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HEADER HYDROLASE/IMMUNE SYSTEM 29-JAN-15 4XX1
TITLE LOW RESOLUTION STRUCTURE OF LCAT IN COMPLEX WITH FAB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB1 LIGHT CHAIN;
COMPND 3 CHAIN: L, G, O;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB1 HEAVY CHAIN;
COMPND 7 CHAIN: H, E, M;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PHOSPHATIDYLCHOLINE-STEROL ACYLTRANSFERASE;
COMPND 11 CHAIN: A, B, J;
COMPND 12 SYNONYM: LECITHIN-CHOLESTEROL ACYLTRANSFERASE,PHOSPHOLIPID-
COMPND 13 CHOLESTEROL ACYLTRANSFERASE;
COMPND 14 EC: 2.3.1.43;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: LCAT;
SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS A/B HYDROLASE, COMPLEX, HYDROLASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.PIPER,N.P.C.WALKER,W.G.ROMANOW,S.T.THIBAULT
REVDAT 1 29-JUL-15 4XX1 0
JRNL AUTH D.E.PIPER,W.G.ROMANOW,R.N.GUNAWARDANE,P.FORDSTROM,
JRNL AUTH 2 S.MASTERMAN,O.PAN,S.T.THIBAULT,R.ZHANG,D.MEININGER,
JRNL AUTH 3 M.SCHWARZ,Z.WANG,C.KING,M.ZHOU,N.P.C.WALKER
JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF HUMAN LCAT
JRNL REF J.LIPID RES. 2015
JRNL REFN ISSN 0022-2275
JRNL DOI 10.1194/JLR.M059873
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 34806
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1750
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 72.0759 - 8.4612 0.99 2552 121 0.1595 0.2365
REMARK 3 2 8.4612 - 6.7174 1.00 2547 145 0.1902 0.2686
REMARK 3 3 6.7174 - 5.8687 1.00 2527 150 0.2041 0.3208
REMARK 3 4 5.8687 - 5.3323 0.99 2560 119 0.1992 0.2995
REMARK 3 5 5.3323 - 4.9502 1.00 2547 124 0.1806 0.2601
REMARK 3 6 4.9502 - 4.6584 1.00 2565 144 0.1923 0.2622
REMARK 3 7 4.6584 - 4.4252 0.99 2530 140 0.1900 0.2862
REMARK 3 8 4.4252 - 4.2326 0.99 2543 123 0.2035 0.2946
REMARK 3 9 4.2326 - 4.0696 1.00 2529 149 0.2170 0.2624
REMARK 3 10 4.0696 - 3.9292 0.99 2560 139 0.2272 0.3050
REMARK 3 11 3.9292 - 3.8064 0.99 2536 132 0.2496 0.3198
REMARK 3 12 3.8064 - 3.6976 0.99 2512 126 0.2588 0.3610
REMARK 3 13 3.6976 - 3.6002 0.99 2548 138 0.2537 0.3129
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 121.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 127.0
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 : 0.005 17757
REMARK 3 ANGLE : 0.992 24204
REMARK 3 CHIRALITY : 0.038 2636
REMARK 3 PLANARITY : 0.005 3097
REMARK 3 DIHEDRAL : 15.824 6298
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 4XX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-10
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2499
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34818
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 144.123
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16400
REMARK 200 FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.90600
REMARK 200 R SYM FOR SHELL (I) : 0.90600
REMARK 200 FOR SHELL : 0.800
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: 4XWG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DI-AMMONIUM TARTRATE, 0.001 M
REMARK 280 ZINC ACETATE, 13% PEG 1500, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.10667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.55333
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, E, 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, M, J
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 GLU L 211
REMARK 465 CYS L 212
REMARK 465 SER L 213
REMARK 465 GLN H 1
REMARK 465 SER H 140
REMARK 465 SER H 141
REMARK 465 LYS H 142
REMARK 465 SER H 143
REMARK 465 THR H 144
REMARK 465 SER H 145
REMARK 465 GLY H 146
REMARK 465 SER H 228
REMARK 465 CYS H 229
REMARK 465 ALA H 230
