HEADER PROTEIN BINDING 10-JUN-14 4TQ0
TITLE CRYSTAL STRUCTURE OF HUMAN ATG5-ATG16N69
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOPHAGY PROTEIN 5;
COMPND 3 CHAIN: A, C, E;
COMPND 4 SYNONYM: APG5-LIKE,APOPTOSIS-SPECIFIC PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: AUTOPHAGY-RELATED PROTEIN 16-1;
COMPND 8 CHAIN: B, D, F;
COMPND 9 FRAGMENT: UNP RESIDUES 1-69;
COMPND 10 SYNONYM: APG16-LIKE 1;
COMPND 11 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: ATG5, APG5L, ASP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ATG16L1, APG16L, UNQ9393/PRO34307;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS AUTOPHAGY PROTEIN COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.KIM,S.B.HONG,H.K.SONG
REVDAT 3 20-MAR-24 4TQ0 1 REMARK
REVDAT 2 29-JAN-20 4TQ0 1 SOURCE REMARK
REVDAT 1 11-MAR-15 4TQ0 0
JRNL AUTH J.H.KIM,S.B.HONG,J.K.LEE,S.HAN,K.H.ROH,K.E.LEE,Y.K.KIM,
JRNL AUTH 2 E.J.CHOI,H.K.SONG
JRNL TITL INSIGHTS INTO AUTOPHAGOSOME MATURATION REVEALED BY THE
JRNL TITL 2 STRUCTURES OF ATG5 WITH ITS INTERACTING PARTNERS
JRNL REF AUTOPHAGY V. 11 75 2015
JRNL REFN ESSN 1554-8635
JRNL PMID 25484072
JRNL DOI 10.4161/15548627.2014.984276
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.150
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 28318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.460
REMARK 3 FREE R VALUE TEST SET COUNT : 1829
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 37.0952 - 6.3326 0.99 2387 165 0.2276 0.2833
REMARK 3 2 6.3326 - 5.0304 0.98 2230 156 0.1991 0.2356
REMARK 3 3 5.0304 - 4.3956 0.97 2158 153 0.1534 0.2227
REMARK 3 4 4.3956 - 3.9943 0.96 2130 152 0.1598 0.2201
REMARK 3 5 3.9943 - 3.7083 0.96 2120 142 0.1820 0.2349
REMARK 3 6 3.7083 - 3.4898 0.99 2172 151 0.1827 0.2598
REMARK 3 7 3.4898 - 3.3151 0.99 2153 151 0.1951 0.2588
REMARK 3 8 3.3151 - 3.1709 0.99 2179 152 0.2080 0.2888
REMARK 3 9 3.1709 - 3.0489 0.93 2012 137 0.2343 0.3217
REMARK 3 10 3.0489 - 2.9437 0.85 1840 128 0.2496 0.3721
REMARK 3 11 2.9437 - 2.8517 0.79 1712 118 0.2598 0.3524
REMARK 3 12 2.8517 - 2.7702 0.80 1741 116 0.2633 0.4047
REMARK 3 13 2.7702 - 2.6973 0.76 1655 108 0.2835 0.4091
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) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.710
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 : 0.010 7256
REMARK 3 ANGLE : 1.390 9834
REMARK 3 CHIRALITY : 0.063 1050
REMARK 3 PLANARITY : 0.008 1248
REMARK 3 DIHEDRAL : 14.636 2681
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4TQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202048.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28321
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.697
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 : 15.80
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.1000
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, MGCL2, KCL, TRIS-HCL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 122.78850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.54700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.54700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.39425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.54700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.54700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 184.18275
