HEADER MEMBRANE PROTEIN 07-SEP-18 6MET
TITLE STRUCTURAL BASIS OF CORECEPTOR RECOGNITION BY HIV-1 ENVELOPE SPIKE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160;
COMPND 3 CHAIN: G;
COMPND 4 FRAGMENT: GP120 DOMAIN RESIDUES 29-489;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND 8 CHAIN: A;
COMPND 9 FRAGMENT: IG-LIKE V-TYPE 1 AND IG-LIKE C2-TYPE 1,2,3 DOMAINS,
COMPND 10 RESIDUES 26-388;
COMPND 11 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: C-C CHEMOKINE RECEPTOR TYPE 5;
COMPND 15 CHAIN: B;
COMPND 16 FRAGMENT: RESIDUES 1-313;
COMPND 17 SYNONYM: CCR5,CHEMR13,HIV-1 FUSION CORECEPTOR;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: ENV;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: 293T;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CD4;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: 293T;
SOURCE 18 MOL_ID: 3;
SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 20 ORGANISM_COMMON: HUMAN;
SOURCE 21 ORGANISM_TAXID: 9606;
SOURCE 22 GENE: CCR5, CMKBR5;
SOURCE 23 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 24 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: 293T
KEYWDS HIV CORECEPTOR, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.M.SHAIK,B.CHEN
REVDAT 5 29-JUL-20 6MET 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 18-DEC-19 6MET 1 REMARK
REVDAT 3 16-JAN-19 6MET 1 JRNL
REVDAT 2 26-DEC-18 6MET 1 JRNL
REVDAT 1 12-DEC-18 6MET 0
JRNL AUTH M.M.SHAIK,H.PENG,J.LU,S.RITS-VOLLOCH,C.XU,M.LIAO,B.CHEN
JRNL TITL STRUCTURAL BASIS OF CORECEPTOR RECOGNITION BY HIV-1 ENVELOPE
JRNL TITL 2 SPIKE.
JRNL REF NATURE V. 565 318 2018
JRNL REFN ISSN 0028-0836
JRNL PMID 30542158
JRNL DOI 10.1038/S41586-018-0804-9
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SERIALEM, CTFFIND, UCSF CHIMERA,
REMARK 3 PHENIX, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 5UIW
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : 200.000
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
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) : 4.500
REMARK 3 NUMBER OF PARTICLES : 307346
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 6MET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000236770.
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 : C-C CHEMOKINE RECEPTOR TYPE 5
REMARK 245 (CCR5) IN COMPLEX WITH T-CELL
REMARK 245 SURFACE GLYCOPROTEIN CD4 AND
REMARK 245 HIV1 ENVELOPE GLYCOPROTEIN
REMARK 245 GP120; ENVELOPE GLYCOPROTEIN
REMARK 245 GP160; T-CELL SURFACE
REMARK 245 GLYCOPROTEIN CD4; C-C CHEMOKINE
REMARK 245 RECEPTOR TYPE 5
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
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) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : OTHER
