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HEADER LIPID BINDING PROTEIN 09-OCT-24 9H0Z
TITLE CRYSTAL STRUCTURE OF TTL[NLE], THERMOPHILIC LIPASE TTL FROM
TITLE 2 THERMOANAEROBACTER THERMOHYDROSULFURICUS CONTAINING NON-CANONICAL
TITLE 3 AMINO ACID NLE AT THE POSITION OF MET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE AMINOPEPTIDASE S33 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER THERMOHYDROSULFURICUS;
SOURCE 3 ORGANISM_TAXID: 1516;
SOURCE 4 GENE: SAMN04244560_02687;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, THERMOPHILIC, NON-CANONICAL AMINO ACID, NLE, NCAAS,
KEYWDS 2 NORLEUCINE, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HROMIC-JAHJEFENDIC,T.PAVKOV-KELLER,B.WILTSCHI,K.GRUBER
REVDAT 1 29-OCT-25 9H0Z 0
JRNL AUTH A.HROMIC-JAHJEFENDIC,T.PAVKOV-KELLER,K.GRUBER,B.WILTSCHI
JRNL TITL NCAA INCORPORATION, LIPASE AND OYE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 45693
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2264
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 54.8900 - 7.0200 0.99 2819 149 0.1875 0.2378
REMARK 3 2 7.0200 - 5.5800 1.00 2764 131 0.2110 0.2244
REMARK 3 3 5.5800 - 4.8700 1.00 2772 134 0.1754 0.2134
REMARK 3 4 4.8700 - 4.4300 1.00 2733 149 0.1579 0.1842
REMARK 3 5 4.4300 - 4.1100 1.00 2737 132 0.1703 0.2022
REMARK 3 6 4.1100 - 3.8700 1.00 2697 154 0.1992 0.2804
REMARK 3 7 3.8700 - 3.6700 1.00 2724 149 0.2205 0.2718
REMARK 3 8 3.6700 - 3.5100 1.00 2718 173 0.2213 0.2970
REMARK 3 9 3.5100 - 3.3800 1.00 2692 142 0.2354 0.3057
REMARK 3 10 3.3800 - 3.2600 1.00 2716 129 0.2516 0.3286
REMARK 3 11 3.2600 - 3.1600 1.00 2728 162 0.2683 0.3429
REMARK 3 12 3.1600 - 3.0700 1.00 2701 120 0.2731 0.3356
REMARK 3 13 3.0700 - 2.9900 1.00 2722 147 0.2722 0.2856
REMARK 3 14 2.9900 - 2.9200 1.00 2705 124 0.2833 0.3422
REMARK 3 15 2.9200 - 2.8500 1.00 2709 146 0.2888 0.3366
REMARK 3 16 2.8500 - 2.7900 0.92 2492 123 0.3012 0.3946
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) : 0.423
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.335
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.45
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 : 0.003 12225
REMARK 3 ANGLE : 0.590 16404
REMARK 3 CHIRALITY : 0.043 1791
REMARK 3 PLANARITY : 0.003 2092
REMARK 3 DIHEDRAL : 4.085 8281
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 9H0Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-OCT-24.
REMARK 100 THE DEPOSITION ID IS D_1292142283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45722
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.790
REMARK 200 RESOLUTION RANGE LOW (A) : 54.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.77900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.560
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8MG/ML PROTEIN CONCENTRATION INDEX
REMARK 280 SCREEN CONDITION D4 CONTAINING 0.1 M CITRIC ACID PH 3.5, 25% W/V
REMARK 280 POLYETHYLENE GLYCOL 3,350 DROPS: 0.5UL + 0.5UL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.14850
REMARK 290 SMTRY3 2 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: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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: 2860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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: 2870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 LYS A 258
REMARK 465 GLY A 259
REMARK 465 GLY A 260
REMARK 465 SER A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 LYS B 258
REMARK 465 GLY B 259
REMARK 465 GLY B 260
REMARK 465 SER B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 GLU C 149
REMARK 465 SER C 150
REMARK 465 VAL C 151
REMARK 465 LYS C 152
REMARK 465 GLN C 153
REMARK 465 TYR C 154
REMARK 465 GLY C 155
REMARK 465 ALA C 156
REMARK 465 ILE C 157
REMARK 465 NLE C 158
REMARK 465 GLU C 159
REMARK 465 GLY C 260
REMARK 465 SER C 261
REMARK 465 HIS C 262
REMARK 465 HIS C 263
REMARK 465 HIS C 264
REMARK 465 HIS C 265
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 ILE D 146
REMARK 465 NLE D 147
REMARK 465 ASN D 148
REMARK 465 GLU D 149
REMARK 465 SER D 150
REMARK 465 VAL D 151
REMARK 465 LYS D 152
REMARK 465 GLN D 153
REMARK 465 TYR D 154
REMARK 465 GLY D 155
REMARK 465 LYS D 258
REMARK 465 GLY D 259
REMARK 465 GLY D 260
REMARK 465 SER D 261
REMARK 465 HIS D 262
REMARK 465 HIS D 263
REMARK 465 HIS D 264
REMARK 465 HIS D 265
REMARK 465 HIS D 266
REMARK 465 HIS D 267
REMARK 465 GLN E 153
REMARK 465 TYR E 154
REMARK 465 GLY E 155
REMARK 465 ALA E 156
REMARK 465 ILE E 157
REMARK 465 NLE E 158
REMARK 465 GLU E 159