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.54700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.54700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.39425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.54700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.54700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 184.18275
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 122.78850
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
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: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 25
REMARK 465 GLU A 26
REMARK 465 ILE A 27
REMARK 465 THR A 28
REMARK 465 GLU A 29
REMARK 465 ARG A 30
REMARK 465 ARG A 61
REMARK 465 GLN A 62
REMARK 465 GLU A 63
REMARK 465 ASP A 64
REMARK 465 ILE A 65
REMARK 465 SER A 66
REMARK 465 PRO A 108
REMARK 465 GLU A 109
REMARK 465 LYS A 110
REMARK 465 ASP A 111
REMARK 465 LEU A 112
REMARK 465 LEU A 113
REMARK 465 HIS A 114
REMARK 465 ASP A 228
REMARK 465 PRO A 229
REMARK 465 GLU A 230
REMARK 465 ASP A 231
REMARK 465 GLY A 232
REMARK 465 GLU A 233
REMARK 465 LYS A 234
REMARK 465 THR A 274
REMARK 465 ASP A 275
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 GLY B 4
REMARK 465 LEU B 5
REMARK 465 ARG B 6
REMARK 465 ALA B 7
REMARK 465 ALA B 8
REMARK 465 ASP B 9
REMARK 465 SER B 50
REMARK 465 VAL B 51
REMARK 465 LEU B 52
REMARK 465 ALA B 53
REMARK 465 GLN B 54
REMARK 465 LYS B 55
REMARK 465 LEU B 56
REMARK 465 GLN B 57
REMARK 465 ALA B 58
REMARK 465 GLU B 59
REMARK 465 LYS B 60
REMARK 465 HIS B 61
REMARK 465 ASP B 62
REMARK 465 VAL B 63
REMARK 465 PRO B 64
REMARK 465 ASN B 65
REMARK 465 ARG B 66
REMARK 465 HIS B 67
REMARK 465 GLU B 68
REMARK 465 ILE B 69
REMARK 465 MET C -13
REMARK 465 GLY C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 SER C -3
REMARK 465 GLN C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ASP C 3
REMARK 465 ARG C 61
REMARK 465 GLN C 62
REMARK 465 GLU C 63
REMARK 465 ASP C 64
REMARK 465 ILE C 65
REMARK 465 SER C 66
REMARK 465 PHE C 107
REMARK 465 PRO C 108
REMARK 465 GLU C 109
REMARK 465 LYS C 110
REMARK 465 ASP C 111
REMARK 465 LEU C 112
REMARK 465 LEU C 113
REMARK 465 HIS C 114
REMARK 465 CYS C 115
REMARK 465 ASP C 228
REMARK 465 PRO C 229
REMARK 465 GLU C 230
REMARK 465 ASP C 231
REMARK 465 GLY C 232
REMARK 465 GLU C 233
REMARK 465 LYS C 234
REMARK 465 THR C 274
REMARK 465 ASP C 275
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 SER D 3
REMARK 465 GLY D 4
REMARK 465 LEU D 5
REMARK 465 ARG D 6
REMARK 465 ALA D 7
REMARK 465 ALA D 8
REMARK 465 ASP D 9
REMARK 465 ASP D 47
REMARK 465 LEU D 48
REMARK 465 HIS D 49
REMARK 465 SER D 50
REMARK 465 VAL D 51
REMARK 465 LEU D 52
REMARK 465 ALA D 53
REMARK 465 GLN D 54
REMARK 465 LYS D 55
REMARK 465 LEU D 56
REMARK 465 GLN D 57
REMARK 465 ALA D 58
REMARK 465 GLU D 59
REMARK 465 LYS D 60
REMARK 465 HIS D 61
REMARK 465 ASP D 62
REMARK 465 VAL D 63
REMARK 465 PRO D 64
REMARK 465 ASN D 65
REMARK 465 ARG D 66
REMARK 465 HIS D 67
REMARK 465 GLU D 68
REMARK 465 ILE D 69
REMARK 465 MET E -13