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 46.00
REMARK 245 ILLUMINATION MODE : OTHER
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, A, B, C, D, E, F, H, I, J,
REMARK 350 AND CHAINS: K, L
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 ASP G 132
REMARK 465 LEU G 133
REMARK 465 ASN G 134
REMARK 465 ASN G 135
REMARK 465 SER G 136
REMARK 465 THR G 137
REMARK 465 ASN G 138
REMARK 465 ASN G 139
REMARK 465 ASN G 140
REMARK 465 ASN G 141
REMARK 465 SER G 142
REMARK 465 SER G 143
REMARK 465 GLY G 144
REMARK 465 VAL G 145
REMARK 465 LYS G 146
REMARK 465 THR G 147
REMARK 465 GLY G 148
REMARK 465 ILE G 149
REMARK 465 ASP G 150
REMARK 465 LYS G 151
REMARK 465 GLY G 152
REMARK 465 GLU G 153
REMARK 465 ILE G 154
REMARK 465 LYS G 155
REMARK 465 ASN G 156
REMARK 465 CYS G 157
REMARK 465 SER G 158
REMARK 465 PHE G 159
REMARK 465 ASN G 160
REMARK 465 THR G 161
REMARK 465 THR G 162
REMARK 465 THR G 163
REMARK 465 SER G 164
REMARK 465 VAL G 165
REMARK 465 LYS G 166
REMARK 465 ASP G 167
REMARK 465 LYS G 168
REMARK 465 GLU G 169
REMARK 465 LYS G 170
REMARK 465 LYS G 171
REMARK 465 GLU G 172
REMARK 465 TYR G 173
REMARK 465 ALA G 174
REMARK 465 LEU G 175
REMARK 465 PHE G 176
REMARK 465 TYR G 177
REMARK 465 ASN G 178
REMARK 465 LEU G 179
REMARK 465 ASP G 180
REMARK 465 VAL G 181
REMARK 465 VAL G 182
REMARK 465 GLN G 183
REMARK 465 ILE G 184
REMARK 465 GLY G 185
REMARK 465 ASN G 186
REMARK 465 GLY G 399
REMARK 465 THR G 400
REMARK 465 SER G 401
REMARK 465 ASN G 402
REMARK 465 THR G 403
REMARK 465 THR G 404
REMARK 465 GLY G 405
REMARK 465 ASN G 406
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 ILE G 131 CG1 CG2 CD1
REMARK 470 ASP G 187 CG OD1 OD2
REMARK 470 ASN G 188 CG OD1 ND2
REMARK 470 THR G 189 OG1 CG2
REMARK 470 SER G 190 OG
REMARK 470 TYR G 191 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG G 192 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 189 CG CD CE NZ
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 325 CG CD CE NZ
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 C8 NAG K 2 O7 NAG G 631 1.76
REMARK 500 OG SER B 7 C1 A2G B 401 1.81
REMARK 500 ND2 ASN G 384 C1 NAG K 1 1.92
REMARK 500 CG2 THR G 209 O4 MAN E 4 1.98
REMARK 500 NE2 HIS A 107 O GLU A 277 2.18
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 CYS G 73 161.73 178.70
REMARK 500 VAL G 126 -73.91 -116.56
REMARK 500 THR G 127 118.03 -173.10
REMARK 500 PHE G 233 -9.87 68.69
REMARK 500 ASN G 234 -8.89 62.38
REMARK 500 THR G 236 32.02 -94.88
REMARK 500 GLN G 258 -11.89 70.38
REMARK 500 LEU G 261 -156.52 -80.98
REMARK 500 ASN G 262 126.28 -34.80
REMARK 500 THR G 278 18.15 59.74
REMARK 500 ASN G 280 44.10 33.04
REMARK 500 ALA G 281 -36.65 -130.18
REMARK 500 HIS G 308 56.86 -91.07
REMARK 500 ALA G 317 160.33 -48.46