REMARK 465 GLN E 160
REMARK 465 LYS E 258
REMARK 465 GLY E 259
REMARK 465 GLY E 260
REMARK 465 SER E 261
REMARK 465 HIS E 262
REMARK 465 HIS E 263
REMARK 465 HIS E 264
REMARK 465 HIS E 265
REMARK 465 HIS E 266
REMARK 465 HIS E 267
REMARK 465 VAL F 151
REMARK 465 LYS F 152
REMARK 465 GLN F 153
REMARK 465 TYR F 154
REMARK 465 LYS F 258
REMARK 465 GLY F 259
REMARK 465 GLY F 260
REMARK 465 SER F 261
REMARK 465 HIS F 262
REMARK 465 HIS F 263
REMARK 465 HIS F 264
REMARK 465 HIS F 265
REMARK 465 HIS F 266
REMARK 465 HIS F 267
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 C 258 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 OE2 GLU F 177 O HOH F 401 1.86
REMARK 500 OG SER E 70 O HOH E 401 1.88
REMARK 500 O HOH F 416 O HOH F 419 1.91
REMARK 500 O GLU E 246 O HOH E 402 1.92
REMARK 500 OD1 ASP F 23 O HOH F 402 1.98
REMARK 500 N GLU E 250 O HOH E 402 1.99
REMARK 500 OD2 ASP F 88 O HOH F 403 2.00
REMARK 500 O NLE C 33 O HOH C 401 2.00
REMARK 500 O LEU F 145 OE1 GLU F 149 2.01
REMARK 500 O GLU E 229 O HOH E 403 2.03
REMARK 500 O ASN F 230 O HOH F 404 2.04
REMARK 500 OG SER B 70 O HOH B 401 2.09
REMARK 500 OE2 GLU D 246 O HOH D 401 2.11
REMARK 500 NZ LYS A 27 O HOH A 401 2.12
REMARK 500 O HOH E 410 O HOH F 420 2.12
REMARK 500 NZ LYS F 41 O HOH F 405 2.17
REMARK 500 O ASN A 148 O HOH A 402 2.17
REMARK 500 O HOH C 410 O HOH C 426 2.18
REMARK 500 OD1 ASP A 178 O HOH A 403 2.18
REMARK 500 O NLE F 33 O HOH F 406 2.18
REMARK 500 O HOH D 414 O HOH D 422 2.18
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 NH2 ARG A 90 O ASP C 23 1545 2.17
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 ASN A 10 -132.11 57.16
REMARK 500 GLU A 43 -177.20 65.55
REMARK 500 HIS A 45 42.59 37.20
REMARK 500 SER A 113 -101.67 48.93
REMARK 500 ALA A 139 59.17 -91.42
REMARK 500 TYR A 154 -14.74 69.28
REMARK 500 ASN A 202 58.77 -96.78
REMARK 500 ASN A 230 -1.44 69.20
REMARK 500 GLU B 43 179.42 61.69
REMARK 500 HIS B 45 39.32 36.34
REMARK 500 SER B 113 -112.89 58.82
REMARK 500 TYR B 126 66.52 -119.61
REMARK 500 GLN B 153 -31.90 -156.54
REMARK 500 GLU C 43 179.70 58.84
REMARK 500 HIS C 45 37.93 38.13
REMARK 500 SER C 113 -105.54 56.61
REMARK 500 ALA C 139 49.15 -86.73
REMARK 500 ILE C 166 70.91 -105.88
REMARK 500 ASN C 230 -3.52 74.80
REMARK 500 ASP C 232 -164.33 -110.57
REMARK 500 PHE C 235 75.98 63.73
REMARK 500 PRO D 29 153.55 -49.36
REMARK 500 GLU D 43 -176.93 66.11
REMARK 500 HIS D 45 40.01 35.48
REMARK 500 SER D 113 -116.39 58.55
REMARK 500 LYS D 181 30.12 -95.98
REMARK 500 GLU E 43 -178.65 59.93
REMARK 500 ARG E 106 48.40 -141.62
REMARK 500 SER E 113 -110.08 52.99
REMARK 500 ASN E 230 -7.04 73.25
REMARK 500 SER E 237 145.68 -171.33
REMARK 500 ASN F 10 -144.32 53.15
REMARK 500 GLU F 43 175.46 71.12
REMARK 500 HIS F 45 35.76 38.44
REMARK 500 SER F 113 -114.81 57.57
REMARK 500 LYS F 181 21.47 -77.88
REMARK 500 ASN F 230 -1.61 69.29
REMARK 500 SER F 237 141.43 -173.68
REMARK 500 LEU F 256 -71.24 -93.53
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9H0Z A 1 259 UNP A0A1G7VV58_THETY
DBREF2 9H0Z A A0A1G7VV58 1 259
DBREF1 9H0Z B 1 259 UNP A0A1G7VV58_THETY
DBREF2 9H0Z B A0A1G7VV58 1 259
DBREF1 9H0Z C 1 259 UNP A0A1G7VV58_THETY
DBREF2 9H0Z C A0A1G7VV58 1 259
DBREF1 9H0Z D 1 259 UNP A0A1G7VV58_THETY
DBREF2 9H0Z D A0A1G7VV58 1 259
DBREF1 9H0Z E 1 259 UNP A0A1G7VV58_THETY
DBREF2 9H0Z E A0A1G7VV58 1 259
DBREF1 9H0Z F 1 259 UNP A0A1G7VV58_THETY
DBREF2 9H0Z F A0A1G7VV58 1 259
SEQADV 9H0Z NLE A 1 UNP A0A1G7VV5 MET 1 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 17 UNP A0A1G7VV5 MET 17 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 18 UNP A0A1G7VV5 MET 18 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 30 UNP A0A1G7VV5 MET 30 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 33 UNP A0A1G7VV5 MET 33 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 51 UNP A0A1G7VV5 MET 51 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 80 UNP A0A1G7VV5 MET 80 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 114 UNP A0A1G7VV5 MET 114 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 142 UNP A0A1G7VV5 MET 142 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 147 UNP A0A1G7VV5 MET 147 ENGINEERED MUTATION
SEQADV 9H0Z ASN A 148 UNP A0A1G7VV5 HIS 148 ENGINEERED MUTATION
SEQADV 9H0Z NLE A 158 UNP A0A1G7VV5 MET 158 ENGINEERED MUTATION
