HEADER CELL CYCLE 12-FEB-15 4Y66
TITLE CRYSTAL STRUCTURE OF GIARDIA LAMBLIA HOP2-MND1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MND1;
COMPND 3 CHAIN: A, C, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PUTATIVE TBPIP FAMILY PROTEIN;
COMPND 7 CHAIN: B, D, F;
COMPND 8 SYNONYM: HOP2;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GIARDIA LAMBLIA ATCC 50803;
SOURCE 3 ORGANISM_TAXID: 184922;
SOURCE 4 STRAIN: ATCC 50803;
SOURCE 5 GENE: GL50803_6626;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: GIARDIA LAMBLIA;
SOURCE 10 ORGANISM_TAXID: 5741;
SOURCE 11 STRAIN: ATCC 50803;
SOURCE 12 GENE: GSB_17044;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.A.KANG,H.C.SHIN,B.H.OH
REVDAT 3 20-MAR-24 4Y66 1 SOURCE JRNL REMARK
REVDAT 2 06-MAY-15 4Y66 1 JRNL
REVDAT 1 18-MAR-15 4Y66 0
JRNL AUTH H.A.KANG,H.C.SHIN,A.S.KALANTZI,C.P.TOSELAND,H.M.KIM,
JRNL AUTH 2 S.GRUBER,M.D.PERARO,B.H.OH
JRNL TITL CRYSTAL STRUCTURE OF HOP2-MND1 AND MECHANISTIC INSIGHTS INTO
JRNL TITL 2 ITS ROLE IN MEIOTIC RECOMBINATION
JRNL REF NUCLEIC ACIDS RES. V. 43 3841 2015
JRNL REFN ESSN 1362-4962
JRNL PMID 25740648
JRNL DOI 10.1093/NAR/GKV172
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.780
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 34247
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1704
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 40.6573 - 7.3132 0.98 3171 160 0.2056 0.2854
REMARK 3 2 7.3132 - 5.8102 0.96 3020 159 0.2779 0.3116
REMARK 3 3 5.8102 - 5.0773 0.96 2999 160 0.2457 0.3007
REMARK 3 4 5.0773 - 4.6138 0.96 2936 153 0.2122 0.2717
REMARK 3 5 4.6138 - 4.2835 0.95 2926 146 0.2076 0.2225
REMARK 3 6 4.2835 - 4.0312 0.92 2838 160 0.2135 0.2346
REMARK 3 7 4.0312 - 3.8294 0.90 2784 141 0.2263 0.2603
REMARK 3 8 3.8294 - 3.6628 0.86 2670 144 0.2484 0.3015
REMARK 3 9 3.6628 - 3.5219 0.83 2548 136 0.2676 0.3108
REMARK 3 10 3.5219 - 3.4004 0.77 2328 115 0.2928 0.3216
REMARK 3 11 3.4004 - 3.2942 0.74 2271 120 0.3236 0.3158
REMARK 3 12 3.2942 - 3.2000 0.66 2052 110 0.3516 0.4248
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) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 7281
REMARK 3 ANGLE : 1.340 9909
REMARK 3 CHIRALITY : 0.051 1238
REMARK 3 PLANARITY : 0.007 1292
REMARK 3 DIHEDRAL : 17.247 2546
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): 20.6299 56.7855 -50.0752
REMARK 3 T TENSOR
REMARK 3 T11: 0.1750 T22: 0.1731
REMARK 3 T33: 0.1417 T12: -0.0645
REMARK 3 T13: -0.0329 T23: 0.2472
REMARK 3 L TENSOR
REMARK 3 L11: -0.0927 L22: 0.0442
REMARK 3 L33: 0.0397 L12: 0.0663
REMARK 3 L13: -0.1320 L23: 0.0213
REMARK 3 S TENSOR
REMARK 3 S11: -0.1132 S12: 0.0019 S13: 0.0242
REMARK 3 S21: -0.1263 S22: -0.1175 S23: -0.0022
REMARK 3 S31: -0.0359 S32: 0.0765 S33: -0.0956
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 4Y66 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206906.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97889
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34750
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TASCIMATE, TRIS, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.92350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.53300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.92350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.53300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 5650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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: 7540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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: 4710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 1