REMARK 465 ALA H 231
REMARK 465 ALA H 232
REMARK 465 GLU H 233
REMARK 465 ASN H 234
REMARK 465 LEU H 235
REMARK 465 TYR H 236
REMARK 465 PHE H 237
REMARK 465 GLN H 238
REMARK 465 PHE A 1
REMARK 465 TRP A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 ASN A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 PHE A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 HIS A 11
REMARK 465 THR A 12
REMARK 465 THR A 13
REMARK 465 PRO A 14
REMARK 465 LYS A 15
REMARK 465 ALA A 16
REMARK 465 GLU A 17
REMARK 465 LEU A 18
REMARK 465 SER A 19
REMARK 465 ASN A 20
REMARK 465 ILE A 231
REMARK 465 PRO A 232
REMARK 465 ILE A 233
REMARK 465 MET A 234
REMARK 465 SER A 235
REMARK 465 SER A 236
REMARK 465 ILE A 237
REMARK 465 ALA A 397
REMARK 465 TYR A 398
REMARK 465 ARG A 399
REMARK 465 GLN A 400
REMARK 465 GLY A 401
REMARK 465 PRO A 402
REMARK 465 PRO A 403
REMARK 465 ALA A 404
REMARK 465 SER A 405
REMARK 465 PRO A 406
REMARK 465 THR A 407
REMARK 465 ALA A 408
REMARK 465 SER A 409
REMARK 465 PRO A 410
REMARK 465 GLU A 411
REMARK 465 PRO A 412
REMARK 465 PRO A 413
REMARK 465 PRO A 414
REMARK 465 PRO A 415
REMARK 465 GLU A 416
REMARK 465 GLU A 417
REMARK 465 ASN A 418
REMARK 465 LEU A 419
REMARK 465 TYR A 420
REMARK 465 PHE A 421
REMARK 465 GLN A 422
REMARK 465 GLU G 211
REMARK 465 CYS G 212
REMARK 465 SER G 213
REMARK 465 GLN E 1
REMARK 465 SER E 140
REMARK 465 SER E 141
REMARK 465 LYS E 142
REMARK 465 SER E 143
REMARK 465 THR E 144
REMARK 465 SER E 145
REMARK 465 GLY E 146
REMARK 465 GLY E 147
REMARK 465 CYS E 229
REMARK 465 ALA E 230
REMARK 465 ALA E 231
REMARK 465 ALA E 232
REMARK 465 GLU E 233
REMARK 465 ASN E 234
REMARK 465 LEU E 235
REMARK 465 TYR E 236
REMARK 465 PHE E 237
REMARK 465 GLN E 238
REMARK 465 PHE B 1
REMARK 465 TRP B 2
REMARK 465 LEU B 3
REMARK 465 LEU B 4
REMARK 465 ASN B 5
REMARK 465 VAL B 6
REMARK 465 LEU B 7
REMARK 465 PHE B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 HIS B 11
REMARK 465 THR B 12
REMARK 465 THR B 13
REMARK 465 PRO B 14
REMARK 465 LYS B 15
REMARK 465 ALA B 16
REMARK 465 GLU B 17
REMARK 465 LEU B 18
REMARK 465 SER B 19
REMARK 465 ASN B 20
REMARK 465 ILE B 231
REMARK 465 PRO B 232
REMARK 465 ILE B 233
REMARK 465 MET B 234
REMARK 465 SER B 235
REMARK 465 SER B 236
REMARK 465 ILE B 237
REMARK 465 ALA B 397
REMARK 465 TYR B 398
REMARK 465 ARG B 399
REMARK 465 GLN B 400
REMARK 465 GLY B 401
REMARK 465 PRO B 402
REMARK 465 PRO B 403
REMARK 465 ALA B 404
REMARK 465 SER B 405
REMARK 465 PRO B 406
REMARK 465 THR B 407
REMARK 465 ALA B 408
REMARK 465 SER B 409
REMARK 465 PRO B 410
REMARK 465 GLU B 411
REMARK 465 PRO B 412
REMARK 465 PRO B 413
REMARK 465 PRO B 414
REMARK 465 PRO B 415
REMARK 465 GLU B 416
REMARK 465 GLU B 417
REMARK 465 ASN B 418
REMARK 465 LEU B 419
REMARK 465 TYR B 420
REMARK 465 PHE B 421
REMARK 465 GLN B 422
REMARK 465 SER O 1
REMARK 465 LEU O 107
REMARK 465 GLY O 108
REMARK 465 GLN O 109
REMARK 465 PRO O 110
REMARK 465 LYS O 111
REMARK 465 ALA O 112
REMARK 465 ALA O 113
REMARK 465 PRO O 114
REMARK 465 SER O 115
REMARK 465 VAL O 116
REMARK 465 THR O 117
REMARK 465 LEU O 118
REMARK 465 PHE O 119
REMARK 465 PRO O 120
REMARK 465 PRO O 121
REMARK 465 SER O 122
REMARK 465 SER O 123
REMARK 465 GLU O 124
REMARK 465 GLU O 125
REMARK 465 LEU O 126
REMARK 465 GLN O 127
REMARK 465 ALA O 128
REMARK 465 ASN O 129
REMARK 465 LYS O 130
REMARK 465 ALA O 131
REMARK 465 THR O 132
REMARK 465 LEU O 133
REMARK 465 VAL O 134
REMARK 465 CYS O 135
REMARK 465 LEU O 136
REMARK 465 ILE O 137
REMARK 465 SER O 138
REMARK 465 ASP O 139
REMARK 465 PHE O 140
REMARK 465 TYR O 141
REMARK 465 PRO O 142
REMARK 465 GLY O 143
REMARK 465 ALA O 144
REMARK 465 VAL O 145