REMARK 500 GLU G 353 61.94 62.37
REMARK 500 ASN G 354 62.34 62.84
REMARK 500 GLN G 387 44.86 -86.79
REMARK 500 LEU G 388 -18.29 -141.80
REMARK 500 GLU G 424 161.14 88.02
REMARK 500 TYR G 430 -169.20 -105.56
REMARK 500 LEU G 479 34.35 -97.26
REMARK 500 ILE A 36 -54.61 -121.71
REMARK 500 GLU A 150 -169.89 -124.82
REMARK 500 LYS A 206 -159.67 -77.96
REMARK 500 LEU A 207 109.99 -55.15
REMARK 500 THR A 208 -33.63 -134.25
REMARK 500 ARG A 219 -0.03 66.32
REMARK 500 ASN A 233 -170.16 71.68
REMARK 500 GLU A 235 141.30 145.77
REMARK 500 LYS A 239 -72.30 -65.89
REMARK 500 ARG A 240 127.91 -177.38
REMARK 500 GLN A 243 179.20 157.46
REMARK 500 PRO A 254 85.90 -69.49
REMARK 500 ALA A 278 -22.82 98.42
REMARK 500 GLN A 298 -156.72 -137.96
REMARK 500 GLU A 320 -3.03 63.67
REMARK 500 ASN A 337 73.04 52.22
REMARK 500 ASP A 349 87.85 -150.59
REMARK 500 ARG B 60 10.35 90.76
REMARK 500 LEU B 61 40.81 37.39
REMARK 500 LYS B 62 4.19 -66.81
REMARK 500 ALA B 92 -81.06 -126.36
REMARK 500 GLN B 93 -156.61 -160.92
REMARK 500 ASN B 98 -26.43 -145.13
REMARK 500 CYS B 178 78.49 -107.09
REMARK 500 HIS B 181 79.62 -104.77
REMARK 500 LEU B 203 -50.58 -121.54
REMARK 500 GLU B 262 -159.96 -85.51
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 NAG K 1
REMARK 610 A2G B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-9109 RELATED DB: EMDB
REMARK 900 STRUCTURAL BASIS OF CORECEPTOR RECOGNITION BY HIV-1 ENVELOPE SPIKE
DBREF 6MET G 31 491 UNP Q70145 Q70145_9HIV1 29 489
DBREF 6MET A 1 363 UNP P01730 CD4_HUMAN 26 388
DBREF 6MET B 1 313 UNP P51681 CCR5_HUMAN 1 313
SEQRES 1 G 461 ASP ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL
SEQRES 2 G 461 TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER ASP
SEQRES 3 G 461 ALA LYS ALA TYR LYS ALA GLU VAL HIS ASN VAL TRP ALA
SEQRES 4 G 461 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU
SEQRES 5 G 461 ILE VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP
SEQRES 6 G 461 LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE
SEQRES 7 G 461 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU
SEQRES 8 G 461 THR PRO LEU CYS VAL THR LEU ASN CYS ILE ASP LEU ASN
SEQRES 9 G 461 ASN SER THR ASN ASN ASN ASN SER SER GLY VAL LYS THR
SEQRES 10 G 461 GLY ILE ASP LYS GLY GLU ILE LYS ASN CYS SER PHE ASN
SEQRES 11 G 461 THR THR THR SER VAL LYS ASP LYS GLU LYS LYS GLU TYR
SEQRES 12 G 461 ALA LEU PHE TYR ASN LEU ASP VAL VAL GLN ILE GLY ASN
SEQRES 13 G 461 ASP ASN THR SER TYR ARG LEU THR SER CYS ASN THR SER
SEQRES 14 G 461 VAL ILE THR GLN ALA CYS PRO LYS VAL THR PHE GLU PRO
SEQRES 15 G 461 ILE PRO ILE HIS TYR CYS THR PRO ALA GLY TYR ALA ILE
SEQRES 16 G 461 LEU LYS CYS ASN GLY LYS LYS PHE ASN GLY THR GLY PRO
SEQRES 17 G 461 CYS THR ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE
SEQRES 18 G 461 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER
SEQRES 19 G 461 LEU ALA GLU GLU ASP ILE VAL ILE ARG SER GLU ASN LEU
SEQRES 20 G 461 THR ASN ASN ALA LYS THR ILE ILE VAL GLN LEU LYS ASP
SEQRES 21 G 461 PRO VAL ASP ILE ASN CYS THR ARG PRO ASN ASN ASN THR
SEQRES 22 G 461 ARG LYS SER ILE HIS ILE GLY PRO GLY ARG ALA PHE TYR
SEQRES 23 G 461 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS
SEQRES 24 G 461 CYS ASN LEU SER ARG ALA GLN TRP ASN ASP THR LEU SER
SEQRES 25 G 461 LYS ILE VAL THR LYS LEU ARG GLU GLN PHE GLU ASN LYS
SEQRES 26 G 461 THR ILE LYS PHE GLN PRO PRO SER GLY GLY ASP PRO GLU
SEQRES 27 G 461 ILE VAL PHE HIS SER PHE ASN CYS GLY GLY GLU PHE PHE
SEQRES 28 G 461 TYR CYS ASN THR THR GLN LEU PHE ASN SER THR TRP THR
SEQRES 29 G 461 ASN ASN THR GLU GLY THR SER ASN THR THR GLY ASN ASP
SEQRES 30 G 461 THR ILE THR LEU PRO CYS ARG ILE LYS GLN ILE VAL ASN
SEQRES 31 G 461 MET TRP GLN GLU VAL GLY LYS ALA MET TYR ALA PRO PRO
SEQRES 32 G 461 ILE LYS GLY LYS ILE LYS CYS SER SER ASN ILE THR GLY
SEQRES 33 G 461 LEU LEU LEU THR ARG ASP GLY GLY ASN ASN GLU MET ASN
SEQRES 34 G 461 THR THR GLU ILE PHE ARG PRO GLY GLY GLY ASP MET ARG
SEQRES 35 G 461 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL
SEQRES 36 G 461 ARG ILE GLU PRO LEU GLY
SEQRES 1 A 363 LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU
SEQRES 2 A 363 LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE
SEQRES 3 A 363 HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN
SEQRES 4 A 363 GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN
SEQRES 5 A 363 ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY
SEQRES 6 A 363 ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP
SEQRES 7 A 363 SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU
SEQRES 8 A 363 GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER
SEQRES 9 A 363 ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR
SEQRES 10 A 363 LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS
SEQRES 11 A 363 ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR
SEQRES 12 A 363 LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR
SEQRES 13 A 363 TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU
SEQRES 14 A 363 PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS ALA
SEQRES 15 A 363 SER SER ILE VAL TYR LYS LYS GLU GLY GLU GLN VAL GLU
SEQRES 16 A 363 PHE SER PHE PRO LEU ALA PHE THR VAL GLU LYS LEU THR
SEQRES 17 A 363 GLY SER GLY GLU LEU TRP TRP GLN ALA GLU ARG ALA SER
SEQRES 18 A 363 SER SER LYS SER TRP ILE THR PHE ASP LEU LYS ASN LYS
SEQRES 19 A 363 GLU VAL SER VAL LYS ARG VAL THR GLN ASP PRO LYS LEU
SEQRES 20 A 363 GLN MET GLY LYS LYS LEU PRO LEU HIS LEU THR LEU PRO