REMARK 465 GLY E -12
REMARK 465 SER E -11
REMARK 465 SER E -10
REMARK 465 HIS E -9
REMARK 465 HIS E -8
REMARK 465 HIS E -7
REMARK 465 HIS E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 SER E -3
REMARK 465 GLN E -2
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 ASP E 3
REMARK 465 ARG E 61
REMARK 465 GLN E 62
REMARK 465 GLU E 63
REMARK 465 ASP E 64
REMARK 465 ILE E 65
REMARK 465 SER E 66
REMARK 465 GLU E 67
REMARK 465 PHE E 104
REMARK 465 LYS E 105
REMARK 465 SER E 106
REMARK 465 PHE E 107
REMARK 465 PRO E 108
REMARK 465 GLU E 109
REMARK 465 LYS E 110
REMARK 465 ASP E 111
REMARK 465 LEU E 112
REMARK 465 LEU E 113
REMARK 465 HIS E 114
REMARK 465 CYS E 115
REMARK 465 ALA E 226
REMARK 465 ILE E 227
REMARK 465 ASP E 228
REMARK 465 PRO E 229
REMARK 465 GLU E 230
REMARK 465 ASP E 231
REMARK 465 GLY E 232
REMARK 465 GLU E 233
REMARK 465 LYS E 234
REMARK 465 ASP E 275
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 SER F 3
REMARK 465 GLY F 4
REMARK 465 LEU F 5
REMARK 465 ARG F 6
REMARK 465 ALA F 7
REMARK 465 ALA F 8
REMARK 465 ASP F 9
REMARK 465 SER F 50
REMARK 465 VAL F 51
REMARK 465 LEU F 52
REMARK 465 ALA F 53
REMARK 465 GLN F 54
REMARK 465 LYS F 55
REMARK 465 LEU F 56
REMARK 465 GLN F 57
REMARK 465 ALA F 58
REMARK 465 GLU F 59
REMARK 465 LYS F 60
REMARK 465 HIS F 61
REMARK 465 ASP F 62
REMARK 465 VAL F 63
REMARK 465 PRO F 64
REMARK 465 ASN F 65
REMARK 465 ARG F 66
REMARK 465 HIS F 67
REMARK 465 GLU F 68
REMARK 465 ILE F 69
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 5 CG CD CE NZ
REMARK 470 GLU A 31 CG CD OE1 OE2
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 VAL A 59 CG1 CG2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 CYS A 115 SG
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 LYS A 171 CG CD CE NZ
REMARK 470 PHE B 10 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 45 CG CD CE NZ
REMARK 470 LYS C 5 CG CD CE NZ
REMARK 470 ARG C 30 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 31 CG CD OE1 OE2
REMARK 470 LYS C 105 CG CD CE NZ
REMARK 470 LYS C 138 CG CD CE NZ
REMARK 470 GLU C 144 CG CD OE1 OE2
REMARK 470 LYS C 147 CG CD CE NZ
REMARK 470 ARG C 161 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 10 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 15 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 5 CG CD CE NZ
REMARK 470 GLN E 24 CG CD OE1 NE2
REMARK 470 ILE E 27 CG1 CG2 CD1
REMARK 470 GLU E 31 CG CD OE1 OE2
REMARK 470 VAL E 59 CG1 CG2
REMARK 470 LYS E 130 CG CD CE NZ
REMARK 470 LYS E 138 CG CD CE NZ
REMARK 470 GLU E 144 CG CD OE1 OE2
REMARK 470 GLN E 146 CG CD OE1 NE2
REMARK 470 LYS E 148 CG CD CE NZ
REMARK 470 GLN E 152 CG CD OE1 NE2
REMARK 470 PHE F 10 CG CD1 CD2 CE1 CE2 CZ
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 O GLN E 211 O HOH E 331 2.08
REMARK 500 NE2 GLN F 28 O HOH F 104 2.13
REMARK 500 O PHE F 10 NH1 ARG F 15 2.14
REMARK 500 OG1 THR A 46 O HOH A 308 2.14
REMARK 500 O HOH A 328 O HOH C 335 2.16
REMARK 500 OH TYR C 175 O HOH C 331 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE C 121 CG1 - CB - CG2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 PRO C 205 C - N - CA ANGL. DEV. = 10.8 DEGREES