REMARK 465 THR O 146
REMARK 465 VAL O 147
REMARK 465 ALA O 148
REMARK 465 TRP O 149
REMARK 465 LYS O 150
REMARK 465 ALA O 151
REMARK 465 ASP O 152
REMARK 465 SER O 153
REMARK 465 SER O 154
REMARK 465 PRO O 155
REMARK 465 VAL O 156
REMARK 465 LYS O 157
REMARK 465 ALA O 158
REMARK 465 GLY O 159
REMARK 465 VAL O 160
REMARK 465 GLU O 161
REMARK 465 THR O 162
REMARK 465 THR O 163
REMARK 465 THR O 164
REMARK 465 PRO O 165
REMARK 465 SER O 166
REMARK 465 LYS O 167
REMARK 465 GLN O 168
REMARK 465 SER O 169
REMARK 465 ASN O 170
REMARK 465 ASN O 171
REMARK 465 LYS O 172
REMARK 465 TYR O 173
REMARK 465 ALA O 174
REMARK 465 ALA O 175
REMARK 465 SER O 176
REMARK 465 SER O 177
REMARK 465 TYR O 178
REMARK 465 LEU O 179
REMARK 465 SER O 180
REMARK 465 LEU O 181
REMARK 465 THR O 182
REMARK 465 PRO O 183
REMARK 465 GLU O 184
REMARK 465 GLN O 185
REMARK 465 TRP O 186
REMARK 465 LYS O 187
REMARK 465 SER O 188
REMARK 465 HIS O 189
REMARK 465 LYS O 190
REMARK 465 SER O 191
REMARK 465 TYR O 192
REMARK 465 SER O 193
REMARK 465 CYS O 194
REMARK 465 GLN O 195
REMARK 465 VAL O 196
REMARK 465 THR O 197
REMARK 465 HIS O 198
REMARK 465 GLU O 199
REMARK 465 GLY O 200
REMARK 465 SER O 201
REMARK 465 THR O 202
REMARK 465 VAL O 203
REMARK 465 GLU O 204
REMARK 465 LYS O 205
REMARK 465 THR O 206
REMARK 465 VAL O 207
REMARK 465 ALA O 208
REMARK 465 PRO O 209
REMARK 465 THR O 210
REMARK 465 GLU O 211
REMARK 465 CYS O 212
REMARK 465 SER O 213
REMARK 465 GLN M 1
REMARK 465 VAL M 2
REMARK 465 ALA M 127
REMARK 465 SER M 128
REMARK 465 THR M 129
REMARK 465 LYS M 130
REMARK 465 GLY M 131
REMARK 465 PRO M 132
REMARK 465 SER M 133
REMARK 465 VAL M 134
REMARK 465 PHE M 135
REMARK 465 PRO M 136
REMARK 465 LEU M 137
REMARK 465 ALA M 138
REMARK 465 PRO M 139
REMARK 465 SER M 140
REMARK 465 SER M 141
REMARK 465 LYS M 142
REMARK 465 SER M 143
REMARK 465 THR M 144
REMARK 465 SER M 145
REMARK 465 GLY M 146
REMARK 465 GLY M 147
REMARK 465 THR M 148
REMARK 465 ALA M 149
REMARK 465 ALA M 150
REMARK 465 LEU M 151
REMARK 465 GLY M 152
REMARK 465 CYS M 153
REMARK 465 LEU M 154
REMARK 465 VAL M 155
REMARK 465 LYS M 156
REMARK 465 ASP M 157
REMARK 465 TYR M 158
REMARK 465 PHE M 159
REMARK 465 PRO M 160
REMARK 465 GLU M 161
REMARK 465 PRO M 162
REMARK 465 VAL M 163
REMARK 465 THR M 164
REMARK 465 VAL M 165
REMARK 465 SER M 166
REMARK 465 TRP M 167
REMARK 465 ASN M 168
REMARK 465 SER M 169
REMARK 465 GLY M 170
REMARK 465 ALA M 171
REMARK 465 LEU M 172
REMARK 465 THR M 173
REMARK 465 SER M 174
REMARK 465 GLY M 175
REMARK 465 VAL M 176
REMARK 465 HIS M 177
REMARK 465 THR M 178
REMARK 465 PHE M 179
REMARK 465 PRO M 180
REMARK 465 ALA M 181
REMARK 465 VAL M 182
REMARK 465 LEU M 183
REMARK 465 GLN M 184
REMARK 465 SER M 185
REMARK 465 SER M 186
REMARK 465 GLY M 187
REMARK 465 LEU M 188
REMARK 465 TYR M 189
REMARK 465 SER M 190
REMARK 465 HIS M 191
REMARK 465 SER M 192
REMARK 465 SER M 193
REMARK 465 VAL M 194
REMARK 465 VAL M 195
REMARK 465 THR M 196
REMARK 465 VAL M 197
REMARK 465 PRO M 198
REMARK 465 SER M 199
REMARK 465 SER M 200
REMARK 465 SER M 201
REMARK 465 LEU M 202
REMARK 465 GLY M 203
REMARK 465 THR M 204
REMARK 465 GLN M 205
REMARK 465 THR M 206
REMARK 465 TYR M 207
REMARK 465 ILE M 208
REMARK 465 CYS M 209
REMARK 465 ASN M 210
REMARK 465 VAL M 211
REMARK 465 ASN M 212
REMARK 465 HIS M 213
REMARK 465 LYS M 214
REMARK 465 PRO M 215
REMARK 465 SER M 216
REMARK 465 ASN M 217
REMARK 465 THR M 218
REMARK 465 LYS M 219
REMARK 465 VAL M 220
REMARK 465 ASP M 221
REMARK 465 LYS M 222
REMARK 465 LYS M 223
REMARK 465 VAL M 224
REMARK 465 GLU M 225
REMARK 465 PRO M 226
REMARK 465 LYS M 227
REMARK 465 SER M 228
REMARK 465 CYS M 229
REMARK 465 ALA M 230