REMARK 465 ALA A 2
REMARK 465 PRO A 3
REMARK 465 LYS A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 SER A 7
REMARK 465 LEU A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 10
REMARK 465 LYS A 11
REMARK 465 LYS A 12
REMARK 465 GLU A 13
REMARK 465 ARG A 14
REMARK 465 LEU A 15
REMARK 465 LEU A 16
REMARK 465 GLU A 17
REMARK 465 GLU A 18
REMARK 465 MET A 19
REMARK 465 LEU A 20
REMARK 465 LYS A 21
REMARK 465 ARG A 22
REMARK 465 GLY A 23
REMARK 465 GLU A 24
REMARK 465 ILE A 25
REMARK 465 TYR A 26
REMARK 465 SER A 27
REMARK 465 ASN A 28
REMARK 465 LYS A 29
REMARK 465 THR A 30
REMARK 465 ILE A 31
REMARK 465 GLU A 32
REMARK 465 THR A 33
REMARK 465 LEU A 34
REMARK 465 SER A 35
REMARK 465 LYS A 36
REMARK 465 PRO A 37
REMARK 465 THR A 38
REMARK 465 GLY A 39
REMARK 465 ILE A 40
REMARK 465 SER A 41
REMARK 465 SER A 42
REMARK 465 MET A 43
REMARK 465 VAL A 44
REMARK 465 ILE A 45
REMARK 465 LYS A 46
REMARK 465 ASN A 47
REMARK 465 VAL A 48
REMARK 465 LEU A 49
REMARK 465 GLN A 50
REMARK 465 ALA A 51
REMARK 465 LEU A 52
REMARK 465 VAL A 53
REMARK 465 ASN A 54
REMARK 465 GLU A 55
REMARK 465 ASP A 56
REMARK 465 LEU A 57
REMARK 465 VAL A 58
REMARK 465 ASP A 59
REMARK 465 THR A 60
REMARK 465 ASP A 61
REMARK 465 LYS A 62
REMARK 465 ILE A 63
REMARK 465 GLY A 64
REMARK 465 ALA A 65
REMARK 465 SER A 66
REMARK 465 THR A 67
REMARK 465 TYR A 68
REMARK 465 TYR A 69
REMARK 465 TRP A 70
REMARK 465 CYS A 71
REMARK 465 PHE A 72
REMARK 465 ALA A 73
REMARK 465 SER A 74
REMARK 465 LYS A 75
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 TYR B 5
REMARK 465 LYS B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 PHE B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 VAL B 12
REMARK 465 LYS B 13
REMARK 465 GLU B 14
REMARK 465 LEU B 15
REMARK 465 MET B 16
REMARK 465 GLN B 17
REMARK 465 THR B 18
REMARK 465 SER B 19
REMARK 465 ASN B 20
REMARK 465 LYS B 21
REMARK 465 PRO B 22
REMARK 465 GLN B 23
REMARK 465 ASN B 24
REMARK 465 VAL B 25
REMARK 465 GLN B 26
REMARK 465 THR B 27
REMARK 465 ALA B 28
REMARK 465 ILE B 29
REMARK 465 ASN B 30
REMARK 465 ASN B 31
REMARK 465 THR B 32
REMARK 465 GLY B 33
REMARK 465 SER B 34
REMARK 465 LYS B 35
REMARK 465 TYR B 36
REMARK 465 GLY B 37
REMARK 465 LYS B 38
REMARK 465 THR B 39
REMARK 465 THR B 40
REMARK 465 VAL B 41
REMARK 465 GLN B 42
REMARK 465 LYS B 43
REMARK 465 ALA B 44
REMARK 465 LEU B 45
REMARK 465 ASP B 46
REMARK 465 GLU B 47
REMARK 465 LEU B 48
REMARK 465 VAL B 49
REMARK 465 ALA B 50
REMARK 465 GLN B 51
REMARK 465 ASN B 52
REMARK 465 LEU B 53
REMARK 465 CYS B 54
REMARK 465 ILE B 55
REMARK 465 TYR B 56
REMARK 465 THR B 57
REMARK 465 GLU B 58
REMARK 465 ILE B 59
REMARK 465 GLY B 60
REMARK 465 LYS B 61
REMARK 465 THR B 62
REMARK 465 GLY B 63
REMARK 465 LYS B 64
REMARK 465 LEU B 65
REMARK 465 TYR B 66
REMARK 465 LEU B 67
REMARK 465 TRP B 68
REMARK 465 ASN B 69
REMARK 465 GLN B 70
REMARK 465 ASN B 71
REMARK 465 LEU B 72
REMARK 465 LEU B 73
REMARK 465 GLU B 74
REMARK 465 VAL B 75
REMARK 465 LEU B 76
REMARK 465 SER B 77
REMARK 465 ASP B 78
REMARK 465 LYS B 231
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PRO C 3