SEQADV 9H0Z GLY A 260 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z SER A 261 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS A 262 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS A 263 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS A 264 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS A 265 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS A 266 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS A 267 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z NLE B 1 UNP A0A1G7VV5 MET 1 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 17 UNP A0A1G7VV5 MET 17 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 18 UNP A0A1G7VV5 MET 18 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 30 UNP A0A1G7VV5 MET 30 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 33 UNP A0A1G7VV5 MET 33 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 51 UNP A0A1G7VV5 MET 51 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 80 UNP A0A1G7VV5 MET 80 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 114 UNP A0A1G7VV5 MET 114 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 142 UNP A0A1G7VV5 MET 142 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 147 UNP A0A1G7VV5 MET 147 ENGINEERED MUTATION
SEQADV 9H0Z ASN B 148 UNP A0A1G7VV5 HIS 148 ENGINEERED MUTATION
SEQADV 9H0Z NLE B 158 UNP A0A1G7VV5 MET 158 ENGINEERED MUTATION
SEQADV 9H0Z GLY B 260 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z SER B 261 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS B 262 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS B 263 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS B 264 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS B 265 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS B 266 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS B 267 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z NLE C 1 UNP A0A1G7VV5 MET 1 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 17 UNP A0A1G7VV5 MET 17 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 18 UNP A0A1G7VV5 MET 18 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 30 UNP A0A1G7VV5 MET 30 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 33 UNP A0A1G7VV5 MET 33 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 51 UNP A0A1G7VV5 MET 51 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 80 UNP A0A1G7VV5 MET 80 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 114 UNP A0A1G7VV5 MET 114 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 142 UNP A0A1G7VV5 MET 142 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 147 UNP A0A1G7VV5 MET 147 ENGINEERED MUTATION
SEQADV 9H0Z ASN C 148 UNP A0A1G7VV5 HIS 148 ENGINEERED MUTATION
SEQADV 9H0Z NLE C 158 UNP A0A1G7VV5 MET 158 ENGINEERED MUTATION
SEQADV 9H0Z GLY C 260 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z SER C 261 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS C 262 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS C 263 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS C 264 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS C 265 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS C 266 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS C 267 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z NLE D 1 UNP A0A1G7VV5 MET 1 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 17 UNP A0A1G7VV5 MET 17 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 18 UNP A0A1G7VV5 MET 18 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 30 UNP A0A1G7VV5 MET 30 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 33 UNP A0A1G7VV5 MET 33 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 51 UNP A0A1G7VV5 MET 51 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 80 UNP A0A1G7VV5 MET 80 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 114 UNP A0A1G7VV5 MET 114 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 142 UNP A0A1G7VV5 MET 142 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 147 UNP A0A1G7VV5 MET 147 ENGINEERED MUTATION
SEQADV 9H0Z ASN D 148 UNP A0A1G7VV5 HIS 148 ENGINEERED MUTATION
SEQADV 9H0Z NLE D 158 UNP A0A1G7VV5 MET 158 ENGINEERED MUTATION
SEQADV 9H0Z GLY D 260 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z SER D 261 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS D 262 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS D 263 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS D 264 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS D 265 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS D 266 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS D 267 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z NLE E 1 UNP A0A1G7VV5 MET 1 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 17 UNP A0A1G7VV5 MET 17 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 18 UNP A0A1G7VV5 MET 18 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 30 UNP A0A1G7VV5 MET 30 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 33 UNP A0A1G7VV5 MET 33 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 51 UNP A0A1G7VV5 MET 51 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 80 UNP A0A1G7VV5 MET 80 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 114 UNP A0A1G7VV5 MET 114 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 142 UNP A0A1G7VV5 MET 142 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 147 UNP A0A1G7VV5 MET 147 ENGINEERED MUTATION