REMARK 465 ALA M 231
REMARK 465 ALA M 232
REMARK 465 GLU M 233
REMARK 465 ASN M 234
REMARK 465 LEU M 235
REMARK 465 TYR M 236
REMARK 465 PHE M 237
REMARK 465 GLN M 238
REMARK 465 PHE J 1
REMARK 465 TRP J 2
REMARK 465 LEU J 3
REMARK 465 LEU J 4
REMARK 465 ASN J 5
REMARK 465 VAL J 6
REMARK 465 LEU J 7
REMARK 465 PHE J 8
REMARK 465 PRO J 9
REMARK 465 PRO J 10
REMARK 465 HIS J 11
REMARK 465 THR J 12
REMARK 465 THR J 13
REMARK 465 PRO J 14
REMARK 465 LYS J 15
REMARK 465 ALA J 16
REMARK 465 GLU J 17
REMARK 465 LEU J 18
REMARK 465 SER J 19
REMARK 465 ASN J 20
REMARK 465 GLY J 230
REMARK 465 ILE J 231
REMARK 465 PRO J 232
REMARK 465 ILE J 233
REMARK 465 MET J 234
REMARK 465 SER J 235
REMARK 465 SER J 236
REMARK 465 ILE J 237
REMARK 465 LYS J 238
REMARK 465 LEU J 239
REMARK 465 LYS J 240
REMARK 465 GLU J 241
REMARK 465 GLU J 242
REMARK 465 GLN J 243
REMARK 465 GLY J 396
REMARK 465 ALA J 397
REMARK 465 TYR J 398
REMARK 465 ARG J 399
REMARK 465 GLN J 400
REMARK 465 GLY J 401
REMARK 465 PRO J 402
REMARK 465 PRO J 403
REMARK 465 ALA J 404
REMARK 465 SER J 405
REMARK 465 PRO J 406
REMARK 465 THR J 407
REMARK 465 ALA J 408
REMARK 465 SER J 409
REMARK 465 PRO J 410
REMARK 465 GLU J 411
REMARK 465 PRO J 412
REMARK 465 PRO J 413
REMARK 465 PRO J 414
REMARK 465 PRO J 415
REMARK 465 GLU J 416
REMARK 465 GLU J 417
REMARK 465 ASN J 418
REMARK 465 LEU J 419
REMARK 465 TYR J 420
REMARK 465 PHE J 421
REMARK 465 GLN J 422
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 OH TYR A 273 OD2 ASP A 284 2.09
REMARK 500 OG1 THR G 132 NZ LYS E 156 2.16
REMARK 500 OH TYR G 2 O ASP G 25 2.16
REMARK 500 OG SER J 225 OD1 ASP J 335 2.19
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 PRO L 209 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO B 320 C - N - CA ANGL. DEV. = 9.1 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 ASP L 50 -68.61 67.58
REMARK 500 SER L 66 107.48 -167.66
REMARK 500 GLN L 78 -160.81 -119.43
REMARK 500 ASP L 91 -143.48 -155.45
REMARK 500 LEU L 107 76.71 -56.35
REMARK 500 ASN L 129 97.53 -54.58
REMARK 500 ASP L 152 -86.26 56.35
REMARK 500 SER L 153 52.02 -155.12
REMARK 500 VAL L 160 141.17 36.64
REMARK 500 GLU L 161 126.92 169.81
REMARK 500 SER L 169 -79.95 -17.96
REMARK 500 ASN L 170 -45.66 1.08
REMARK 500 GLU L 184 50.60 -113.55
REMARK 500 GLU L 199 26.38 45.85
REMARK 500 LYS L 205 123.72 -174.34
REMARK 500 PRO L 209 -4.89 -37.75
REMARK 500 CYS H 22 89.65 -151.95
REMARK 500 PRO H 41 109.58 -51.45
REMARK 500 SER H 56 -95.81 -79.18
REMARK 500 ARG H 87 -157.94 -96.42
REMARK 500 ALA H 92 -170.48 -170.74
REMARK 500 ARG H 104 -95.55 -101.75
REMARK 500 SER H 105 -128.05 -95.94
REMARK 500 SER H 125 -102.88 -142.74
REMARK 500 SER H 126 -22.68 -172.83
REMARK 500 ALA H 150 111.32 -160.70
REMARK 500 LEU H 151 -165.14 -104.28
REMARK 500 LYS H 156 157.75 -48.30
REMARK 500 ASP H 157 102.23 -50.19
REMARK 500 SER H 190 125.92 179.20
REMARK 500 THR H 204 -54.31 -152.72
REMARK 500 PRO H 215 12.19 -61.26
REMARK 500 SER H 216 -0.86 -154.30
REMARK 500 ASN H 217 81.96 55.20
REMARK 500 LEU A 68 149.47 177.51
REMARK 500 LEU A 70 -4.92 73.32
REMARK 500 SER A 87 -3.62 -171.23
REMARK 500 TYR A 120 -86.33 -134.13
REMARK 500 GLU A 137 -75.29 -138.77
REMARK 500 TYR A 171 -4.53 -140.03
REMARK 500 SER A 181 -121.01 50.85
REMARK 500 ASP A 204 -71.07 -81.62
REMARK 500 ALA A 224 -72.04 -79.20
REMARK 500 ASN A 228 82.65 -64.99
REMARK 500 GLN A 229 145.17 176.55
REMARK 500 LEU A 239 72.71 171.09
REMARK 500 GLN A 243 103.16 -13.94
REMARK 500 ARG A 244 85.68 -163.51
REMARK 500 PRO A 250 29.97 -69.37
REMARK 500 PRO A 254 101.91 -53.15
REMARK 500
REMARK 500 THIS ENTRY HAS 162 RAMACHANDRAN OUTLIERS.