REMARK 465 LYS C 4
REMARK 465 GLY C 5
REMARK 465 GLU C 203
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 TYR D 5
REMARK 465 LYS D 6
REMARK 465 GLU D 7
REMARK 465 THR D 57
REMARK 465 GLU D 58
REMARK 465 ILE D 59
REMARK 465 GLY D 60
REMARK 465 LYS D 61
REMARK 465 THR D 62
REMARK 465 GLY D 63
REMARK 465 LYS D 64
REMARK 465 SER D 221
REMARK 465 LYS D 222
REMARK 465 LYS D 226
REMARK 465 ALA D 227
REMARK 465 ALA D 228
REMARK 465 LEU D 229
REMARK 465 LYS D 230
REMARK 465 LYS D 231
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 PRO E 3
REMARK 465 LYS E 4
REMARK 465 GLY E 5
REMARK 465 THR E 6
REMARK 465 SER E 7
REMARK 465 LEU E 8
REMARK 465 THR E 38
REMARK 465 GLY E 39
REMARK 465 ILE E 63
REMARK 465 GLY E 64
REMARK 465 ALA E 65
REMARK 465 ALA E 164
REMARK 465 ASN E 165
REMARK 465 LEU E 166
REMARK 465 TRP E 167
REMARK 465 THR E 168
REMARK 465 ASP E 169
REMARK 465 ASN E 170
REMARK 465 ILE E 171
REMARK 465 PHE E 172
REMARK 465 CYS E 173
REMARK 465 LEU E 174
REMARK 465 GLN E 175
REMARK 465 LYS E 176
REMARK 465 TYR E 177
REMARK 465 MET E 178
REMARK 465 LEU E 179
REMARK 465 THR E 180
REMARK 465 LYS E 181
REMARK 465 LEU E 182
REMARK 465 GLN E 183
REMARK 465 MET E 184
REMARK 465 ASP E 185
REMARK 465 LYS E 186
REMARK 465 LYS E 187
REMARK 465 THR E 188
REMARK 465 VAL E 189
REMARK 465 SER E 190
REMARK 465 THR E 191
REMARK 465 ALA E 192
REMARK 465 LEU E 193
REMARK 465 GLY E 194
REMARK 465 ILE E 195
REMARK 465 THR E 196
REMARK 465 GLY E 197
REMARK 465 GLU E 198
REMARK 465 PHE E 199
REMARK 465 ASP E 200
REMARK 465 TYR E 201
REMARK 465 LEU E 202
REMARK 465 GLU E 203
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 ARG F 143
REMARK 465 GLU F 144
REMARK 465 SER F 145
REMARK 465 ASN F 146
REMARK 465 ALA F 147
REMARK 465 ILE F 148
REMARK 465 VAL F 149
REMARK 465 SER F 150
REMARK 465 ASP F 151
REMARK 465 ALA F 152
REMARK 465 THR F 166
REMARK 465 ALA F 167
REMARK 465 TRP F 168
REMARK 465 ALA F 169
REMARK 465 THR F 170
REMARK 465 ARG F 171
REMARK 465 ARG F 172
REMARK 465 ALA F 173
REMARK 465 LYS F 174
REMARK 465 CYS F 175
REMARK 465 ARG F 176
REMARK 465 GLU F 177
REMARK 465 VAL F 178
REMARK 465 ILE F 179
REMARK 465 ASP F 180
REMARK 465 THR F 181
REMARK 465 LEU F 182
REMARK 465 SER F 183
REMARK 465 GLU F 184
REMARK 465 GLY F 185
REMARK 465 MET F 186
REMARK 465 GLY F 187
REMARK 465 VAL F 188
REMARK 465 LYS F 189
REMARK 465 PRO F 190
REMARK 465 SER F 191
REMARK 465 ALA F 192
REMARK 465 PHE F 193
REMARK 465 MET F 194
REMARK 465 ASP F 195
REMARK 465 GLN F 196
REMARK 465 LEU F 197
REMARK 465 GLY F 198
REMARK 465 LEU F 199
REMARK 465 GLU F 200
REMARK 465 GLU F 201
REMARK 465 GLY F 202
REMARK 465 LEU F 203
REMARK 465 PRO F 204
REMARK 465 ASN F 219
REMARK 465 VAL F 220
REMARK 465 SER F 221
REMARK 465 LYS F 222
REMARK 465 ALA F 223
REMARK 465 ASP F 224
REMARK 465 ILE F 225
REMARK 465 LYS F 226
REMARK 465 ALA F 227
REMARK 465 ALA F 228
REMARK 465 LEU F 229
REMARK 465 LYS F 230
REMARK 465 LYS F 231
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 76 CG CD NE CZ NH1 NH2
REMARK 470 SER A 77 OG
REMARK 470 GLN A 78 CG CD OE1 NE2
REMARK 470 ARG A 81 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 LEU A 84 CG CD1 CD2
REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 THR A 95 OG1 CG2
REMARK 470 ASN A 96 CG OD1 ND2
REMARK 470 ASP A 99 CG OD1 OD2