SEQADV 9H0Z ASN E 148 UNP A0A1G7VV5 HIS 148 ENGINEERED MUTATION
SEQADV 9H0Z NLE E 158 UNP A0A1G7VV5 MET 158 ENGINEERED MUTATION
SEQADV 9H0Z GLY E 260 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z SER E 261 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS E 262 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS E 263 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS E 264 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS E 265 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS E 266 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS E 267 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z NLE F 1 UNP A0A1G7VV5 MET 1 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 17 UNP A0A1G7VV5 MET 17 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 18 UNP A0A1G7VV5 MET 18 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 30 UNP A0A1G7VV5 MET 30 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 33 UNP A0A1G7VV5 MET 33 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 51 UNP A0A1G7VV5 MET 51 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 80 UNP A0A1G7VV5 MET 80 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 114 UNP A0A1G7VV5 MET 114 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 142 UNP A0A1G7VV5 MET 142 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 147 UNP A0A1G7VV5 MET 147 ENGINEERED MUTATION
SEQADV 9H0Z ASN F 148 UNP A0A1G7VV5 HIS 148 ENGINEERED MUTATION
SEQADV 9H0Z NLE F 158 UNP A0A1G7VV5 MET 158 ENGINEERED MUTATION
SEQADV 9H0Z GLY F 260 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z SER F 261 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS F 262 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS F 263 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS F 264 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS F 265 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS F 266 UNP A0A1G7VV5 EXPRESSION TAG
SEQADV 9H0Z HIS F 267 UNP A0A1G7VV5 EXPRESSION TAG
SEQRES 1 A 267 NLE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 A 267 LEU ARG GLY NLE NLE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 A 267 LYS VAL PRO NLE VAL ILE NLE PHE HIS GLY PHE THR GLY
SEQRES 4 A 267 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS NLE SER
SEQRES 5 A 267 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 A 267 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 A 267 GLU NLE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 A 267 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 A 267 GLU ARG ILE GLY LEU LEU GLY LEU SER NLE GLY GLY ALA
SEQRES 10 A 267 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 A 267 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN NLE PRO
SEQRES 12 A 267 GLU LEU ILE NLE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 A 267 ILE NLE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 A 267 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 A 267 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 A 267 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 A 267 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 A 267 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 A 267 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 A 267 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY GLY
SEQRES 21 A 267 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 NLE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 B 267 LEU ARG GLY NLE NLE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 B 267 LYS VAL PRO NLE VAL ILE NLE PHE HIS GLY PHE THR GLY
SEQRES 4 B 267 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS NLE SER
SEQRES 5 B 267 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 B 267 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 B 267 GLU NLE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 B 267 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 B 267 GLU ARG ILE GLY LEU LEU GLY LEU SER NLE GLY GLY ALA