SEQRES 21 A 363 GLN ALA LEU PRO GLN TYR ALA GLY SER GLY ASN LEU THR
SEQRES 22 A 363 LEU ALA LEU GLU ALA LYS THR GLY LYS LEU HIS GLN GLU
SEQRES 23 A 363 VAL ASN LEU VAL VAL MET ARG ALA THR GLN LEU GLN LYS
SEQRES 24 A 363 ASN LEU THR CYS GLU VAL TRP GLY PRO THR SER PRO LYS
SEQRES 25 A 363 LEU MET LEU SER LEU LYS LEU GLU ASN LYS GLU ALA LYS
SEQRES 26 A 363 VAL SER LYS ARG GLU LYS ALA VAL TRP VAL LEU ASN PRO
SEQRES 27 A 363 GLU ALA GLY MET TRP GLN CYS LEU LEU SER ASP SER GLY
SEQRES 28 A 363 GLN VAL LEU LEU GLU SER ASN ILE LYS VAL LEU PRO
SEQRES 1 B 313 MET ASP TYR GLN VAL SER SER PRO ILE TYS ASP ILE ASN
SEQRES 2 B 313 TYS TYR THR SER GLU PRO CYS GLN LYS ILE ASN VAL LYS
SEQRES 3 B 313 GLN ILE ALA ALA ARG LEU LEU PRO PRO LEU TYR SER LEU
SEQRES 4 B 313 VAL PHE ILE PHE GLY PHE VAL GLY ASN MET LEU VAL ILE
SEQRES 5 B 313 LEU ILE LEU ILE ASN CYS LYS ARG LEU LYS SER MET THR
SEQRES 6 B 313 ASP ILE TYR LEU LEU ASN LEU ALA ILE SER ASP LEU PHE
SEQRES 7 B 313 PHE LEU LEU THR VAL PRO PHE TRP ALA HIS TYR ALA ALA
SEQRES 8 B 313 ALA GLN TRP ASP PHE GLY ASN THR MET CYS GLN LEU LEU
SEQRES 9 B 313 THR GLY LEU TYR PHE ILE GLY PHE PHE SER GLY ILE PHE
SEQRES 10 B 313 PHE ILE ILE LEU LEU THR ILE ASP ARG TYR LEU ALA VAL
SEQRES 11 B 313 VAL HIS ALA VAL PHE ALA LEU LYS ALA ARG THR VAL THR
SEQRES 12 B 313 PHE GLY VAL VAL THR SER VAL ILE THR TRP VAL VAL ALA
SEQRES 13 B 313 VAL PHE ALA SER LEU PRO GLY ILE ILE PHE THR ARG SER
SEQRES 14 B 313 GLN LYS GLU GLY LEU HIS TYR THR CYS SER SER HIS PHE
SEQRES 15 B 313 PRO TYR SER GLN TYR GLN PHE TRP LYS ASN PHE GLN THR
SEQRES 16 B 313 LEU LYS ILE VAL ILE LEU GLY LEU VAL LEU PRO LEU LEU
SEQRES 17 B 313 VAL MET VAL ILE CYS TYR SER GLY ILE LEU LYS THR LEU
SEQRES 18 B 313 LEU ARG CYS ARG ASN GLU LYS LYS ARG HIS ARG ALA VAL
SEQRES 19 B 313 ARG LEU ILE PHE THR ILE MET ILE VAL TYR PHE LEU PHE
SEQRES 20 B 313 TRP ALA PRO TYR ASN ILE VAL LEU LEU LEU ASN THR PHE
SEQRES 21 B 313 GLN GLU PHE PHE GLY LEU ASN ASN CYS SER SER SER ASN
SEQRES 22 B 313 ARG LEU ASP GLN ALA MET GLN VAL THR GLU THR LEU GLY
SEQRES 23 B 313 MET THR HIS CYS CYS ILE ASN PRO ILE ILE TYR ALA PHE
SEQRES 24 B 313 VAL GLY GLU LYS PHE ARG ASN TYR LEU LEU VAL PHE PHE
SEQRES 25 B 313 GLN
MODRES 6MET TYS B 10 TYR MODIFIED RESIDUE
MODRES 6MET TYS B 14 TYR MODIFIED RESIDUE
HET TYS B 10 16
HET TYS B 14 16
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET MAN E 6 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG G 601 14
HET NAG G 619 14
HET NAG G 620 14
HET NAG G 626 14
HET NAG G 627 14
HET NAG G 628 14
HET NAG G 631 14
HET A2G B 401 14
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE
FORMUL 3 TYS 2(C9 H11 N O6 S)
FORMUL 4 NAG 25(C8 H15 N O6)
FORMUL 5 BMA 3(C6 H12 O6)
FORMUL 6 MAN 3(C6 H12 O6)
FORMUL 20 A2G C8 H15 N O6