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 THR A 102 OG1 CG2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 GLU A 116 CG CD OE1 OE2
REMARK 470 GLU A 117 CG CD OE1 OE2
REMARK 470 SER A 119 OG
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 LYS A 125 CG CD CE NZ
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 ASP A 148 CG OD1 OD2
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 TYR A 177 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 180 OG1 CG2
REMARK 470 LYS A 181 CG CD CE NZ
REMARK 470 GLN A 183 CG CD OE1 NE2
REMARK 470 ASP A 185 CG OD1 OD2
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 GLU A 198 CG CD OE1 OE2
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 GLN B 80 CG CD OE1 NE2
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 ASN B 85 CG OD1 ND2
REMARK 470 ASP B 90 CG OD1 OD2
REMARK 470 LYS B 92 CG CD CE NZ
REMARK 470 GLN B 94 CG CD OE1 NE2
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 LYS B 97 CG CD CE NZ
REMARK 470 GLN B 100 CG CD OE1 NE2
REMARK 470 GLN B 101 CG CD OE1 NE2
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 LEU B 105 CG CD1 CD2
REMARK 470 ARG B 106 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 107 CG1 CG2 CD1
REMARK 470 LEU B 112 CG CD1 CD2
REMARK 470 GLU B 113 CG CD OE1 OE2
REMARK 470 LEU B 121 CG CD1 CD2
REMARK 470 ASP B 136 CG OD1 OD2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 ARG B 176 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 180 CG OD1 OD2
REMARK 470 MET B 186 CG SD CE
REMARK 470 LYS B 189 CG CD CE NZ
REMARK 470 ASP B 195 CG OD1 OD2
REMARK 470 GLN B 196 CG CD OE1 NE2
REMARK 470 GLU B 200 CG CD OE1 OE2
REMARK 470 GLU B 201 CG CD OE1 OE2
REMARK 470 LYS B 212 CG CD CE NZ
REMARK 470 LYS B 213 CG CD CE NZ
REMARK 470 LEU B 229 CG CD1 CD2
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 GLU C 13 CG CD OE1 OE2
REMARK 470 ARG C 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 GLU C 24 CG CD OE1 OE2
REMARK 470 LYS C 29 CG CD CE NZ
REMARK 470 LYS C 36 CG CD CE NZ
REMARK 470 LYS C 89 CG CD CE NZ
REMARK 470 ARG C 104 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 107 CG CD OE1 OE2
REMARK 470 GLU C 116 CG CD OE1 OE2
REMARK 470 GLU C 117 CG CD OE1 OE2
REMARK 470 GLU C 133 CG CD OE1 OE2
REMARK 470 GLU C 134 CG CD OE1 OE2
REMARK 470 LYS C 152 CG CD CE NZ
REMARK 470 LYS C 186 CG CD CE NZ
REMARK 470 LYS C 187 CG CD CE NZ
REMARK 470 LYS D 13 CG CD CE NZ
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 LEU D 15 CG CD1 CD2
REMARK 470 LYS D 21 CG CD CE NZ
REMARK 470 VAL D 25 CG1 CG2
REMARK 470 GLN D 26 CG CD OE1 NE2
REMARK 470 ILE D 29 CG1 CG2 CD1
REMARK 470 THR D 32 OG1 CG2
REMARK 470 TYR D 36 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 38 CG CD CE NZ
REMARK 470 ASP D 46 CG OD1 OD2
REMARK 470 ILE D 55 CG1 CG2 CD1
REMARK 470 TYR D 66 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU D 81 CG CD1 CD2
REMARK 470 GLU D 83 CG CD OE1 OE2
REMARK 470 ASP D 90 CG OD1 OD2
REMARK 470 LYS D 97 CG CD CE NZ
REMARK 470 ARG D 129 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 203 CG CD1 CD2
REMARK 470 ASP D 224 CG OD1 OD2
REMARK 470 ILE D 225 CG1 CG2 CD1
REMARK 470 GLU E 10 CG CD OE1 OE2
REMARK 470 LYS E 11 CG CD CE NZ
REMARK 470 LYS E 12 CG CD CE NZ
REMARK 470 ARG E 14 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 15 CG CD1 CD2
REMARK 470 LYS E 29 CG CD CE NZ
REMARK 470 ILE E 31 CG1 CG2 CD1
