HEADER VIRAL PROTEIN/TRANSPORT PROTEIN 30-NOV-15 5F1B
TITLE STRUCTURAL BASIS OF EBOLA VIRUS ENTRY: VIRAL GLYCOPROTEIN BOUND TO ITS
TITLE 2 ENDOSOMAL RECEPTOR NIEMANN-PICK C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GP1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 32-188;
COMPND 5 SYNONYM: GP1,2,GP;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GP2;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 509-598;
COMPND 11 SYNONYM: GP1,2,GP;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: NIEMANN-PICK C1 PROTEIN;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: UNP RESIDUES 374-620;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZAIRE EBOLAVIRUS;
SOURCE 3 ORGANISM_COMMON: ZEBOV;
SOURCE 4 ORGANISM_TAXID: 128951;
SOURCE 5 STRAIN: KIKWIT-95;
SOURCE 6 GENE: GP;
SOURCE 7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC1;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: ZAIRE EBOLAVIRUS;
SOURCE 14 ORGANISM_COMMON: ZEBOV;
SOURCE 15 ORGANISM_TAXID: 128951;
SOURCE 16 STRAIN: KIKWIT-95;
SOURCE 17 GENE: GP;
SOURCE 18 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE CELLS;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_VECTOR: PFASTBAC1;
SOURCE 23 MOL_ID: 3;
SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 25 ORGANISM_COMMON: HUMAN;
SOURCE 26 ORGANISM_TAXID: 9606;
SOURCE 27 GENE: NPC1;
SOURCE 28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EBOLA VIRUS, GLYCOPROTEIN, NPC1-C, VIRAL PROTEIN-TRANSPORT PROTEIN
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WANG,Y.SHI,J.SONG,J.QI,G.LU,J.YAN,G.F.GAO
REVDAT 4 08-NOV-23 5F1B 1 HETSYN
REVDAT 3 29-JUL-20 5F1B 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 27-JAN-16 5F1B 1 JRNL
REVDAT 1 20-JAN-16 5F1B 0
JRNL AUTH H.WANG,Y.SHI,J.SONG,J.QI,G.LU,J.YAN,G.F.GAO
JRNL TITL EBOLA VIRAL GLYCOPROTEIN BOUND TO ITS ENDOSOMAL RECEPTOR
JRNL TITL 2 NIEMANN-PICK C1.
JRNL REF CELL V. 164 258 2016
JRNL REFN ISSN 1097-4172
JRNL PMID 26771495
JRNL DOI 10.1016/J.CELL.2015.12.044
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1369
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 41.8651 - 4.9509 1.00 2657 141 0.1748 0.2222
REMARK 3 2 4.9509 - 3.9306 1.00 2605 137 0.1467 0.1904
REMARK 3 3 3.9306 - 3.4340 1.00 2587 145 0.1713 0.1976
REMARK 3 4 3.4340 - 3.1202 1.00 2601 144 0.1971 0.2563
REMARK 3 5 3.1202 - 2.8966 1.00 2603 109 0.2022 0.2875
REMARK 3 6 2.8966 - 2.7259 1.00 2586 142 0.1978 0.2719
REMARK 3 7 2.7259 - 2.5894 1.00 2594 137 0.2071 0.2677
REMARK 3 8 2.5894 - 2.4767 1.00 2584 146 0.2061 0.2513
REMARK 3 9 2.4767 - 2.3813 1.00 2567 127 0.2130 0.2849
REMARK 3 10 2.3813 - 2.2992 1.00 2557 141 0.2343 0.2800
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.610
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 : 0.008 3761
REMARK 3 ANGLE : 1.152 5123
REMARK 3 CHIRALITY : 0.052 567
REMARK 3 PLANARITY : 0.006 667