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 ALA L 128 ASN L 129 -149.71
REMARK 500 GLU L 184 GLN L 185 148.34
REMARK 500 LYS O 52 ARG O 53 133.57
REMARK 500 ARG O 53 PRO O 54 -115.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound
REMARK 800 to ASN A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 503 bound
REMARK 800 to ASN A 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 502 bound
REMARK 800 to ASN B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 503 bound
REMARK 800 to ASN B 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG J 501 bound
REMARK 800 to ASN J 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG J 502 bound
REMARK 800 to ASN J 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG J 503 bound
REMARK 800 to ASN J 384
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XWG RELATED DB: PDB
REMARK 900 THIS IS A LOW RESOLUTION STRUCTURE OF THE WILD TYPE LCAT PROTEIN.
REMARK 900 4XWG IS A HIGHER RESOLUTION STRUCTURE WITH A SINGLE POINT MUTATION
REMARK 900 IN LCAT (C31Y).
DBREF 4XX1 L 1 213 PDB 4XX1 4XX1 1 213
DBREF 4XX1 H 1 238 PDB 4XX1 4XX1 1 238
DBREF 4XX1 A 1 416 UNP P04180 LCAT_HUMAN 25 440
DBREF 4XX1 G 1 213 PDB 4XX1 4XX1 1 213
DBREF 4XX1 E 1 238 PDB 4XX1 4XX1 1 238
DBREF 4XX1 B 1 416 UNP P04180 LCAT_HUMAN 25 440
DBREF 4XX1 O 1 213 PDB 4XX1 4XX1 1 213
DBREF 4XX1 M 1 238 PDB 4XX1 4XX1 1 238
DBREF 4XX1 J 1 416 UNP P04180 LCAT_HUMAN 25 440
SEQADV 4XX1 GLU A 417 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 ASN A 418 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 LEU A 419 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 TYR A 420 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 PHE A 421 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 GLN A 422 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 GLU B 417 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 ASN B 418 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 LEU B 419 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 TYR B 420 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 PHE B 421 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 GLN B 422 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 GLU J 417 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 ASN J 418 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 LEU J 419 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 TYR J 420 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 PHE J 421 UNP P04180 EXPRESSION TAG
SEQADV 4XX1 GLN J 422 UNP P04180 EXPRESSION TAG
SEQRES 1 L 213 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER
SEQRES 2 L 213 PRO GLY GLN THR ALA SER ILE THR CYS SER GLY ASP LYS
SEQRES 3 L 213 LEU GLY ASN LYS PHE THR SER TRP TYR GLN ARG LYS PRO
SEQRES 4 L 213 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP THR LYS
SEQRES 5 L 213 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER THR
SEQRES 6 L 213 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN
SEQRES 7 L 213 ALA MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP
SEQRES 8 L 213 SER SER THR ALA TRP VAL PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 213 GLU VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR
SEQRES 10 L 213 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS
SEQRES 11 L 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY
SEQRES 12 L 213 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL
SEQRES 13 L 213 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER
SEQRES 14 L 213 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR
SEQRES 15 L 213 PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN
SEQRES 16 L 213 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA
SEQRES 17 L 213 PRO THR GLU CYS SER
SEQRES 1 H 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 H 238 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 238 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 H 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP
SEQRES 5 H 238 TYR ASP GLY SER ASN LYS PHE TYR GLU ASP SER VAL LYS
SEQRES 6 H 238 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 H 238 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 238 ALA VAL TYR TYR CYS ALA ARG GLU GLY ALA ALA VAL ARG
SEQRES 9 H 238 SER PHE TYR TYR SER TYR TYR GLY MET ASP VAL TRP GLY
SEQRES 10 H 238 GLN GLY THR THR VAL THR VAL SER SER ALA SER THR LYS
SEQRES 11 H 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 12 H 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 13 H 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 14 H 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 15 H 238 LEU GLN SER SER GLY LEU TYR SER HIS SER SER VAL VAL