REMARK 470 GLU E 32 CG CD OE1 OE2
REMARK 470 LEU E 34 CG CD1 CD2
REMARK 470 LYS E 36 CG CD CE NZ
REMARK 470 ILE E 40 CG1 CG2 CD1
REMARK 470 SER E 41 OG
REMARK 470 MET E 43 CG SD CE
REMARK 470 ILE E 45 CG1 CG2 CD1
REMARK 470 LYS E 46 CG CD CE NZ
REMARK 470 ASN E 47 CG OD1 ND2
REMARK 470 VAL E 48 CG1 CG2
REMARK 470 SER E 66 OG
REMARK 470 SER E 74 OG
REMARK 470 ARG E 76 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 86 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 89 CG CD CE NZ
REMARK 470 ILE E 98 CG1 CG2 CD1
REMARK 470 ASP E 99 CG OD1 OD2
REMARK 470 LYS E 100 CG CD CE NZ
REMARK 470 THR E 102 OG1 CG2
REMARK 470 ARG E 104 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 106 CG CD OE1 OE2
REMARK 470 LYS E 109 CG CD CE NZ
REMARK 470 VAL E 110 CG1 CG2
REMARK 470 GLU E 113 CG CD OE1 OE2
REMARK 470 GLU E 114 CG CD OE1 OE2
REMARK 470 GLU E 116 CG CD OE1 OE2
REMARK 470 GLU E 117 CG CD OE1 OE2
REMARK 470 SER E 119 OG
REMARK 470 SER E 120 OG
REMARK 470 LYS E 131 CG CD CE NZ
REMARK 470 GLU E 134 CG CD OE1 OE2
REMARK 470 ARG E 136 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 140 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 141 CG OD1 OD2
REMARK 470 LEU E 142 CG CD1 CD2
REMARK 470 LEU E 143 CG CD1 CD2
REMARK 470 LYS E 144 CG CD CE NZ
REMARK 470 ASN E 145 CG OD1 ND2
REMARK 470 ASP E 146 CG OD1 OD2
REMARK 470 VAL E 149 CG1 CG2
REMARK 470 GLN E 151 CG CD OE1 NE2
REMARK 470 LEU E 153 CG CD1 CD2
REMARK 470 ARG E 154 CG CD NE CZ NH1 NH2
REMARK 470 TYR E 156 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP E 158 CG OD1 OD2
REMARK 470 LYS E 161 CG CD CE NZ
REMARK 470 GLN E 162 CG CD OE1 NE2
REMARK 470 GLU E 163 CG CD OE1 OE2
REMARK 470 LYS F 6 CG CD CE NZ
REMARK 470 GLU F 7 CG CD OE1 OE2
REMARK 470 LYS F 13 CG CD CE NZ
REMARK 470 GLU F 14 CG CD OE1 OE2
REMARK 470 GLN F 17 CG CD OE1 NE2
REMARK 470 LYS F 21 CG CD CE NZ
REMARK 470 GLN F 26 CG CD OE1 NE2
REMARK 470 LYS F 38 CG CD CE NZ
REMARK 470 LYS F 43 CG CD CE NZ
REMARK 470 ILE F 55 CG1 CG2 CD1
REMARK 470 LYS F 61 CG CD CE NZ
REMARK 470 THR F 62 OG1 CG2
REMARK 470 LYS F 64 CG CD CE NZ
REMARK 470 SER F 77 OG
REMARK 470 GLU F 83 CG CD OE1 OE2
REMARK 470 ASP F 90 CG OD1 OD2
REMARK 470 GLU F 96 CG CD OE1 OE2
REMARK 470 LYS F 97 CG CD CE NZ
REMARK 470 ARG F 106 CG CD NE CZ NH1 NH2
REMARK 470 LEU F 112 CG CD1 CD2
REMARK 470 GLU F 124 CG CD OE1 OE2
REMARK 470 ASP F 126 CG OD1 OD2
REMARK 470 LEU F 128 CG CD1 CD2
REMARK 470 ARG F 129 CG CD NE CZ NH1 NH2
REMARK 470 SER F 133 OG
REMARK 470 GLU F 137 CG CD OE1 OE2
REMARK 470 ARG F 140 CG CD NE CZ NH1 NH2
REMARK 470 LEU F 141 CG CD1 CD2
REMARK 470 VAL F 142 CG1 CG2
REMARK 470 ASP F 153 CG OD1 OD2
REMARK 470 LEU F 155 CG CD1 CD2
REMARK 470 THR F 156 OG1 CG2
REMARK 470 GLN F 158 CG CD OE1 NE2
REMARK 470 LYS F 159 CG CD CE NZ
REMARK 470 ASN F 160 CG OD1 ND2
REMARK 470 LYS F 162 CG CD CE NZ
REMARK 470 ASP F 163 CG OD1 OD2
REMARK 470 MET F 205 CG SD CE
REMARK 470 THR F 206 OG1 CG2
REMARK 470 THR F 207 OG1 CG2
REMARK 470 TYR F 208 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR F 209 OG1 CG2
REMARK 470 LYS F 212 CG CD CE NZ
REMARK 470 LYS F 213 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 O GLU D 14 OG1 THR D 18 2.06
REMARK 500 O GLU E 92 ND2 ASN E 96 2.08
REMARK 500 NH2 ARG C 118 O PRO D 116 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU F 103 CG GLU F 103 CD 0.095