REMARK 3 DIHEDRAL : 14.571 1333
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2833 -16.3893-320.9409
REMARK 3 T TENSOR
REMARK 3 T11: 0.2617 T22: 0.2557
REMARK 3 T33: 0.2749 T12: 0.0041
REMARK 3 T13: 0.0421 T23: 0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 0.3580 L22: 0.2324
REMARK 3 L33: 0.1052 L12: -0.1253
REMARK 3 L13: 0.2223 L23: -0.1891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: -0.0146 S13: 0.0127
REMARK 3 S21: -0.0221 S22: 0.0372 S23: 0.0583
REMARK 3 S31: 0.0118 S32: -0.0441 S33: -0.0000
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 5F1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215827.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27329
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.6000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3CSY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (V/V) PENTAERYTHRITOLPROPOXYLATE,
REMARK 280 0.2M SODIUM CHLORIDE, PH 5.5, 0.1M MES-NAOH, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
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,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.88850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 46.88850
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.88850
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 ASP B 522
REMARK 465 GLU B 523
REMARK 465 GLY B 524
REMARK 465 GLY B 599
REMARK 465 THR B 600
REMARK 465 CYS B 601
REMARK 465 HIS B 602
REMARK 465 ILE B 603
REMARK 465 LEU B 604
REMARK 465 GLY B 605
REMARK 465 PRO B 606
REMARK 465 ASP B 607
REMARK 465 CYS B 608
REMARK 465 CYS B 609
REMARK 465 ILE B 610
REMARK 465 GLU B 611
REMARK 465 PRO B 612
REMARK 465 HIS B 613
REMARK 465 ASP B 614
REMARK 465 TRP B 615
REMARK 465 THR B 616
REMARK 465 LYS B 617
REMARK 465 ASN B 618
REMARK 465 ILE B 619
REMARK 465 THR B 620
REMARK 465 ASP B 621
REMARK 465 LYS B 622
REMARK 465 ILE B 623
REMARK 465 ASP B 624
REMARK 465 GLN B 625
REMARK 465 ILE B 626
REMARK 465 ILE B 627
REMARK 465 HIS B 628
REMARK 465 ASP B 629
REMARK 465 PHE B 630
REMARK 465 VAL B 631
REMARK 465 ASP B 632
REMARK 465 HIS B 633
REMARK 465 HIS B 634
REMARK 465 HIS B 635
REMARK 465 HIS B 636
REMARK 465 HIS B 637
REMARK 465 HIS B 638
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 THR C 3
REMARK 465 ASN C 4
REMARK 465 PRO C 5
REMARK 465 VAL C 6
REMARK 465 ASP C 7
REMARK 465 LEU C 8
REMARK 465 TRP C 9
REMARK 465 SER C 10
REMARK 465 ALA C 11
REMARK 465 PRO C 12
REMARK 465 SER C 13
REMARK 465 SER C 14
REMARK 465 GLN C 15
REMARK 465 ALA C 16
REMARK 465 ARG C 17
REMARK 465 ALA C 233
REMARK 465 GLU C 234
REMARK 465 ARG C 235
REMARK 465 SER C 236
REMARK 465 ILE C 237
REMARK 465 GLU C 238
REMARK 465 ASP C 239
REMARK 465 GLU C 240
REMARK 465 LEU C 241
REMARK 465 ASN C 242
REMARK 465 ARG C 243
REMARK 465 GLU C 244
REMARK 465 SER C 245
REMARK 465 ASP C 246
REMARK 465 SER C 247