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 SER A 43 -165.19 -110.78
REMARK 500 GLN A 57 58.80 -140.93
REMARK 500 LYS A 58 70.83 -103.03
REMARK 500 THR A 192 -58.48 69.08
REMARK 500 CYS A 223 71.44 -154.77
REMARK 500 GLN B 28 -60.01 -97.36
REMARK 500 SER C 43 -162.37 -107.97
REMARK 500 LYS C 58 5.50 -63.81
REMARK 500 THR C 192 -57.44 65.76
REMARK 500 CYS C 223 69.89 -157.20
REMARK 500 SER E 43 -164.19 -109.84
REMARK 500 LYS E 58 -15.17 -42.07
REMARK 500 SER E 117 129.69 105.48
REMARK 500 THR E 192 -62.36 64.69
REMARK 500 ALA E 208 -93.19 74.09
REMARK 500 CYS E 223 73.51 -156.26
REMARK 500 GLN F 28 -62.40 -108.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 57 LYS A 58 134.56
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 E 340 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH E 342 DISTANCE = 6.64 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TQ1 RELATED DB: PDB
DBREF 4TQ0 A 1 275 UNP Q9H1Y0 ATG5_HUMAN 1 275
DBREF 4TQ0 B 1 69 UNP Q676U5 A16L1_HUMAN 1 69
DBREF 4TQ0 C 1 275 UNP Q9H1Y0 ATG5_HUMAN 1 275
DBREF 4TQ0 D 1 69 UNP Q676U5 A16L1_HUMAN 1 69
DBREF 4TQ0 E 1 275 UNP Q9H1Y0 ATG5_HUMAN 1 275
DBREF 4TQ0 F 1 69 UNP Q676U5 A16L1_HUMAN 1 69
SEQADV 4TQ0 MET A -13 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLY A -12 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER A -11 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER A -10 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS A -9 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS A -8 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS A -7 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS A -6 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS A -5 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS A -4 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER A -3 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLN A -2 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLY A -1 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER A 0 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 MET C -13 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLY C -12 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER C -11 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER C -10 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS C -9 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS C -8 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS C -7 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS C -6 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS C -5 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS C -4 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER C -3 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLN C -2 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLY C -1 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER C 0 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 MET E -13 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLY E -12 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER E -11 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER E -10 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS E -9 