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 LYS A 181 -59.87 -121.37
REMARK 500 ALA B 214 -70.68 -49.12
REMARK 500 ILE C 63 -80.10 -106.37
REMARK 500 VAL C 110 -73.44 -51.44
REMARK 500 THR C 115 -175.86 -172.18
REMARK 500 ASN D 30 -73.64 -58.23
REMARK 500 GLU D 144 -70.56 -70.90
REMARK 500 ILE D 148 75.39 46.00
REMARK 500 LEU D 215 115.69 -173.54
REMARK 500 ASN E 28 -70.52 -49.16
REMARK 500 PRO E 147 -165.87 -67.85
REMARK 500 ASP E 148 -18.52 -48.95
REMARK 500 LYS F 61 -0.95 60.77
REMARK 500 ALA F 164 -70.37 -57.54
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 ASN D 31 THR D 32 140.05
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4Y66 A 1 203 UNP E2RTU1 E2RTU1_GIAIC 1 203
DBREF 4Y66 B 1 231 UNP V6TR15 V6TR15_GIAIN 1 231
DBREF 4Y66 C 1 203 UNP E2RTU1 E2RTU1_GIAIC 1 203
DBREF 4Y66 D 1 231 UNP V6TR15 V6TR15_GIAIN 1 231
DBREF 4Y66 E 1 203 UNP E2RTU1 E2RTU1_GIAIC 1 203
DBREF 4Y66 F 1 231 UNP V6TR15 V6TR15_GIAIN 1 231
SEQRES 1 A 203 MET ALA PRO LYS GLY THR SER LEU ASP GLU LYS LYS GLU
SEQRES 2 A 203 ARG LEU LEU GLU GLU MET LEU LYS ARG GLY GLU ILE TYR
SEQRES 3 A 203 SER ASN LYS THR ILE GLU THR LEU SER LYS PRO THR GLY
SEQRES 4 A 203 ILE SER SER MET VAL ILE LYS ASN VAL LEU GLN ALA LEU
SEQRES 5 A 203 VAL ASN GLU ASP LEU VAL ASP THR ASP LYS ILE GLY ALA
SEQRES 6 A 203 SER THR TYR TYR TRP CYS PHE ALA SER LYS ARG SER GLN
SEQRES 7 A 203 ALA ALA ARG THR GLU LEU ALA ARG LEU GLN LYS ALA LEU
SEQRES 8 A 203 GLU GLU GLN THR ASN PHE ILE ASP LYS ALA THR ALA ARG
SEQRES 9 A 203 ILE GLU GLU LEU LYS VAL GLY ARG GLU GLU THR GLU GLU
SEQRES 10 A 203 ARG SER SER LEU LEU LYS GLU LYS LEU ALA LEU GLN VAL
SEQRES 11 A 203 LYS LEU GLU GLU GLN ARG GLY THR PHE ARG ASP LEU LEU
SEQRES 12 A 203 LYS ASN ASP PRO ASP VAL ALA GLN LYS LEU ARG ASN TYR
SEQRES 13 A 203 THR ASP ILE ALA LYS GLN GLU ALA ASN LEU TRP THR ASP
SEQRES 14 A 203 ASN ILE PHE CYS LEU GLN LYS TYR MET LEU THR LYS LEU
SEQRES 15 A 203 GLN MET ASP LYS LYS THR VAL SER THR ALA LEU GLY ILE
SEQRES 16 A 203 THR GLY GLU PHE ASP TYR LEU GLU
SEQRES 1 B 231 MET ALA ALA ALA TYR LYS GLU ALA PHE ALA ALA VAL LYS
SEQRES 2 B 231 GLU LEU MET GLN THR SER ASN LYS PRO GLN ASN VAL GLN
SEQRES 3 B 231 THR ALA ILE ASN ASN THR GLY SER LYS TYR GLY LYS THR
SEQRES 4 B 231 THR VAL GLN LYS ALA LEU ASP GLU LEU VAL ALA GLN ASN
SEQRES 5 B 231 LEU CYS ILE TYR THR GLU ILE GLY LYS THR GLY LYS LEU
SEQRES 6 B 231 TYR LEU TRP ASN GLN ASN LEU LEU GLU VAL LEU SER ASP
SEQRES 7 B 231 ALA GLN LEU MET GLU VAL ASN ALA GLN ILE ASN ASP LEU
SEQRES 8 B 231 LYS ALA GLN VAL GLU LYS LEU THR GLN GLN GLY GLU THR
SEQRES 9 B 231 LEU ARG ILE THR GLN ARG ASN LEU GLU ALA ALA PRO ILE
SEQRES 10 B 231 THR GLU VAL LEU LYS GLN GLU VAL ASP GLU LEU ARG GLN
SEQRES 11 B 231 GLN VAL SER ALA ASN ASP GLU LYS LEU ARG LEU VAL ARG
SEQRES 12 B 231 GLU SER ASN ALA ILE VAL SER ASP ALA ASP MET LEU THR
SEQRES 13 B 231 LEU GLN LYS ASN TYR LYS ASP ALA MET THR ALA TRP ALA
SEQRES 14 B 231 THR ARG ARG ALA LYS CYS ARG GLU VAL ILE ASP THR LEU
SEQRES 15 B 231 SER GLU GLY MET GLY VAL LYS PRO SER ALA PHE MET ASP
SEQRES 16 B 231 GLN LEU GLY LEU GLU GLU GLY LEU PRO MET THR THR TYR
SEQRES 17 B 231 THR GLU MET LYS LYS ALA LEU PRO PRO VAL ASN VAL SER
SEQRES 18 B 231 LYS ALA ASP ILE LYS ALA ALA LEU LYS LYS
SEQRES 1 C 203 MET ALA PRO LYS GLY THR SER LEU ASP GLU LYS LYS GLU
SEQRES 2 C 203 ARG LEU LEU GLU GLU MET LEU LYS ARG GLY GLU ILE TYR