SEQRES 16 H 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 17 H 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 18 H 238 LYS LYS VAL GLU PRO LYS SER CYS ALA ALA ALA GLU ASN
SEQRES 19 H 238 LEU TYR PHE GLN
SEQRES 1 A 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 A 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 A 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 A 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 A 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 A 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 A 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 A 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 A 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 A 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 A 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 A 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 A 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 A 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 A 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 A 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 A 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 A 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 A 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 A 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 A 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 A 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 A 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 A 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 A 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 A 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 A 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 A 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 A 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 A 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 A 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 A 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 A 422 GLU ASN LEU TYR PHE GLN
SEQRES 1 G 213 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER
SEQRES 2 G 213 PRO GLY GLN THR ALA SER ILE THR CYS SER GLY ASP LYS
SEQRES 3 G 213 LEU GLY ASN LYS PHE THR SER TRP TYR GLN ARG LYS PRO
SEQRES 4 G 213 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP THR LYS
SEQRES 5 G 213 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER THR
SEQRES 6 G 213 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN
SEQRES 7 G 213 ALA MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP
SEQRES 8 G 213 SER SER THR ALA TRP VAL PHE GLY GLY GLY THR LYS LEU
SEQRES 9 G 213 GLU VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR
SEQRES 10 G 213 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS
SEQRES 11 G 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY
SEQRES 12 G 213 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL
SEQRES 13 G 213 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER
SEQRES 14 G 213 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR
SEQRES 15 G 213 PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN
SEQRES 16 G 213 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA
SEQRES 17 G 213 PRO THR GLU CYS SER
SEQRES 1 E 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 E 238 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 E 238 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 E 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP
SEQRES 5 E 238 TYR ASP GLY SER ASN LYS PHE TYR GLU ASP SER VAL LYS
SEQRES 6 E 238 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 E 238 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR
SEQRES 8 E 238 ALA VAL TYR TYR CYS ALA ARG GLU GLY ALA ALA VAL ARG
SEQRES 9 E 238 SER PHE TYR TYR SER TYR TYR GLY MET ASP VAL TRP GLY
SEQRES 10 E 238 GLN GLY THR THR VAL THR VAL SER SER ALA SER THR LYS
SEQRES 11 E 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 12 E 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 13 E 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 14 E 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 15 E 238 LEU GLN SER SER GLY LEU TYR SER HIS SER SER VAL VAL
SEQRES 16 E 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 17 E 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 18 E 238 LYS LYS VAL GLU PRO LYS SER CYS ALA ALA ALA GLU ASN
SEQRES 19 E 238 LEU TYR PHE GLN