REMARK 465 ASP C 248
REMARK 465 LEU C 249
REMARK 465 GLU C 250
REMARK 465 HIS C 251
REMARK 465 HIS C 252
REMARK 465 HIS C 253
REMARK 465 HIS C 254
REMARK 465 HIS C 255
REMARK 465 HIS C 256
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 LYS A 50 CG CD CE NZ
REMARK 470 VAL A 52 CG1 CG2
REMARK 470 ARG A 54 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 TRP B 597 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 597 CZ3 CH2
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 NZ LYS B 510 O6 NAG D 1 1.86
REMARK 500 O HOH A 263 O HOH A 271 2.02
REMARK 500 O HOH A 267 O HOH A 275 2.03
REMARK 500 O HOH A 270 O HOH A 274 2.05
REMARK 500 O GLU B 564 O HOH B 801 2.08
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 O HOH A 251 O HOH B 815 3655 2.00
REMARK 500 ND2 ASN B 550 O HOH C 329 5555 2.07
REMARK 500 OH TYR A 137 ND2 ASN C 217 5555 2.19
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 HIS A 39 -97.70 -93.64
REMARK 500 SER A 41 19.33 -150.61
REMARK 500 VAL A 45 92.78 -67.49
REMARK 500 SER A 46 -152.69 -111.94
REMARK 500 ASP A 49 25.53 -76.37
REMARK 500 LYS A 50 -32.46 -173.40
REMARK 500 LEU A 51 95.82 -41.71
REMARK 500 VAL A 52 150.67 -47.42
REMARK 500 ALA A 148 42.60 -89.24
REMARK 500 TYR A 162 -155.50 -106.10
REMARK 500 LYS B 510 59.28 36.51
REMARK 500 ALA B 526 44.07 -98.41
REMARK 500 ASN B 550 49.24 28.74
REMARK 500 TRP B 597 -5.25 -174.14
REMARK 500 PHE C 27 -87.28 -96.02
REMARK 500 ASP C 86 -123.71 52.30
REMARK 500 TYR C 103 -57.14 1.35
REMARK 500 ASP C 129 -155.90 -137.56
REMARK 500 THR C 154 -2.95 65.79
REMARK 500 ASP C 180 -124.76 56.83
REMARK 500 ASN C 224 103.37 -160.89
REMARK 500 PHE C 231 -163.27 -111.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASN A 69 0.07 SIDE CHAIN
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 275 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 276 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH A 277 DISTANCE = 7.87 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F18 RELATED DB: PDB
DBREF 5F1B A 32 188 UNP P87666 VGP_EBOZ5 32 188
DBREF 5F1B B 509 632 UNP P87666 VGP_EBOZ5 509 632
DBREF 5F1B C 2 248 UNP O15118 NPC1_HUMAN 374 620
SEQADV 5F1B ARG A 31 UNP P87666 EXPRESSION TAG
SEQADV 5F1B VAL A 42 UNP P87666 THR 42 ENGINEERED MUTATION
SEQADV 5F1B HIS B 633 UNP P87666 EXPRESSION TAG
SEQADV 5F1B HIS B 634 UNP P87666 EXPRESSION TAG
SEQADV 5F1B HIS B 635 UNP P87666 EXPRESSION TAG
SEQADV 5F1B HIS B 636 UNP P87666 EXPRESSION TAG
SEQADV 5F1B HIS B 637 UNP P87666 EXPRESSION TAG
SEQADV 5F1B HIS B 638 UNP P87666 EXPRESSION TAG
SEQADV 5F1B MET C 1 UNP O15118 EXPRESSION TAG
SEQADV 5F1B LEU C 249 UNP O15118 EXPRESSION TAG
SEQADV 5F1B GLU C 250 UNP O15118 EXPRESSION TAG
SEQADV 5F1B HIS C 251 UNP O15118 EXPRESSION TAG
SEQADV 5F1B HIS C 252 UNP O15118 EXPRESSION TAG
SEQADV 5F1B HIS C 253 UNP O15118 EXPRESSION TAG
SEQADV 5F1B HIS C 254 UNP O15118 EXPRESSION TAG