SEQRES 10 B 267 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 B 267 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN NLE PRO
SEQRES 12 B 267 GLU LEU ILE NLE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 B 267 ILE NLE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 B 267 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 B 267 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 B 267 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 B 267 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 B 267 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 B 267 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 B 267 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY GLY
SEQRES 21 B 267 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 267 NLE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 C 267 LEU ARG GLY NLE NLE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 C 267 LYS VAL PRO NLE VAL ILE NLE PHE HIS GLY PHE THR GLY
SEQRES 4 C 267 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS NLE SER
SEQRES 5 C 267 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 C 267 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 C 267 GLU NLE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 C 267 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 C 267 GLU ARG ILE GLY LEU LEU GLY LEU SER NLE GLY GLY ALA
SEQRES 10 C 267 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 C 267 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN NLE PRO
SEQRES 12 C 267 GLU LEU ILE NLE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 C 267 ILE NLE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 C 267 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 C 267 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 C 267 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 C 267 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 C 267 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 C 267 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 C 267 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY GLY
SEQRES 21 C 267 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 267 NLE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 D 267 LEU ARG GLY NLE NLE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 D 267 LYS VAL PRO NLE VAL ILE NLE PHE HIS GLY PHE THR GLY
SEQRES 4 D 267 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS NLE SER
SEQRES 5 D 267 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 D 267 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 D 267 GLU NLE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 D 267 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 D 267 GLU ARG ILE GLY LEU LEU GLY LEU SER NLE GLY GLY ALA
SEQRES 10 D 267 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 D 267 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN NLE PRO
SEQRES 12 D 267 GLU LEU ILE NLE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 D 267 ILE NLE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 D 267 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 D 267 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 D 267 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 D 267 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 D 267 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 D 267 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 D 267 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY GLY
SEQRES 21 D 267 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 267 NLE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 E 267 LEU ARG GLY NLE NLE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 E 267 LYS VAL PRO NLE VAL ILE NLE PHE HIS GLY PHE THR GLY
SEQRES 4 E 267 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS NLE SER
SEQRES 5 E 267 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 E 267 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 E 267 GLU NLE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 E 267 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 E 267 GLU ARG ILE GLY LEU LEU GLY LEU SER NLE GLY GLY ALA
SEQRES 10 E 267 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 E 267 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN NLE PRO