SEQRES 1 B 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 B 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 B 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 B 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 B 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 B 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 B 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 B 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 B 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 B 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 B 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 B 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 B 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 B 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 B 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 B 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 B 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 B 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 B 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 B 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 B 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 B 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 B 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 B 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 B 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 B 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 B 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 B 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 B 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 B 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 B 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 B 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 B 422 GLU ASN LEU TYR PHE GLN
SEQRES 1 O 213 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER
SEQRES 2 O 213 PRO GLY GLN THR ALA SER ILE THR CYS SER GLY ASP LYS
SEQRES 3 O 213 LEU GLY ASN LYS PHE THR SER TRP TYR GLN ARG LYS PRO
SEQRES 4 O 213 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP THR LYS
SEQRES 5 O 213 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER THR
SEQRES 6 O 213 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN
SEQRES 7 O 213 ALA MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP
SEQRES 8 O 213 SER SER THR ALA TRP VAL PHE GLY GLY GLY THR LYS LEU
SEQRES 9 O 213 GLU VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR
SEQRES 10 O 213 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS
SEQRES 11 O 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY
SEQRES 12 O 213 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL
SEQRES 13 O 213 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER
SEQRES 14 O 213 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR
SEQRES 15 O 213 PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN
SEQRES 16 O 213 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA
SEQRES 17 O 213 PRO THR GLU CYS SER
SEQRES 1 M 238 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN
SEQRES 2 M 238 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 M 238 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN
SEQRES 4 M 238 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP
SEQRES 5 M 238 TYR ASP GLY SER ASN LYS PHE TYR GLU ASP SER VAL LYS
SEQRES 6 M 238 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 M 238 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR
SEQRES 8 M 238 ALA VAL TYR TYR CYS ALA ARG GLU GLY ALA ALA VAL ARG
SEQRES 9 M 238 SER PHE TYR TYR SER TYR TYR GLY MET ASP VAL TRP GLY
SEQRES 10 M 238 GLN GLY THR THR VAL THR VAL SER SER ALA SER THR LYS
SEQRES 11 M 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 12 M 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 13 M 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 14 M 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 15 M 238 LEU GLN SER SER GLY LEU TYR SER HIS SER SER VAL VAL
SEQRES 16 M 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 17 M 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 18 M 238 LYS LYS VAL GLU PRO LYS SER CYS ALA ALA ALA GLU ASN
SEQRES 19 M 238 LEU TYR PHE GLN
SEQRES 1 J 422 PHE TRP LEU LEU ASN VAL LEU PHE PRO PRO HIS THR THR
SEQRES 2 J 422 PRO LYS ALA GLU LEU SER ASN HIS THR ARG PRO VAL ILE
SEQRES 3 J 422 LEU VAL PRO GLY CYS LEU GLY ASN GLN LEU GLU ALA LYS
SEQRES 4 J 422 LEU ASP LYS PRO ASP VAL VAL ASN TRP MET CYS TYR ARG
SEQRES 5 J 422 LYS THR GLU ASP PHE PHE THR ILE TRP LEU ASP LEU ASN
SEQRES 6 J 422 MET PHE LEU PRO LEU GLY VAL ASP CYS TRP ILE ASP ASN
SEQRES 7 J 422 THR ARG VAL VAL TYR ASN ARG SER SER GLY LEU VAL SER
SEQRES 8 J 422 ASN ALA PRO GLY VAL GLN ILE ARG VAL PRO GLY PHE GLY
SEQRES 9 J 422 LYS THR TYR SER VAL GLU TYR LEU ASP SER SER LYS LEU
SEQRES 10 J 422 ALA GLY TYR LEU HIS THR LEU VAL GLN ASN LEU VAL ASN
SEQRES 11 J 422 ASN GLY TYR VAL ARG ASP GLU THR VAL ARG ALA ALA PRO
SEQRES 12 J 422 TYR ASP TRP ARG LEU GLU PRO GLY GLN GLN GLU GLU TYR