SEQADV 5F1B HIS C 255 UNP O15118 EXPRESSION TAG
SEQADV 5F1B HIS C 256 UNP O15118 EXPRESSION TAG
SEQRES 1 A 158 ARG SER ILE PRO LEU GLY VAL ILE HIS ASN SER VAL LEU
SEQRES 2 A 158 GLN VAL SER ASP VAL ASP LYS LEU VAL CYS ARG ASP LYS
SEQRES 3 A 158 LEU SER SER THR ASN GLN LEU ARG SER VAL GLY LEU ASN
SEQRES 4 A 158 LEU GLU GLY ASN GLY VAL ALA THR ASP VAL PRO SER ALA
SEQRES 5 A 158 THR LYS ARG TRP GLY PHE ARG SER GLY VAL PRO PRO LYS
SEQRES 6 A 158 VAL VAL ASN TYR GLU ALA GLY GLU TRP ALA GLU ASN CYS
SEQRES 7 A 158 TYR ASN LEU GLU ILE LYS LYS PRO ASP GLY SER GLU CYS
SEQRES 8 A 158 LEU PRO ALA ALA PRO ASP GLY ILE ARG GLY PHE PRO ARG
SEQRES 9 A 158 CYS ARG TYR VAL HIS LYS VAL SER GLY THR GLY PRO CYS
SEQRES 10 A 158 ALA GLY ASP PHE ALA PHE HIS LYS GLU GLY ALA PHE PHE
SEQRES 11 A 158 LEU TYR ASP ARG LEU ALA SER THR VAL ILE TYR ARG GLY
SEQRES 12 A 158 THR THR PHE ALA GLU GLY VAL VAL ALA PHE LEU ILE LEU
SEQRES 13 A 158 PRO GLN
SEQRES 1 B 130 PRO LYS CYS ASN PRO ASN LEU HIS TYR TRP THR THR GLN
SEQRES 2 B 130 ASP GLU GLY ALA ALA ILE GLY LEU ALA TRP ILE PRO TYR
SEQRES 3 B 130 PHE GLY PRO ALA ALA GLU GLY ILE TYR THR GLU GLY LEU
SEQRES 4 B 130 MET HIS ASN GLN ASP GLY LEU ILE CYS GLY LEU ARG GLN
SEQRES 5 B 130 LEU ALA ASN GLU THR THR GLN ALA LEU GLN LEU PHE LEU
SEQRES 6 B 130 ARG ALA THR THR GLU LEU ARG THR PHE SER ILE LEU ASN
SEQRES 7 B 130 ARG LYS ALA ILE ASP PHE LEU LEU GLN ARG TRP GLY GLY
SEQRES 8 B 130 THR CYS HIS ILE LEU GLY PRO ASP CYS CYS ILE GLU PRO
SEQRES 9 B 130 HIS ASP TRP THR LYS ASN ILE THR ASP LYS ILE ASP GLN
SEQRES 10 B 130 ILE ILE HIS ASP PHE VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 C 256 MET THR THR ASN PRO VAL ASP LEU TRP SER ALA PRO SER
SEQRES 2 C 256 SER GLN ALA ARG LEU GLU LYS GLU TYR PHE ASP GLN HIS
SEQRES 3 C 256 PHE GLY PRO PHE PHE ARG THR GLU GLN LEU ILE ILE ARG
SEQRES 4 C 256 ALA PRO LEU THR ASP LYS HIS ILE TYR GLN PRO TYR PRO
SEQRES 5 C 256 SER GLY ALA ASP VAL PRO PHE GLY PRO PRO LEU ASP ILE
SEQRES 6 C 256 GLN ILE LEU HIS GLN VAL LEU ASP LEU GLN ILE ALA ILE
SEQRES 7 C 256 GLU ASN ILE THR ALA SER TYR ASP ASN GLU THR VAL THR
SEQRES 8 C 256 LEU GLN ASP ILE CYS LEU ALA PRO LEU SER PRO TYR ASN
SEQRES 9 C 256 THR ASN CYS THR ILE LEU SER VAL LEU ASN TYR PHE GLN
SEQRES 10 C 256 ASN SER HIS SER VAL LEU ASP HIS LYS LYS GLY ASP ASP
SEQRES 11 C 256 PHE PHE VAL TYR ALA ASP TYR HIS THR HIS PHE LEU TYR
SEQRES 12 C 256 CYS VAL ARG ALA PRO ALA SER LEU ASN ASP THR SER LEU
SEQRES 13 C 256 LEU HIS ASP PRO CYS LEU GLY THR PHE GLY GLY PRO VAL
SEQRES 14 C 256 PHE PRO TRP LEU VAL LEU GLY GLY TYR ASP ASP GLN ASN
SEQRES 15 C 256 TYR ASN ASN ALA THR ALA LEU VAL ILE THR PHE PRO VAL
SEQRES 16 C 256 ASN ASN TYR TYR ASN ASP THR GLU LYS LEU GLN ARG ALA
SEQRES 17 C 256 GLN ALA TRP GLU LYS GLU PHE ILE ASN PHE VAL LYS ASN
SEQRES 18 C 256 TYR LYS ASN PRO ASN LEU THR ILE SER PHE THR ALA GLU