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS E -8 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS E -7 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS E -6 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS E -5 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 HIS E -4 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER E -3 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLN E -2 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 GLY E -1 UNP Q9H1Y0 EXPRESSION TAG
SEQADV 4TQ0 SER E 0 UNP Q9H1Y0 EXPRESSION TAG
SEQRES 1 A 289 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN GLY
SEQRES 2 A 289 SER MET THR ASP ASP LYS ASP VAL LEU ARG ASP VAL TRP
SEQRES 3 A 289 PHE GLY ARG ILE PRO THR CYS PHE THR LEU TYR GLN ASP
SEQRES 4 A 289 GLU ILE THR GLU ARG GLU ALA GLU PRO TYR TYR LEU LEU
SEQRES 5 A 289 LEU PRO ARG VAL SER TYR LEU THR LEU VAL THR ASP LYS
SEQRES 6 A 289 VAL LYS LYS HIS PHE GLN LYS VAL MET ARG GLN GLU ASP
SEQRES 7 A 289 ILE SER GLU ILE TRP PHE GLU TYR GLU GLY THR PRO LEU
SEQRES 8 A 289 LYS TRP HIS TYR PRO ILE GLY LEU LEU PHE ASP LEU LEU
SEQRES 9 A 289 ALA SER SER SER ALA LEU PRO TRP ASN ILE THR VAL HIS
SEQRES 10 A 289 PHE LYS SER PHE PRO GLU LYS ASP LEU LEU HIS CYS PRO
SEQRES 11 A 289 SER LYS ASP ALA ILE GLU ALA HIS PHE MET SER CYS MET
SEQRES 12 A 289 LYS GLU ALA ASP ALA LEU LYS HIS LYS SER GLN VAL ILE
SEQRES 13 A 289 ASN GLU MET GLN LYS LYS ASP HIS LYS GLN LEU TRP MET
SEQRES 14 A 289 GLY LEU GLN ASN ASP ARG PHE ASP GLN PHE TRP ALA ILE
SEQRES 15 A 289 ASN ARG LYS LEU MET GLU TYR PRO ALA GLU GLU ASN GLY
SEQRES 16 A 289 PHE ARG TYR ILE PRO PHE ARG ILE TYR GLN THR THR THR
SEQRES 17 A 289 GLU ARG PRO PHE ILE GLN LYS LEU PHE ARG PRO VAL ALA
SEQRES 18 A 289 ALA ASP GLY GLN LEU HIS THR LEU GLY ASP LEU LEU LYS
SEQRES 19 A 289 GLU VAL CYS PRO SER ALA ILE ASP PRO GLU ASP GLY GLU
SEQRES 20 A 289 LYS LYS ASN GLN VAL MET ILE HIS GLY ILE GLU PRO MET
SEQRES 21 A 289 LEU GLU THR PRO LEU GLN TRP LEU SER GLU HIS LEU SER
SEQRES 22 A 289 TYR PRO ASP ASN PHE LEU HIS ILE SER ILE ILE PRO GLN
SEQRES 23 A 289 PRO THR ASP
SEQRES 1 B 69 MET SER SER GLY LEU ARG ALA ALA ASP PHE PRO ARG TRP
SEQRES 2 B 69 LYS ARG HIS ILE SER GLU GLN LEU ARG ARG ARG ASP ARG
SEQRES 3 B 69 LEU GLN ARG GLN ALA PHE GLU GLU ILE ILE LEU GLN TYR
SEQRES 4 B 69 ASN LYS LEU LEU GLU LYS SER ASP LEU HIS SER VAL LEU
SEQRES 5 B 69 ALA GLN LYS LEU GLN ALA GLU LYS HIS ASP VAL PRO ASN
SEQRES 6 B 69 ARG HIS GLU ILE
SEQRES 1 C 289 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN GLY
SEQRES 2 C 289 SER MET THR ASP ASP LYS ASP VAL LEU ARG ASP VAL TRP
SEQRES 3 C 289 PHE GLY ARG ILE PRO THR CYS PHE THR LEU TYR GLN ASP
SEQRES 4 C 289 GLU ILE THR GLU ARG GLU ALA GLU PRO TYR TYR LEU LEU
SEQRES 5 C 289 LEU PRO ARG VAL SER TYR LEU THR LEU VAL THR ASP LYS
SEQRES 6 C 289 VAL LYS LYS HIS PHE GLN LYS VAL MET ARG GLN GLU ASP
SEQRES 7 C 289 ILE SER GLU ILE TRP PHE GLU TYR GLU GLY THR PRO LEU
SEQRES 8 C 289 LYS TRP HIS TYR PRO ILE GLY LEU LEU PHE ASP LEU LEU
SEQRES 9 C 289 ALA SER SER SER ALA LEU PRO TRP ASN ILE THR VAL HIS
SEQRES 10 C 289 PHE LYS SER PHE PRO GLU LYS ASP LEU LEU HIS CYS PRO
SEQRES 11 C 289 SER LYS ASP ALA ILE GLU ALA HIS PHE MET SER CYS MET