HELIX 1 AA1 GLU G 63 ALA G 72 1 10
HELIX 2 AA2 MET G 99 LEU G 115 1 17
HELIX 3 AA3 ARG G 334 GLU G 353 1 20
HELIX 4 AA4 ASP G 366 PHE G 371 1 6
HELIX 5 AA5 THR G 385 PHE G 389 5 5
HELIX 6 AA6 ASP G 470 SER G 477 1 8
HELIX 7 AA7 ARG A 58 GLN A 64 5 7
HELIX 8 AA8 GLU A 150 SER A 154 5 5
HELIX 9 AA9 LEU A 263 TYR A 266 5 4
HELIX 10 AB1 LYS B 26 ARG B 31 1 6
HELIX 11 AB2 LEU B 32 CYS B 58 1 27
HELIX 12 AB3 SER B 63 LEU B 81 1 19
HELIX 13 AB4 THR B 82 ALA B 91 1 10
HELIX 14 AB5 MET B 100 VAL B 131 1 32
HELIX 15 AB6 HIS B 132 ARG B 140 1 9
HELIX 16 AB7 THR B 141 ALA B 159 1 19
HELIX 17 AB8 SER B 160 ILE B 165 5 6
HELIX 18 AB9 GLN B 186 LEU B 203 1 18
HELIX 19 AC1 LEU B 203 CYS B 224 1 22
HELIX 20 AC2 GLU B 227 PHE B 260 1 34
HELIX 21 AC3 ASN B 268 THR B 288 1 21
HELIX 22 AC4 CYS B 291 VAL B 300 1 10
HELIX 23 AC5 ARG B 305 GLN B 313 1 9
SHEET 1 AA1 5 LYS G 45 GLU G 46 0
SHEET 2 AA1 5 TYR G 482 ARG G 486 -1 O ARG G 486 N LYS G 45
SHEET 3 AA1 5 TYR G 223 CYS G 228 -1 N ALA G 224 O VAL G 485
SHEET 4 AA1 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227
SHEET 5 AA1 5 ILE G 83 VAL G 84 -1 N ILE G 83 O THR G 244
SHEET 1 AA2 2 PHE G 52 SER G 55 0
SHEET 2 AA2 2 ILE G 215 CYS G 218 -1 O CYS G 218 N PHE G 52
SHEET 1 AA3 4 CYS G 196 THR G 202 0
SHEET 2 AA3 4 VAL G 119 CYS G 125 -1 N LEU G 124 O ASN G 197
SHEET 3 AA3 4 LYS G 427 MET G 429 -1 O MET G 429 N VAL G 119
SHEET 4 AA3 4 VAL G 419 ASN G 420 -1 N VAL G 419 O ALA G 428
SHEET 1 AA4 3 VAL G 271 ARG G 273 0
SHEET 2 AA4 3 ILE G 284 GLN G 287 -1 O ILE G 285 N ARG G 273
SHEET 3 AA4 3 GLY G 446 LEU G 449 -1 O LEU G 449 N ILE G 284
SHEET 1 AA5 4 THR G 408 ARG G 414 0
SHEET 2 AA5 4 GLN G 327 SER G 333 -1 N CYS G 330 O LEU G 411
SHEET 3 AA5 4 ILE G 294 THR G 297 -1 N THR G 297 O HIS G 329
SHEET 4 AA5 4 LYS G 439 SER G 442 -1 O CYS G 440 N CYS G 296
SHEET 1 AA6 2 ILE G 357 PHE G 359 0
SHEET 2 AA6 2 GLU G 462 PHE G 464 1 O GLU G 462 N LYS G 358
SHEET 1 AA7 2 HIS G 372 CYS G 376 0
SHEET 2 AA7 2 GLU G 379 CYS G 383 -1 O CYS G 383 N HIS G 372
SHEET 1 AA8 2 LEU A 5 GLY A 6 0
SHEET 2 AA8 2 LEU A 96 VAL A 97 1 O LEU A 96 N GLY A 6
SHEET 1 AA9 3 VAL A 12 GLU A 13 0
SHEET 2 AA9 3 ILE A 70 ILE A 71 -1 O ILE A 71 N VAL A 12
SHEET 3 AA9 3 ALA A 55 ASP A 56 -1 N ASP A 56 O ILE A 70
SHEET 1 AB1 4 PHE A 43 LEU A 44 0
SHEET 2 AB1 4 LYS A 35 GLN A 40 -1 N GLN A 40 O PHE A 43
SHEET 3 AB1 4 HIS A 27 ASN A 30 -1 N TRP A 28 O ILE A 36
SHEET 4 AB1 4 TYR A 82 CYS A 84 -1 O ILE A 83 N LYS A 29
SHEET 1 AB2 2 GLY A 99 THR A 101 0
SHEET 2 AB2 2 THR A 117 GLU A 119 -1 O GLU A 119 N GLY A 99
SHEET 1 AB3 2 LEU A 108 LEU A 109 0
SHEET 2 AB3 2 VAL A 176 LEU A 177 1 O LEU A 177 N LEU A 108
SHEET 1 AB4 2 LEU A 114 THR A 115 0
SHEET 2 AB4 2 SER A 145 VAL A 146 -1 O VAL A 146 N LEU A 114
