEU D 611 5 3
HELIX 98 AK8 GLU D 660 ARG D 666 1 7
HELIX 99 AK9 VAL D 686 TYR D 696 1 11
HELIX 100 AL1 TYR D 696 LEU D 708 1 13
SHEET 1 AA1 4 ARG A 612 PHE A 616 0
SHEET 2 AA1 4 CYS A 679 SER A 685 -1 O LEU A 681 N GLU A 614
SHEET 3 AA1 4 LYS A 631 HIS A 637 -1 N PHE A 634 O TYR A 682
SHEET 4 AA1 4 TYR A 657 PHE A 658 -1 O PHE A 658 N TYR A 633
SHEET 1 AA2 4 TYR A 621 ILE A 623 0
SHEET 2 AA2 4 SER A 672 ALA A 675 -1 O VAL A 673 N ILE A 623
SHEET 3 AA2 4 VAL A 640 THR A 644 -1 N SER A 641 O ARG A 674
SHEET 4 AA2 4 LYS A 648 LEU A 652 -1 O LEU A 652 N VAL A 640
SHEET 1 AA3 4 ARG B 612 PHE B 616 0
SHEET 2 AA3 4 CYS B 679 SER B 685 -1 O LEU B 681 N GLU B 614
SHEET 3 AA3 4 LYS B 631 HIS B 637 -1 N PHE B 634 O TYR B 682
SHEET 4 AA3 4 TYR B 657 PHE B 658 -1 O PHE B 658 N TYR B 633
SHEET 1 AA4 4 TYR B 621 ILE B 623 0
SHEET 2 AA4 4 SER B 672 ALA B 675 -1 O VAL B 673 N ILE B 623
SHEET 3 AA4 4 VAL B 640 THR B 644 -1 N SER B 641 O ARG B 674
SHEET 4 AA4 4 LYS B 648 LEU B 652 -1 O LEU B 652 N VAL B 640
SHEET 1 AA5 4 ARG C 612 PHE C 616 0
SHEET 2 AA5 4 CYS C 679 SER C 685 -1 O LEU C 681 N GLU C 614
SHEET 3 AA5 4 LYS C 631 HIS C 637 -1 N PHE C 634 O TYR C 682
SHEET 4 AA5 4 TYR C 657 PHE C 658 -1 O PHE C 658 N TYR C 633
SHEET 1 AA6 4 TYR C 621 ILE C 623 0
SHEET 2 AA6 4 SER C 672 ALA C 675 -1 O VAL C 673 N ILE C 623
SHEET 3 AA6 4 VAL C 640 THR C 644 -1 N SER C 641 O ARG C 674
SHEET 4 AA6 4 LYS C 648 LEU C 652 -1 O LEU C 652 N VAL C 640
SHEET 1 AA7 4 ARG D 612 PHE D 616 0
SHEET 2 AA7 4 CYS D 679 SER D 685 -1 O LEU D 681 N GLU D 614
SHEET 3 AA7 4 LYS D 631 HIS D 637 -1 N PHE D 634 O TYR D 682
SHEET 4 AA7 4 TYR D 657 PHE D 658 -1 O PHE D 658 N TYR D 633
SHEET 1 AA8 4 TYR D 621 ILE D 623 0
SHEET 2 AA8 4 SER D 672 ALA D 675 -1 O VAL D 673 N ILE D 623
SHEET 3 AA8 4 VAL D 640 THR D 644 -1 N SER D 641 O ARG D 674
SHEET 4 AA8 4 LYS D 648 LEU D 652 -1 O LEU D 652 N VAL D 640
CISPEP 1 GLY A 480 TYR A 481 0 -21.88
CISPEP 2 GLY B 480 TYR B 481 0 -21.82
CISPEP 3 GLY C 480 TYR C 481 0 -21.79
CISPEP 4 GLY D 480 TYR D 481 0 -21.80
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END