SEQRES 12 C 289 LYS GLU ALA ASP ALA LEU LYS HIS LYS SER GLN VAL ILE
SEQRES 13 C 289 ASN GLU MET GLN LYS LYS ASP HIS LYS GLN LEU TRP MET
SEQRES 14 C 289 GLY LEU GLN ASN ASP ARG PHE ASP GLN PHE TRP ALA ILE
SEQRES 15 C 289 ASN ARG LYS LEU MET GLU TYR PRO ALA GLU GLU ASN GLY
SEQRES 16 C 289 PHE ARG TYR ILE PRO PHE ARG ILE TYR GLN THR THR THR
SEQRES 17 C 289 GLU ARG PRO PHE ILE GLN LYS LEU PHE ARG PRO VAL ALA
SEQRES 18 C 289 ALA ASP GLY GLN LEU HIS THR LEU GLY ASP LEU LEU LYS
SEQRES 19 C 289 GLU VAL CYS PRO SER ALA ILE ASP PRO GLU ASP GLY GLU
SEQRES 20 C 289 LYS LYS ASN GLN VAL MET ILE HIS GLY ILE GLU PRO MET
SEQRES 21 C 289 LEU GLU THR PRO LEU GLN TRP LEU SER GLU HIS LEU SER
SEQRES 22 C 289 TYR PRO ASP ASN PHE LEU HIS ILE SER ILE ILE PRO GLN
SEQRES 23 C 289 PRO THR ASP
SEQRES 1 D 69 MET SER SER GLY LEU ARG ALA ALA ASP PHE PRO ARG TRP
SEQRES 2 D 69 LYS ARG HIS ILE SER GLU GLN LEU ARG ARG ARG ASP ARG
SEQRES 3 D 69 LEU GLN ARG GLN ALA PHE GLU GLU ILE ILE LEU GLN TYR
SEQRES 4 D 69 ASN LYS LEU LEU GLU LYS SER ASP LEU HIS SER VAL LEU
SEQRES 5 D 69 ALA GLN LYS LEU GLN ALA GLU LYS HIS ASP VAL PRO ASN
SEQRES 6 D 69 ARG HIS GLU ILE
SEQRES 1 E 289 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN GLY
SEQRES 2 E 289 SER MET THR ASP ASP LYS ASP VAL LEU ARG ASP VAL TRP
SEQRES 3 E 289 PHE GLY ARG ILE PRO THR CYS PHE THR LEU TYR GLN ASP
SEQRES 4 E 289 GLU ILE THR GLU ARG GLU ALA GLU PRO TYR TYR LEU LEU
SEQRES 5 E 289 LEU PRO ARG VAL SER TYR LEU THR LEU VAL THR ASP LYS
SEQRES 6 E 289 VAL LYS LYS HIS PHE GLN LYS VAL MET ARG GLN GLU ASP
SEQRES 7 E 289 ILE SER GLU ILE TRP PHE GLU TYR GLU GLY THR PRO LEU
SEQRES 8 E 289 LYS TRP HIS TYR PRO ILE GLY LEU LEU PHE ASP LEU LEU
SEQRES 9 E 289 ALA SER SER SER ALA LEU PRO TRP ASN ILE THR VAL HIS
SEQRES 10 E 289 PHE LYS SER PHE PRO GLU LYS ASP LEU LEU HIS CYS PRO
SEQRES 11 E 289 SER LYS ASP ALA ILE GLU ALA HIS PHE MET SER CYS MET
SEQRES 12 E 289 LYS GLU ALA ASP ALA LEU LYS HIS LYS SER GLN VAL ILE
SEQRES 13 E 289 ASN GLU MET GLN LYS LYS ASP HIS LYS GLN LEU TRP MET
SEQRES 14 E 289 GLY LEU GLN ASN ASP ARG PHE ASP GLN PHE TRP ALA ILE
SEQRES 15 E 289 ASN ARG LYS LEU MET GLU TYR PRO ALA GLU GLU ASN GLY
SEQRES 16 E 289 PHE ARG TYR ILE PRO PHE ARG ILE TYR GLN THR THR THR
SEQRES 17 E 289 GLU ARG PRO PHE ILE GLN LYS LEU PHE ARG PRO VAL ALA
SEQRES 18 E 289 ALA ASP GLY GLN LEU HIS THR LEU GLY ASP LEU LEU LYS
SEQRES 19 E 289 GLU VAL CYS PRO SER ALA ILE ASP PRO GLU ASP GLY GLU
SEQRES 20 E 289 LYS LYS ASN GLN VAL MET ILE HIS GLY ILE GLU PRO MET
SEQRES 21 E 289 LEU GLU THR PRO LEU GLN TRP LEU SER GLU HIS LEU SER
SEQRES 22 E 289 TYR PRO ASP ASN PHE LEU HIS ILE SER ILE ILE PRO GLN
SEQRES 23 E 289 PRO THR ASP
SEQRES 1 F 69 MET SER SER GLY LEU ARG ALA ALA ASP PHE PRO ARG TRP
SEQRES 2 F 69 LYS ARG HIS ILE SER GLU GLN LEU ARG ARG ARG ASP ARG
SEQRES 3 F 69 LEU GLN ARG GLN ALA PHE GLU GLU ILE ILE LEU GLN TYR
SEQRES 4 F 69 ASN LYS LEU LEU GLU LYS SER ASP LEU HIS SER VAL LEU
SEQRES 5 F 69 ALA GLN LYS LEU GLN ALA GLU LYS HIS ASP VAL PRO ASN
SEQRES 6 F 69 ARG HIS GLU ILE
FORMUL 7 HOH *162(H2 O)
HELIX 1 AA1 ASP A 4 PHE A 13 1 10
HELIX 2 AA2 TYR A 44 THR A 49 1 6
HELIX 3 AA3 THR A 49 PHE A 56 1 8
HELIX 4 AA4 PRO A 82 ALA A 91 1 10