SHEET 1 AB5 2 VAL A 128 ARG A 131 0
SHEET 2 AB5 2 THR A 158 VAL A 161 -1 O THR A 160 N GLN A 129
SHEET 1 AB6 6 SER A 183 LYS A 189 0
SHEET 2 AB6 6 GLY A 281 ALA A 294 1 O VAL A 290 N VAL A 186
SHEET 3 AB6 6 GLY A 268 LEU A 276 -1 N LEU A 272 O GLN A 285
SHEET 4 AB6 6 GLY A 209 ALA A 217 -1 N GLN A 216 O SER A 269
SHEET 5 AB6 6 THR A 228 LEU A 231 -1 O PHE A 229 N GLY A 211
SHEET 6 AB6 6 SER A 237 VAL A 238 -1 O SER A 237 N ASP A 230
SHEET 1 AB7 4 SER A 183 LYS A 189 0
SHEET 2 AB7 4 GLY A 281 ALA A 294 1 O VAL A 290 N VAL A 186
SHEET 3 AB7 4 LEU A 301 TRP A 306 -1 O TRP A 306 N VAL A 291
SHEET 4 AB7 4 ALA A 332 VAL A 335 -1 O VAL A 333 N CYS A 303
SHEET 1 AB8 3 VAL A 194 PHE A 198 0
SHEET 2 AB8 3 LEU A 255 LEU A 259 -1 O LEU A 259 N VAL A 194
SHEET 3 AB8 3 GLN A 248 MET A 249 -1 N GLN A 248 O THR A 258
SHEET 1 AB9 4 ALA A 324 LYS A 328 0
SHEET 2 AB9 4 MET A 314 LYS A 318 -1 N LEU A 315 O LYS A 328
SHEET 3 AB9 4 GLY A 341 SER A 348 -1 O GLN A 344 N LYS A 318
SHEET 4 AB9 4 VAL A 353 VAL A 361 -1 O LEU A 354 N LEU A 347
SSBOND 1 CYS G 53 CYS G 73 1555 1555 2.03
SSBOND 2 CYS G 118 CYS G 205 1555 1555 2.03
SSBOND 3 CYS G 125 CYS G 196 1555 1555 2.03
SSBOND 4 CYS G 218 CYS G 247 1555 1555 2.03
SSBOND 5 CYS G 228 CYS G 239 1555 1555 2.04
SSBOND 6 CYS G 296 CYS G 330 1555 1555 2.03
SSBOND 7 CYS G 376 CYS G 440 1555 1555 2.03
SSBOND 8 CYS G 383 CYS G 413 1555 1555 2.03
SSBOND 9 CYS A 16 CYS A 84 1555 1555 2.04
SSBOND 10 CYS A 130 CYS A 159 1555 1555 2.03
SSBOND 11 CYS B 20 CYS B 269 1555 1555 2.03
SSBOND 12 CYS B 101 CYS B 178 1555 1555 2.03
LINK ND2 ASN G 87 C1 NAG G 601 1555 1555 1.44
LINK ND2 ASN G 197 C1 NAG G 628 1555 1555 1.43
LINK ND2 ASN G 234 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN G 241 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN G 262 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN G 276 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN G 295 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN G 301 C1 NAG J 1 1555 1555 1.46
LINK ND2 ASN G 331 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN G 338 C1 NAG G 619 1555 1555 1.44
LINK ND2 ASN G 354 C1 NAG G 620 1555 1555 1.45
LINK ND2 ASN G 390 C1 NAG G 631 1555 1555 1.44
LINK ND2 ASN G 395 C1 NAG G 626 1555 1555 1.45
LINK ND2 ASN G 443 C1 NAG L 1 1555 1555 1.46
LINK ND2 ASN G 459 C1 NAG G 627 1555 1555 1.44
LINK C ILE B 9 N TYS B 10 1555 1555 1.33
LINK C TYS B 10 N ASP B 11 1555 1555 1.33
LINK C ASN B 13 N TYS B 14 1555 1555 1.33
LINK C TYS B 14 N TYR B 15 1555 1555 1.33
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45
LINK O6 BMA E 3 C1 MAN E 6 1555 1555 1.44
LINK O2 MAN E 4 C1 MAN E 5 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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