SEQRES 12 E 267 GLU LEU ILE NLE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 E 267 ILE NLE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 E 267 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 E 267 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 E 267 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 E 267 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 E 267 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 E 267 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 E 267 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY GLY
SEQRES 21 E 267 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 267 NLE GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 F 267 LEU ARG GLY NLE NLE HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 F 267 LYS VAL PRO NLE VAL ILE NLE PHE HIS GLY PHE THR GLY
SEQRES 4 F 267 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS NLE SER
SEQRES 5 F 267 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 F 267 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 F 267 GLU NLE THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 F 267 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 F 267 GLU ARG ILE GLY LEU LEU GLY LEU SER NLE GLY GLY ALA
SEQRES 10 F 267 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 F 267 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN NLE PRO
SEQRES 12 F 267 GLU LEU ILE NLE ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 F 267 ILE NLE GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 F 267 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 F 267 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 F 267 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 F 267 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 F 267 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 F 267 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 F 267 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY GLY
SEQRES 21 F 267 SER HIS HIS HIS HIS HIS HIS
HET NLE A 1 8
HET NLE A 17 8
HET NLE A 18 8
HET NLE A 30 8
HET NLE A 33 8
HET NLE A 51 8
HET NLE A 80 8
HET NLE A 114 8
HET NLE A 142 8
HET NLE A 147 8
HET NLE A 158 8
HET NLE B 1 8
HET NLE B 17 8
HET NLE B 18 8
HET NLE B 30 8
HET NLE B 33 8
HET NLE B 51 8
HET NLE B 80 8
HET NLE B 114 8
HET NLE B 142 8
HET NLE B 147 8
HET NLE B 158 8
HET NLE C 1 8
HET NLE C 17 8
HET NLE C 18 8
HET NLE C 30 8
HET NLE C 33 8
HET NLE C 51 8
HET NLE C 80 8
HET NLE C 114 8
HET NLE C 142 8
HET NLE C 147 8
HET NLE D 1 8
HET NLE D 17 8
HET NLE D 18 8
HET NLE D 30 8
HET NLE D 33 8
HET NLE D 51 8
HET NLE D 80 8
HET NLE D 114 8
HET NLE D 142 8
HET NLE D 158 8
HET NLE E 1 8
HET NLE E 17 8
HET NLE E 18 8
HET NLE E 30 8
HET NLE E 33 8
HET NLE E 51 8
HET NLE E 80 8
HET NLE E 114 8
HET NLE E 142 8
HET NLE E 147 8
HET NLE F 1 8
HET NLE F 17 8
HET NLE F 18 8
HET NLE F 30 8
HET NLE F 33 8
HET NLE F 51 8
HET NLE F 80 8
HET NLE F 114 8
HET NLE F 142 8
HET NLE F 147 8
HET NLE F 158 8
HET SO4 A 301 5
HET SO4 B 301 5
HET SO4 C 301 5
HET SO4 D 301 5
HET SO4 E 301 5
HET SO4 F 301 5
HETNAM NLE NORLEUCINE
HETNAM SO4 SULFATE ION
FORMUL 1 NLE 63(C6 H13 N O2)
FORMUL 7 SO4 6(O4 S 2-)
FORMUL 13 HOH *122(H2 O)
HELIX 1 AA1 GLU A 43 HIS A 45 5 3
HELIX 2 AA2 PHE A 46 LYS A 57 1 12
HELIX 3 AA3 ASP A 76 NLE A 80 5 5
HELIX 4 AA4 THR A 81 GLU A 98 1 18
HELIX 5 AA5 SER A 113 TYR A 126 1 14
HELIX 6 AA6 ASN A 141 LYS A 152 1 12
HELIX 7 AA7 TYR A 154 GLY A 162 1 9
HELIX 8 AA8 LYS A 173 LYS A 181 1 9
HELIX 9 AA9 ASN A 183 LYS A 189 1 7
HELIX 10 AB1 TYR A 208 VAL A 218 1 11
HELIX 11 AB2 SER A 237 LEU A 257 1 21
HELIX 12 AB3 GLU B 43 HIS B 45 5 3
HELIX 13 AB4 PHE B 46 VAL B 58 1 13
HELIX 14 AB5 ASP B 76 NLE B 80 5 5
HELIX 15 AB6 THR B 81 GLU B 98 1 18
HELIX 16 AB7 SER B 113 TYR B 126 1 14
HELIX 17 AB8 ASN B 141 GLN B 153 1 13
HELIX 18 AB9 GLN B 153 GLY B 162 1 10
HELIX 19 AC1 LYS B 173 LYS B 181 1 9
HELIX 20 AC2 ASN B 183 LYS B 189 1 7
HELIX 21 AC3 TYR B 208 VAL B 218 1 11
HELIX 22 AC4 SER B 237 LEU B 257 1 21
HELIX 23 AC5 GLU C 43 HIS C 45 5 3
HELIX 24 AC6 PHE C 46 LYS C 57 1 12
HELIX 25 AC7 ASP C 76 NLE C 80 5 5
HELIX 26 AC8 THR C 81 GLU C 98 1 18
HELIX 27 AC9 SER C 113 TYR C 126 1 14
HELIX 28 AD1 ASN C 141 ASN C 148 1 8
HELIX 29 AD2 LYS C 173 LYS C 181 1 9
HELIX 30 AD3 ASN C 183 LYS C 189 1 7
HELIX 31 AD4 LYS C 209 VAL C 218 1 10
HELIX 32 AD5 SER C 237 LEU C 257 1 21
HELIX 33 AD6 GLU D 43 HIS D 45 5 3
HELIX 34 AD7 PHE D 46 GLY D 59 1 14
HELIX 35 AD8 ASP D 76 NLE D 80 5 5
HELIX 36 AD9 THR D 81 GLU D 98 1 18
HELIX 37 AE1 SER D 113 TYR D 126 1 14
HELIX 38 AE2 ILE D 157 GLY D 162 1 6
HELIX 39 AE3 LYS D 173 LYS D 181 1 9
HELIX 40 AE4 ASN D 183 LYS D 189 1 7
HELIX 41 AE5 GLU D 207 VAL D 218 1 12
HELIX 42 AE6 SER D 237 LEU D 257 1 21
HELIX 43 AE7 GLU E 43 HIS E 45 5 3
HELIX 44 AE8 PHE E 46 GLY E 59 1 14
HELIX 45 AE9 ASP E 76 NLE E 80 5 5