SEQRES 3 C 203 SER ASN LYS THR ILE GLU THR LEU SER LYS PRO THR GLY
SEQRES 4 C 203 ILE SER SER MET VAL ILE LYS ASN VAL LEU GLN ALA LEU
SEQRES 5 C 203 VAL ASN GLU ASP LEU VAL ASP THR ASP LYS ILE GLY ALA
SEQRES 6 C 203 SER THR TYR TYR TRP CYS PHE ALA SER LYS ARG SER GLN
SEQRES 7 C 203 ALA ALA ARG THR GLU LEU ALA ARG LEU GLN LYS ALA LEU
SEQRES 8 C 203 GLU GLU GLN THR ASN PHE ILE ASP LYS ALA THR ALA ARG
SEQRES 9 C 203 ILE GLU GLU LEU LYS VAL GLY ARG GLU GLU THR GLU GLU
SEQRES 10 C 203 ARG SER SER LEU LEU LYS GLU LYS LEU ALA LEU GLN VAL
SEQRES 11 C 203 LYS LEU GLU GLU GLN ARG GLY THR PHE ARG ASP LEU LEU
SEQRES 12 C 203 LYS ASN ASP PRO ASP VAL ALA GLN LYS LEU ARG ASN TYR
SEQRES 13 C 203 THR ASP ILE ALA LYS GLN GLU ALA ASN LEU TRP THR ASP
SEQRES 14 C 203 ASN ILE PHE CYS LEU GLN LYS TYR MET LEU THR LYS LEU
SEQRES 15 C 203 GLN MET ASP LYS LYS THR VAL SER THR ALA LEU GLY ILE
SEQRES 16 C 203 THR GLY GLU PHE ASP TYR LEU GLU
SEQRES 1 D 231 MET ALA ALA ALA TYR LYS GLU ALA PHE ALA ALA VAL LYS
SEQRES 2 D 231 GLU LEU MET GLN THR SER ASN LYS PRO GLN ASN VAL GLN
SEQRES 3 D 231 THR ALA ILE ASN ASN THR GLY SER LYS TYR GLY LYS THR
SEQRES 4 D 231 THR VAL GLN LYS ALA LEU ASP GLU LEU VAL ALA GLN ASN
SEQRES 5 D 231 LEU CYS ILE TYR THR GLU ILE GLY LYS THR GLY LYS LEU
SEQRES 6 D 231 TYR LEU TRP ASN GLN ASN LEU LEU GLU VAL LEU SER ASP
SEQRES 7 D 231 ALA GLN LEU MET GLU VAL ASN ALA GLN ILE ASN ASP LEU
SEQRES 8 D 231 LYS ALA GLN VAL GLU LYS LEU THR GLN GLN GLY GLU THR
SEQRES 9 D 231 LEU ARG ILE THR GLN ARG ASN LEU GLU ALA ALA PRO ILE
SEQRES 10 D 231 THR GLU VAL LEU LYS GLN GLU VAL ASP GLU LEU ARG GLN
SEQRES 11 D 231 GLN VAL SER ALA ASN ASP GLU LYS LEU ARG LEU VAL ARG
SEQRES 12 D 231 GLU SER ASN ALA ILE VAL SER ASP ALA ASP MET LEU THR
SEQRES 13 D 231 LEU GLN LYS ASN TYR LYS ASP ALA MET THR ALA TRP ALA
SEQRES 14 D 231 THR ARG ARG ALA LYS CYS ARG GLU VAL ILE ASP THR LEU
SEQRES 15 D 231 SER GLU GLY MET GLY VAL LYS PRO SER ALA PHE MET ASP
SEQRES 16 D 231 GLN LEU GLY LEU GLU GLU GLY LEU PRO MET THR THR TYR
SEQRES 17 D 231 THR GLU MET LYS LYS ALA LEU PRO PRO VAL ASN VAL SER
SEQRES 18 D 231 LYS ALA ASP ILE LYS ALA ALA LEU LYS LYS
SEQRES 1 E 203 MET ALA PRO LYS GLY THR SER LEU ASP GLU LYS LYS GLU
SEQRES 2 E 203 ARG LEU LEU GLU GLU MET LEU LYS ARG GLY GLU ILE TYR
SEQRES 3 E 203 SER ASN LYS THR ILE GLU THR LEU SER LYS PRO THR GLY
SEQRES 4 E 203 ILE SER SER MET VAL ILE LYS ASN VAL LEU GLN ALA LEU
SEQRES 5 E 203 VAL ASN GLU ASP LEU VAL ASP THR ASP LYS ILE GLY ALA
SEQRES 6 E 203 SER THR TYR TYR TRP CYS PHE ALA SER LYS ARG SER GLN
SEQRES 7 E 203 ALA ALA ARG THR GLU LEU ALA ARG LEU GLN LYS ALA LEU
SEQRES 8 E 203 GLU GLU GLN THR ASN PHE ILE ASP LYS ALA THR ALA ARG
SEQRES 9 E 203 ILE GLU GLU LEU LYS VAL GLY ARG GLU GLU THR GLU GLU
SEQRES 10 E 203 ARG SER SER LEU LEU LYS GLU LYS LEU ALA LEU GLN VAL
SEQRES 11 E 203 LYS LEU GLU GLU GLN ARG GLY THR PHE ARG ASP LEU LEU
SEQRES 12 E 203 LYS ASN ASP PRO ASP VAL ALA GLN LYS LEU ARG ASN TYR
SEQRES 13 E 203 THR ASP ILE ALA LYS GLN GLU ALA ASN LEU TRP THR ASP
SEQRES 14 E 203 ASN ILE PHE CYS LEU GLN LYS TYR MET LEU THR LYS LEU
SEQRES 15 E 203 GLN MET ASP LYS LYS THR VAL SER THR ALA LEU GLY ILE
SEQRES 16 E 203 THR GLY GLU PHE ASP TYR LEU GLU
SEQRES 1 F 231 MET ALA ALA ALA TYR LYS GLU ALA PHE ALA ALA VAL LYS
SEQRES 2 F 231 GLU LEU MET GLN THR SER ASN LYS PRO GLN ASN VAL GLN