HELIX 5 AA5 SER A 117 HIS A 137 1 21
HELIX 6 AA6 GLN A 140 MET A 145 1 6
HELIX 7 AA7 GLN A 146 ASN A 159 1 14
HELIX 8 AA8 ARG A 161 MET A 173 1 13
HELIX 9 AA9 PRO A 176 ASN A 180 5 5
HELIX 10 AB1 THR A 214 CYS A 223 1 10
HELIX 11 AB2 PRO A 224 ILE A 227 5 4
HELIX 12 AB3 PRO A 250 LEU A 258 1 9
HELIX 13 AB4 PRO B 11 LEU B 48 1 38
HELIX 14 AB5 LYS C 5 GLY C 14 1 10
HELIX 15 AB6 TYR C 44 THR C 49 1 6
HELIX 16 AB7 THR C 49 LYS C 58 1 10
HELIX 17 AB8 PRO C 82 ALA C 91 1 10
HELIX 18 AB9 SER C 117 HIS C 137 1 21
HELIX 19 AC1 GLN C 140 MET C 145 1 6
HELIX 20 AC2 GLN C 146 ASN C 159 1 14
HELIX 21 AC3 ARG C 161 MET C 173 1 13
HELIX 22 AC4 PRO C 176 ASN C 180 5 5
HELIX 23 AC5 THR C 214 CYS C 223 1 10
HELIX 24 AC6 PRO C 224 ILE C 227 5 4
HELIX 25 AC7 PRO C 250 LEU C 258 1 9
HELIX 26 AC8 PRO D 11 ARG D 29 1 19
HELIX 27 AC9 ARG D 29 SER D 46 1 18
HELIX 28 AD1 LYS E 5 GLY E 14 1 10
HELIX 29 AD2 TYR E 44 THR E 49 1 6
HELIX 30 AD3 THR E 49 LYS E 58 1 10
HELIX 31 AD4 PRO E 82 ALA E 91 1 10
HELIX 32 AD5 SER E 117 HIS E 137 1 21
HELIX 33 AD6 GLN E 146 ASN E 159 1 14
HELIX 34 AD7 ARG E 161 MET E 173 1 13
HELIX 35 AD8 THR E 214 CYS E 223 1 10
HELIX 36 AD9 PRO E 250 LEU E 258 1 9
HELIX 37 AE1 PRO F 11 ASP F 47 1 37
SHEET 1 AA1 5 TYR A 35 PRO A 40 0
SHEET 2 AA1 5 ARG A 15 LEU A 22 -1 N ILE A 16 O LEU A 39
SHEET 3 AA1 5 TRP A 98 PHE A 104 1 O TRP A 98 N CYS A 19
SHEET 4 AA1 5 ILE A 68 TYR A 72 -1 N GLU A 71 O THR A 101
SHEET 5 AA1 5 THR A 75 PRO A 76 -1 O THR A 75 N TYR A 72
SHEET 1 AA2 3 PHE A 187 GLN A 191 0
SHEET 2 AA2 3 LEU A 265 PRO A 271 1 O ILE A 267 N TYR A 190
SHEET 3 AA2 3 ASN A 236 MET A 239 -1 N GLN A 237 O ILE A 270
SHEET 1 AA3 5 TYR C 35 PRO C 40 0
SHEET 2 AA3 5 ARG C 15 LEU C 22 -1 N PHE C 20 O TYR C 35
SHEET 3 AA3 5 TRP C 98 PHE C 104 1 O TRP C 98 N CYS C 19
SHEET 4 AA3 5 ILE C 68 TYR C 72 -1 N GLU C 71 O THR C 101
SHEET 5 AA3 5 THR C 75 PRO C 76 -1 O THR C 75 N TYR C 72
SHEET 1 AA4 3 PHE C 187 GLN C 191 0
SHEET 2 AA4 3 LEU C 265 PRO C 271 1 O ILE C 267 N TYR C 190
SHEET 3 AA4 3 ASN C 236 MET C 239 -1 N MET C 239 O SER C 268
SHEET 1 AA5 5 TYR E 35 PRO E 40 0
SHEET 2 AA5 5 ARG E 15 LEU E 22 -1 N PHE E 20 O TYR E 35
SHEET 3 AA5 5 TRP E 98 HIS E 103 1 O TRP E 98 N PRO E 17
SHEET 4 AA5 5 TRP E 69 TYR E 72 -1 N GLU E 71 O THR E 101
SHEET 5 AA5 5 THR E 75 PRO E 76 -1 O THR E 75 N TYR E 72
SHEET 1 AA6 3 PHE E 187 GLN E 191 0
SHEET 2 AA6 3 LEU E 265 PRO E 271 1 O ILE E 267 N TYR E 190
SHEET 3 AA6 3 ASN E 236 MET E 239 -1 N GLN E 237 O ILE E 270
SHEET 1 AA7 2 VAL E 206 ALA E 207 0
SHEET 2 AA7 2 GLN E 211 LEU E 212 -1 O GLN E 211 N ALA E 207
CISPEP 1 LEU A 96 PRO A 97 0 -9.36
CISPEP 2 GLN A 272 PRO A 273 0 -23.42
CISPEP 3 LEU C 96 PRO C 97 0 -11.51
CISPEP 4 GLN C 272 PRO C 273 0 -12.94
CISPEP 5 PHE D 10 PRO D 11 0 0.20
CISPEP 6 GLU E 73 GLY E 74 0 -17.85
CISPEP 7 LEU E 96 PRO E 97 0 -10.34
CISPEP 8 ASP E 209 GLY E 210 0 -9.50
CRYST1 93.094 93.094 245.577 90.00 90.00 90.00 P 41 21 2 24
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 0.010742 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010742 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004072 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