HELIX 46 AF1 THR E 81 GLU E 98 1 18
HELIX 47 AF2 SER E 113 TYR E 126 1 14
HELIX 48 AF3 ASN E 141 VAL E 151 1 11
HELIX 49 AF4 LYS E 173 LYS E 181 1 9
HELIX 50 AF5 ASN E 183 LYS E 189 1 7
HELIX 51 AF6 LYS E 209 VAL E 218 1 10
HELIX 52 AF7 SER E 237 LEU E 256 1 20
HELIX 53 AF8 GLU F 43 HIS F 45 5 3
HELIX 54 AF9 PHE F 46 LYS F 57 1 12
HELIX 55 AG1 ASP F 76 NLE F 80 5 5
HELIX 56 AG2 THR F 81 GLU F 98 1 18
HELIX 57 AG3 NLE F 114 TYR F 126 1 13
HELIX 58 AG4 ASN F 141 ASN F 148 1 8
HELIX 59 AG5 ALA F 156 GLY F 162 1 7
HELIX 60 AG6 LYS F 173 ILE F 179 1 7
HELIX 61 AG7 ASN F 183 SER F 188 1 6
HELIX 62 AG8 GLU F 207 VAL F 218 1 12
HELIX 63 AG9 SER F 237 LEU F 256 1 20
SHEET 1 AA1 8 GLN A 2 TYR A 9 0
SHEET 2 AA1 8 LYS A 12 HIS A 19 -1 O LEU A 14 N ILE A 7
SHEET 3 AA1 8 GLY A 61 PHE A 65 -1 O SER A 62 N HIS A 19
SHEET 4 AA1 8 VAL A 28 PHE A 34 1 N PRO A 29 O GLY A 61
SHEET 5 AA1 8 THR A 102 LEU A 112 1 O GLY A 108 N NLE A 30
SHEET 6 AA1 8 ALA A 132 TRP A 136 1 O TRP A 136 N GLY A 111
SHEET 7 AA1 8 LYS A 194 GLY A 200 1 O LEU A 196 N LEU A 135
SHEET 8 AA1 8 ALA A 223 ILE A 228 1 O VAL A 226 N ILE A 197
SHEET 1 AA2 2 PHE A 163 ASP A 165 0
SHEET 2 AA2 2 LYS A 170 SER A 172 -1 O LEU A 171 N VAL A 164
SHEET 1 AA3 8 GLN B 2 TYR B 9 0
SHEET 2 AA3 8 LYS B 12 HIS B 19 -1 O LEU B 14 N ILE B 7
SHEET 3 AA3 8 GLY B 61 PHE B 65 -1 O SER B 62 N HIS B 19
SHEET 4 AA3 8 VAL B 28 PHE B 34 1 N NLE B 33 O VAL B 63
SHEET 5 AA3 8 THR B 102 LEU B 112 1 O LEU B 110 N PHE B 34
SHEET 6 AA3 8 ILE B 130 TRP B 136 1 O VAL B 134 N LEU B 109
SHEET 7 AA3 8 LYS B 194 GLY B 200 1 O LEU B 196 N LEU B 135
SHEET 8 AA3 8 ALA B 223 ILE B 228 1 O VAL B 226 N ILE B 197
SHEET 1 AA4 2 PHE B 163 ASP B 165 0
SHEET 2 AA4 2 LYS B 170 SER B 172 -1 O LEU B 171 N VAL B 164
SHEET 1 AA5 8 GLN C 2 TYR C 9 0
SHEET 2 AA5 8 LYS C 12 HIS C 19 -1 O NLE C 18 N LYS C 3
SHEET 3 AA5 8 GLY C 61 ASP C 66 -1 O SER C 62 N HIS C 19
SHEET 4 AA5 8 VAL C 28 PHE C 34 1 N PRO C 29 O GLY C 61
SHEET 5 AA5 8 THR C 102 LEU C 112 1 O GLY C 108 N NLE C 30
SHEET 6 AA5 8 ALA C 132 TRP C 136 1 O VAL C 134 N LEU C 109
SHEET 7 AA5 8 VAL C 195 GLY C 200 1 O LEU C 196 N LEU C 135
SHEET 8 AA5 8 ALA C 223 ILE C 228 1 O THR C 224 N ILE C 197
SHEET 1 AA6 2 PHE C 163 ASP C 165 0
SHEET 2 AA6 2 LYS C 170 SER C 172 -1 O LEU C 171 N VAL C 164
SHEET 1 AA7 8 GLN D 2 TYR D 9 0
SHEET 2 AA7 8 LYS D 12 HIS D 19 -1 O LEU D 14 N ILE D 7
SHEET 3 AA7 8 GLY D 61 ASP D 66 -1 O ARG D 64 N NLE D 17
SHEET 4 AA7 8 VAL D 28 PHE D 34 1 N PRO D 29 O GLY D 61
SHEET 5 AA7 8 THR D 102 LEU D 112 1 O GLY D 108 N NLE D 30
SHEET 6 AA7 8 ILE D 130 TRP D 136 1 O TRP D 136 N GLY D 111
SHEET 7 AA7 8 VAL D 195 VAL D 198 1 O LEU D 196 N LEU D 135
SHEET 8 AA7 8 ALA D 223 ARG D 225 1 O THR D 224 N ILE D 197
SHEET 1 AA8 2 PHE D 163 ASP D 165 0
SHEET 2 AA8 2 LYS D 170 SER D 172 -1 O LEU D 171 N VAL D 164
SHEET 1 AA9 8 GLN E 2 TYR E 9 0
SHEET 2 AA9 8 LYS E 12 HIS E 19 -1 O LEU E 14 N ILE E 7
SHEET 3 AA9 8 GLY E 61 ASP E 66 -1 O SER E 62 N HIS E 19
SHEET 4 AA9 8 VAL E 28 PHE E 34 1 N PRO E 29 O GLY E 61
SHEET 5 AA9 8 THR E 102 LEU E 112 1 O GLY E 108 N ILE E 32
SHEET 6 AA9 8 ILE E 130 TRP E 136 1 O TRP E 136 N GLY E 111
SHEET 7 AA9 8 VAL E 195 GLY E 200 1 O LEU E 196 N LEU E 135
SHEET 8 AA9 8 ALA E 223 ILE E 228 1 O VAL E 226 N ILE E 197
SHEET 1 AB1 2 PHE E 163 ASP E 165 0
SHEET 2 AB1 2 LYS E 170 SER E 172 -1 O LEU E 171 N VAL E 164
SHEET 1 AB2 8 GLN F 2 TYR F 9 0
SHEET 2 AB2 8 LYS F 12 HIS F 19 -1 O LEU F 14 N ILE F 7
SHEET 3 AB2 8 GLY F 61 ASP F 66 -1 O SER F 62 N HIS F 19
SHEET 4 AB2 8 VAL F 28 PHE F 34 1 N PRO F 29 O GLY F 61
SHEET 5 AB2 8 THR F 102 SER F 113 1 O LEU F 110 N ILE F 32
SHEET 6 AB2 8 ALA F 132 PRO F 138 1 O TRP F 136 N GLY F 111
SHEET 7 AB2 8 VAL F 195 GLY F 200 1 O LEU F 196 N LEU F 135
SHEET 8 AB2 8 ALA F 223 ILE F 228 1 O VAL F 226 N ILE F 197
SHEET 1 AB3 2 PHE F 163 ASP F 165 0
SHEET 2 AB3 2 LYS F 170 SER F 172 -1 O LEU F 171 N VAL F 164
LINK C NLE A 1 N GLN A 2 1555 1555 1.33
LINK C GLY A 16 N NLE A 17 1555 1555 1.33
LINK C NLE A 17 N NLE A 18 1555 1555 1.33
LINK C NLE A 18 N HIS A 19 1555 1555 1.33
LINK C PRO A 29 N NLE A 30 1555 1555 1.33
LINK C NLE A 30 N VAL A 31 1555 1555 1.33
LINK C ILE A 32 N NLE A 33 1555 1555 1.33
LINK C NLE A 33 N PHE A 34 1555 1555 1.33
LINK C LYS A 50 N NLE A 51 1555 1555 1.33
LINK C NLE A 51 N SER A 52 1555 1555 1.33
LINK C GLU A 79 N NLE A 80 1555 1555 1.33
LINK C NLE A 80 N THR A 81 1555 1555 1.33
LINK C SER A 113 N NLE A 114 1555 1555 1.33
LINK C NLE A 114 N GLY A 115 1555 1555 1.33
LINK C ASN A 141 N NLE A 142 1555 1555 1.33
LINK C NLE A 142 N PRO A 143 1555 1555 1.36