SEQRES 3 F 231 THR ALA ILE ASN ASN THR GLY SER LYS TYR GLY LYS THR
SEQRES 4 F 231 THR VAL GLN LYS ALA LEU ASP GLU LEU VAL ALA GLN ASN
SEQRES 5 F 231 LEU CYS ILE TYR THR GLU ILE GLY LYS THR GLY LYS LEU
SEQRES 6 F 231 TYR LEU TRP ASN GLN ASN LEU LEU GLU VAL LEU SER ASP
SEQRES 7 F 231 ALA GLN LEU MET GLU VAL ASN ALA GLN ILE ASN ASP LEU
SEQRES 8 F 231 LYS ALA GLN VAL GLU LYS LEU THR GLN GLN GLY GLU THR
SEQRES 9 F 231 LEU ARG ILE THR GLN ARG ASN LEU GLU ALA ALA PRO ILE
SEQRES 10 F 231 THR GLU VAL LEU LYS GLN GLU VAL ASP GLU LEU ARG GLN
SEQRES 11 F 231 GLN VAL SER ALA ASN ASP GLU LYS LEU ARG LEU VAL ARG
SEQRES 12 F 231 GLU SER ASN ALA ILE VAL SER ASP ALA ASP MET LEU THR
SEQRES 13 F 231 LEU GLN LYS ASN TYR LYS ASP ALA MET THR ALA TRP ALA
SEQRES 14 F 231 THR ARG ARG ALA LYS CYS ARG GLU VAL ILE ASP THR LEU
SEQRES 15 F 231 SER GLU GLY MET GLY VAL LYS PRO SER ALA PHE MET ASP
SEQRES 16 F 231 GLN LEU GLY LEU GLU GLU GLY LEU PRO MET THR THR TYR
SEQRES 17 F 231 THR GLU MET LYS LYS ALA LEU PRO PRO VAL ASN VAL SER
SEQRES 18 F 231 LYS ALA ASP ILE LYS ALA ALA LEU LYS LYS
HELIX 1 AA1 ARG A 76 LYS A 109 1 34
HELIX 2 AA2 THR A 115 LYS A 144 1 30
HELIX 3 AA3 ASP A 146 LYS A 181 1 36
HELIX 4 AA4 ASP A 185 GLY A 194 1 10
HELIX 5 AA5 LEU B 81 ALA B 114 1 34
HELIX 6 AA6 GLU B 119 SER B 145 1 27
HELIX 7 AA7 SER B 150 MET B 186 1 37
HELIX 8 AA8 LYS B 189 GLY B 198 1 10
HELIX 9 AA9 PRO B 204 LEU B 215 1 12
HELIX 10 AB1 SER B 221 LEU B 229 1 9
HELIX 11 AB2 SER C 7 GLY C 23 1 17
HELIX 12 AB3 LYS C 29 THR C 33 5 5
HELIX 13 AB4 LEU C 34 GLY C 39 1 6
HELIX 14 AB5 VAL C 44 GLU C 55 1 12
HELIX 15 AB6 SER C 74 VAL C 110 1 37
HELIX 16 AB7 THR C 115 ASN C 145 1 31
HELIX 17 AB8 ASP C 146 THR C 180 1 35
HELIX 18 AB9 ASP C 185 GLY C 194 1 10
HELIX 19 AC1 PHE D 9 GLN D 17 1 9
HELIX 20 AC2 ASN D 24 ASN D 31 1 8
HELIX 21 AC3 LYS D 38 GLN D 51 1 14
HELIX 22 AC4 GLN D 70 LEU D 73 5 4
HELIX 23 AC5 ALA D 79 ALA D 114 1 36
HELIX 24 AC6 ILE D 117 ASN D 146 1 30
HELIX 25 AC7 SER D 150 MET D 186 1 37
HELIX 26 AC8 LYS D 189 GLY D 198 1 10
HELIX 27 AC9 MET D 205 ALA D 214 1 10
HELIX 28 AD1 GLU E 10 ARG E 22 1 13
HELIX 29 AD2 LYS E 29 THR E 33 5 5
HELIX 30 AD3 VAL E 44 GLU E 55 1 12
HELIX 31 AD4 SER E 74 ARG E 112 1 39
HELIX 32 AD5 THR E 115 ASN E 145 1 31
HELIX 33 AD6 PRO E 147 GLU E 163 1 17
HELIX 34 AD7 ALA F 4 SER F 19 1 16
HELIX 35 AD8 ASN F 24 THR F 32 1 9
HELIX 36 AD9 GLY F 37 GLN F 51 1 15
HELIX 37 AE1 GLN F 70 LEU F 73 5 4
HELIX 38 AE2 SER F 77 GLU F 113 1 37
HELIX 39 AE3 ILE F 117 LEU F 141 1 25
HELIX 40 AE4 MET F 154 MET F 165 1 12
HELIX 41 AE5 THR F 206 LEU F 215 1 10
SHEET 1 AA1 2 ASP C 59 LYS C 62 0
SHEET 2 AA1 2 THR C 67 TRP C 70 -1 O TYR C 68 N ASP C 61
SHEET 1 AA2 2 CYS D 54 ILE D 55 0
SHEET 2 AA2 2 LEU D 67 TRP D 68 -1 O LEU D 67 N ILE D 55
SHEET 1 AA3 3 TYR E 26 SER E 27 0
SHEET 2 AA3 3 TYR E 68 TRP E 70 -1 O TYR E 69 N TYR E 26
SHEET 3 AA3 3 ASP E 59 ASP E 61 -1 N ASP E 61 O TYR E 68
SHEET 1 AA4 3 PRO F 22 GLN F 23 0
SHEET 2 AA4 3 GLY F 63 TRP F 68 -1 O TYR F 66 N GLN F 23
SHEET 3 AA4 3 CYS F 54 ILE F 59 -1 N THR F 57 O LEU F 65
CISPEP 1 THR D 32 GLY D 33 0 7.10
CRYST1 117.847 69.066 292.137 90.00 95.34 90.00 C 1 2 1 12
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 0.008486 0.000000 0.000794 0.00000
SCALE2 0.000000 0.014479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003438 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