SEQRES 19 C 256 ARG SER ILE GLU ASP GLU LEU ASN ARG GLU SER ASP SER
SEQRES 20 C 256 ASP LEU GLU HIS HIS HIS HIS HIS HIS
HET NAG D 1 14
HET NAG D 2 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 5 HOH *171(H2 O)
HELIX 1 AA1 SER A 59 ASN A 61 5 3
HELIX 2 AA2 ASP A 78 THR A 83 1 6
HELIX 3 AA3 ALA B 538 GLY B 541 5 4
HELIX 4 AA4 GLN B 551 THR B 576 1 26
HELIX 5 AA5 SER B 583 ARG B 596 1 14
HELIX 6 AA6 GLU C 19 HIS C 26 1 8
HELIX 7 AA7 GLY C 60 LEU C 63 5 4
HELIX 8 AA8 ASP C 64 ASN C 80 1 17
HELIX 9 AA9 THR C 91 CYS C 96 1 6
HELIX 10 AB1 SER C 111 GLN C 117 5 7
HELIX 11 AB2 SER C 119 ASP C 124 1 6
HELIX 12 AB3 ASP C 136 VAL C 145 1 10
HELIX 13 AB4 PHE C 170 VAL C 174 1 5
HELIX 14 AB5 ASN C 182 ALA C 186 5 5
HELIX 15 AB6 ASP C 201 ASN C 221 1 21
SHEET 1 AA1 4 LEU A 43 SER A 46 0
SHEET 2 AA1 4 LEU A 35 ILE A 38 -1 N VAL A 37 O GLN A 44
SHEET 3 AA1 4 ALA A 177 ILE A 185 1 O PHE A 183 N GLY A 36
SHEET 4 AA1 4 LEU A 63 ASN A 69 -1 N ARG A 64 O LEU A 184
SHEET 1 AA2 7 LEU A 43 SER A 46 0
SHEET 2 AA2 7 LEU A 35 ILE A 38 -1 N VAL A 37 O GLN A 44
SHEET 3 AA2 7 ALA A 177 ILE A 185 1 O PHE A 183 N GLY A 36
SHEET 4 AA2 7 PHE A 159 LEU A 161 -1 N LEU A 161 O ALA A 177
SHEET 5 AA2 7 LEU A 165 SER A 167 -1 O SER A 167 N PHE A 160
SHEET 6 AA2 7 VAL A 96 ASN A 98 -1 N VAL A 97 O ALA A 166
SHEET 7 AA2 7 ARG B 580 THR B 581 1 O THR B 581 N VAL A 96
SHEET 1 AA3 2 TRP A 86 ARG A 89 0
SHEET 2 AA3 2 PHE A 151 HIS A 154 -1 O PHE A 153 N GLY A 87
SHEET 1 AA4 3 ALA A 101 GLU A 103 0
SHEET 2 AA4 3 LEU B 515 THR B 520 -1 O TRP B 518 N GLY A 102
SHEET 3 AA4 3 TYR B 543 MET B 548 -1 O THR B 544 N THR B 519
SHEET 1 AA5 2 ALA A 105 LYS A 114 0
SHEET 2 AA5 2 CYS A 135 THR A 144 1 O ARG A 136 N ALA A 105
SHEET 1 AA6 4 LEU C 175 GLY C 176 0
SHEET 2 AA6 4 ALA C 188 ASN C 196 -1 O ALA C 188 N GLY C 176
SHEET 3 AA6 4 PHE C 31 ARG C 39 -1 N ARG C 32 O VAL C 195
SHEET 4 AA6 4 THR C 228 SER C 230 -1 O SER C 230 N ILE C 37
SHEET 1 AA7 2 HIS C 46 TYR C 48 0
SHEET 2 AA7 2 VAL C 57 PHE C 59 -1 O PHE C 59 N HIS C 46
SHEET 1 AA8 2 ALA C 83 TYR C 85 0
SHEET 2 AA8 2 GLU C 88 VAL C 90 -1 O VAL C 90 N ALA C 83
SHEET 1 AA9 2 LYS C 127 GLY C 128 0
SHEET 2 AA9 2 VAL C 133 ALA C 135 -1 O TYR C 134 N LYS C 127
SSBOND 1 CYS A 108 CYS A 135 1555 1555 2.07
SSBOND 2 CYS A 121 CYS A 147 1555 1555 2.06
SSBOND 3 CYS B 511 CYS B 556 1555 1555 2.04
SSBOND 4 CYS C 96 CYS C 107 1555 1555 2.05
SSBOND 5 CYS C 144 CYS C 161 1555 1555 2.04
LINK ND2 ASN B 563 C1 NAG D 1 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
CISPEP 1 GLY C 28 PRO C 29 0 0.44
CISPEP 2 TYR C 51 PRO C 52 0 -0.28
CISPEP 3 SER C 101 PRO C 102 0 -3.71
CRYST1 107.261 107.261 93.777 90.00 90.00 120.00 P 63 6
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 0.009323 0.005383 0.000000 0.00000
SCALE2 0.000000 0.010765 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010664 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