LINK C ILE A 146 N NLE A 147 1555 1555 1.33
LINK C NLE A 147 N ASN A 148 1555 1555 1.33
LINK C ILE A 157 N NLE A 158 1555 1555 1.33
LINK C NLE A 158 N GLU A 159 1555 1555 1.33
LINK C NLE B 1 N GLN B 2 1555 1555 1.33
LINK C GLY B 16 N NLE B 17 1555 1555 1.33
LINK C NLE B 17 N NLE B 18 1555 1555 1.33
LINK C NLE B 18 N HIS B 19 1555 1555 1.33
LINK C PRO B 29 N NLE B 30 1555 1555 1.33
LINK C NLE B 30 N VAL B 31 1555 1555 1.33
LINK C ILE B 32 N NLE B 33 1555 1555 1.33
LINK C NLE B 33 N PHE B 34 1555 1555 1.33
LINK C LYS B 50 N NLE B 51 1555 1555 1.33
LINK C NLE B 51 N SER B 52 1555 1555 1.33
LINK C GLU B 79 N NLE B 80 1555 1555 1.33
LINK C NLE B 80 N THR B 81 1555 1555 1.33
LINK C SER B 113 N NLE B 114 1555 1555 1.33
LINK C NLE B 114 N GLY B 115 1555 1555 1.33
LINK C ASN B 141 N NLE B 142 1555 1555 1.33
LINK C NLE B 142 N PRO B 143 1555 1555 1.35
LINK C ILE B 146 N NLE B 147 1555 1555 1.33
LINK C NLE B 147 N ASN B 148 1555 1555 1.33
LINK C ILE B 157 N NLE B 158 1555 1555 1.33
LINK C NLE B 158 N GLU B 159 1555 1555 1.33
LINK C NLE C 1 N GLN C 2 1555 1555 1.33
LINK C GLY C 16 N NLE C 17 1555 1555 1.33
LINK C NLE C 17 N NLE C 18 1555 1555 1.33
LINK C NLE C 18 N HIS C 19 1555 1555 1.33
LINK C PRO C 29 N NLE C 30 1555 1555 1.33
LINK C NLE C 30 N VAL C 31 1555 1555 1.33
LINK C ILE C 32 N NLE C 33 1555 1555 1.33
LINK C NLE C 33 N PHE C 34 1555 1555 1.33
LINK C LYS C 50 N NLE C 51 1555 1555 1.33
LINK C NLE C 51 N SER C 52 1555 1555 1.33
LINK C GLU C 79 N NLE C 80 1555 1555 1.33
LINK C NLE C 80 N THR C 81 1555 1555 1.33
LINK C SER C 113 N NLE C 114 1555 1555 1.33
LINK C NLE C 114 N GLY C 115 1555 1555 1.33
LINK C ASN C 141 N NLE C 142 1555 1555 1.33
LINK C NLE C 142 N PRO C 143 1555 1555 1.35
LINK C ILE C 146 N NLE C 147 1555 1555 1.33
LINK C NLE C 147 N ASN C 148 1555 1555 1.33
LINK C NLE D 1 N GLN D 2 1555 1555 1.33
LINK C GLY D 16 N NLE D 17 1555 1555 1.33
LINK C NLE D 17 N NLE D 18 1555 1555 1.33
LINK C NLE D 18 N HIS D 19 1555 1555 1.33
LINK C PRO D 29 N NLE D 30 1555 1555 1.33
LINK C NLE D 30 N VAL D 31 1555 1555 1.33
LINK C ILE D 32 N NLE D 33 1555 1555 1.33
LINK C NLE D 33 N PHE D 34 1555 1555 1.33
LINK C LYS D 50 N NLE D 51 1555 1555 1.33
LINK C NLE D 51 N SER D 52 1555 1555 1.33
LINK C GLU D 79 N NLE D 80 1555 1555 1.33
LINK C NLE D 80 N THR D 81 1555 1555 1.33
LINK C SER D 113 N NLE D 114 1555 1555 1.33
LINK C NLE D 114 N GLY D 115 1555 1555 1.33
LINK C ASN D 141 N NLE D 142 1555 1555 1.33
LINK C NLE D 142 N PRO D 143 1555 1555 1.35
LINK C ILE D 157 N NLE D 158 1555 1555 1.33
LINK C NLE D 158 N GLU D 159 1555 1555 1.33
LINK C NLE E 1 N GLN E 2 1555 1555 1.33
LINK C GLY E 16 N NLE E 17 1555 1555 1.33
LINK C NLE E 17 N NLE E 18 1555 1555 1.33
LINK C NLE E 18 N HIS E 19 1555 1555 1.33
LINK C PRO E 29 N NLE E 30 1555 1555 1.33
LINK C NLE E 30 N VAL E 31 1555 1555 1.33
LINK C ILE E 32 N NLE E 33 1555 1555 1.33
LINK C NLE E 33 N PHE E 34 1555 1555 1.33
LINK C LYS E 50 N NLE E 51 1555 1555 1.33
LINK C NLE E 51 N SER E 52 1555 1555 1.33
LINK C GLU E 79 N NLE E 80 1555 1555 1.33
LINK C NLE E 80 N THR E 81 1555 1555 1.33
LINK C SER E 113 N NLE E 114 1555 1555 1.33
LINK C NLE E 114 N GLY E 115 1555 1555 1.33
LINK C ASN E 141 N NLE E 142 1555 1555 1.33
LINK C NLE E 142 N PRO E 143 1555 1555 1.35
LINK C ILE E 146 N NLE E 147 1555 1555 1.33
LINK C NLE E 147 N ASN E 148 1555 1555 1.33
LINK C NLE F 1 N GLN F 2 1555 1555 1.33
LINK C GLY F 16 N NLE F 17 1555 1555 1.33
LINK C NLE F 17 N NLE F 18 1555 1555 1.33
LINK C NLE F 18 N HIS F 19 1555 1555 1.33
LINK C PRO F 29 N NLE F 30 1555 1555 1.33
LINK C NLE F 30 N VAL F 31 1555 1555 1.33
LINK C ILE F 32 N NLE F 33 1555 1555 1.33
LINK C NLE F 33 N PHE F 34 1555 1555 1.33
LINK C LYS F 50 N NLE F 51 1555 1555 1.33
LINK C NLE F 51 N SER F 52 1555 1555 1.33
LINK C GLU F 79 N NLE F 80 1555 1555 1.33
LINK C NLE F 80 N THR F 81 1555 1555 1.33
LINK C SER F 113 N NLE F 114 1555 1555 1.33
LINK C NLE F 114 N GLY F 115 1555 1555 1.33
LINK C ASN F 141 N NLE F 142 1555 1555 1.33
LINK C NLE F 142 N PRO F 143 1555 1555 1.35
LINK C ILE F 146 N NLE F 147 1555 1555 1.33
LINK C NLE F 147 N ASN F 148 1555 1555 1.33
LINK C ILE F 157 N NLE F 158 1555 1555 1.32
LINK C NLE F 158 N GLU F 159 1555 1555 1.33
CRYST1 64.900 76.297 187.790 90.00 93.52 90.00 P 1 21 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 0.015408 0.000000 0.000948 0.00000
SCALE2 0.000000 0.013107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005335 0.00000
TER 2047 LEU A 257
TER 4085 LEU B 257
TER 6046 GLY C 259
TER 8004 LEU D 257
TER 9984 LEU E 257
TER 11985 LEU F 257
MASTER 435 0 69 63 60 0 0 612116 6 642 126
END |