SEQRES 13 J 422 TYR ARG LYS LEU ALA GLY LEU VAL GLU GLU MET HIS ALA
SEQRES 14 J 422 ALA TYR GLY LYS PRO VAL PHE LEU ILE GLY HIS SER LEU
SEQRES 15 J 422 GLY CYS LEU HIS LEU LEU TYR PHE LEU LEU ARG GLN PRO
SEQRES 16 J 422 GLN ALA TRP LYS ASP ARG PHE ILE ASP GLY PHE ILE SER
SEQRES 17 J 422 LEU GLY ALA PRO TRP GLY GLY SER ILE LYS PRO MET LEU
SEQRES 18 J 422 VAL LEU ALA SER GLY ASP ASN GLN GLY ILE PRO ILE MET
SEQRES 19 J 422 SER SER ILE LYS LEU LYS GLU GLU GLN ARG ILE THR THR
SEQRES 20 J 422 THR SER PRO TRP MET PHE PRO SER ARG MET ALA TRP PRO
SEQRES 21 J 422 GLU ASP HIS VAL PHE ILE SER THR PRO SER PHE ASN TYR
SEQRES 22 J 422 THR GLY ARG ASP PHE GLN ARG PHE PHE ALA ASP LEU HIS
SEQRES 23 J 422 PHE GLU GLU GLY TRP TYR MET TRP LEU GLN SER ARG ASP
SEQRES 24 J 422 LEU LEU ALA GLY LEU PRO ALA PRO GLY VAL GLU VAL TYR
SEQRES 25 J 422 CYS LEU TYR GLY VAL GLY LEU PRO THR PRO ARG THR TYR
SEQRES 26 J 422 ILE TYR ASP HIS GLY PHE PRO TYR THR ASP PRO VAL GLY
SEQRES 27 J 422 VAL LEU TYR GLU ASP GLY ASP ASP THR VAL ALA THR ARG
SEQRES 28 J 422 SER THR GLU LEU CYS GLY LEU TRP GLN GLY ARG GLN PRO
SEQRES 29 J 422 GLN PRO VAL HIS LEU LEU PRO LEU HIS GLY ILE GLN HIS
SEQRES 30 J 422 LEU ASN MET VAL PHE SER ASN LEU THR LEU GLU HIS ILE
SEQRES 31 J 422 ASN ALA ILE LEU LEU GLY ALA TYR ARG GLN GLY PRO PRO
SEQRES 32 J 422 ALA SER PRO THR ALA SER PRO GLU PRO PRO PRO PRO GLU
SEQRES 33 J 422 GLU ASN LEU TYR PHE GLN
HET NAG A 501 14
HET NAG A 502 14
HET NAG A 503 14
HET NAG B 501 14
HET NAG B 502 14
HET NAG B 503 14
HET NAG J 501 14
HET NAG J 502 14
HET NAG J 503 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 10 NAG 9(C8 H15 N O6)
HELIX 1 AA1 LYS L 26 LYS L 30 5 5
HELIX 2 AA2 SER L 122 LEU L 126 5 5
HELIX 3 AA3 THR L 182 TRP L 186 5 5
HELIX 4 AA4 ASP H 62 LYS H 65 5 4
HELIX 5 AA5 ASN H 74 LYS H 76 5 3
HELIX 6 AA6 LYS H 214 ASN H 217 5 4
HELIX 7 AA7 LEU A 70 ARG A 80 1 11
HELIX 8 AA8 THR A 106 TYR A 111 1 6
HELIX 9 AA9 LEU A 121 ASN A 131 1 11
HELIX 10 AB1 GLU A 149 GLN A 152 5 4
HELIX 11 AB2 GLN A 153 GLY A 172 1 20
HELIX 12 AB3 SER A 181 ARG A 193 1 13
HELIX 13 AB4 PRO A 195 PHE A 202 1 8
HELIX 14 AB5 ILE A 217 SER A 225 1 9
HELIX 15 AB6 ASP A 277 LEU A 285 1 9
HELIX 16 AB7 PHE A 287 ASP A 299 1 13
HELIX 17 AB8 ALA A 349 GLU A 354 1 6
HELIX 18 AB9 LEU A 355 LEU A 358 5 4
HELIX 19 AC1 GLN A 376 PHE A 382 5 7
HELIX 20 AC2 SER A 383 LEU A 395 1 13
HELIX 21 AC3 SER G 122 GLN G 127 1 6
HELIX 22 AC4 THR G 182 HIS G 189 1 8
HELIX 23 AC5 THR E 28 TYR E 32 5 5
HELIX 24 AC6 ASP E 62 LYS E 65 5 4
HELIX 25 AC7 ARG E 87 THR E 91 5 5
HELIX 26 AC8 SER E 169 ALA E 171 5 3
HELIX 27 AC9 PRO E 198 LEU E 202 5 5
HELIX 28 AD1 LYS E 214 ASN E 217 5 4
HELIX 29 AD2 ASP B 63 PHE B 67 5 5
HELIX 30 AD3 LEU B 70 ARG B 80 1 11
HELIX 31 AD4 THR B 106 TYR B 111 1 6
HELIX 32 AD5 LEU B 121 ASN B 130 1 10
HELIX 33 AD6 GLU B 149 GLN B 152 5 4
HELIX 34 AD7 GLN B 153 GLY B 172 1 20
HELIX 35 AD8 SER B 181 GLN B 194 1 14
HELIX 36 AD9 PRO B 195 PHE B 202 1 8
HELIX 37 AE1 ILE B 217 SER B 225 1 9
HELIX 38 AE2 ASP B 277 LEU B 285 1 9
HELIX 39 AE3 GLU B 288 ARG B 298 1 11
HELIX 40 AE4 ALA B 349 GLU B 354 1 6
HELIX 41 AE5 LEU B 355 GLN B 363 5 9
HELIX 42 AE6 LEU B 378 PHE B 382 5 5
HELIX 43 AE7 SER B 383 GLY B 396 1 14
HELIX 44 AE8 LYS O 26 LYS O 30 5 5
HELIX 45 AE9 ASP J 63 PHE J 67 5 5
HELIX 46 AF1 LEU J 70 THR J 79 1 10
HELIX 47 AF2 THR J 106 TYR J 111 1 6
HELIX 48 AF3 LEU J 121 ASN J 130 1 10
HELIX 49 AF4 GLU J 149 GLN J 153 5 5
HELIX 50 AF5 ARG J 158 GLY J 172 1 15
HELIX 51 AF6 SER J 181 GLN J 194 1 14
HELIX 52 AF7 GLN J 196 ARG J 201 1 6
HELIX 53 AF8 ILE J 217 GLY J 226 1 10
HELIX 54 AF9 SER J 249 PHE J 253 5 5
HELIX 55 AG1 THR J 274 ASP J 277 5 4
HELIX 56 AG2 PHE J 278 ASP J 284 1 7
HELIX 57 AG3 GLY J 290 ARG J 298 1 9
HELIX 58 AG4 ALA J 349 GLU J 354 1 6
HELIX 59 AG5 LEU J 355 LEU J 358 5 4
HELIX 60 AG6 HIS J 377 VAL J 381 5 5
HELIX 61 AG7 SER J 383 LEU J 395 1 13
SHEET 1 AA1 3 ALA L 18 THR L 21 0
SHEET 2 AA1 3 THR L 69 ILE L 74 -1 O ILE L 74 N ALA L 18
SHEET 3 AA1 3 PHE L 61 SER L 66 -1 N SER L 64 O THR L 71
SHEET 1 AA2 4 VAL L 44 TYR L 48 0
SHEET 2 AA2 4 SER L 33 ARG L 37 -1 N TRP L 34 O VAL L 46
SHEET 3 AA2 4 ASP L 84 ALA L 89 -1 O ASP L 84 N ARG L 37
SHEET 4 AA2 4 VAL L 97 PHE L 98 -1 O VAL L 97 N ALA L 89
SHEET 1 AA3 4 VAL L 44 TYR L 48 0
SHEET 2 AA3 4 SER L 33 ARG L 37 -1 N TRP L 34 O VAL L 46
SHEET 3 AA3 4 ASP L 84 ALA L 89 -1 O ASP L 84 N ARG L 37
SHEET 4 AA3 4 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 85
SHEET 1 AA4 4 THR L 117 PHE L 119 0
SHEET 2 AA4 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 AA4 4 LYS L 172 LEU L 181 -1 O ALA L 175 N ILE L 137
SHEET 4 AA4 4 SER L 166 GLN L 168 -1 N SER L 166 O ALA L 174
SHEET 1 AA5 4 SER L 154 PRO L 155 0
SHEET 2 AA5 4 VAL L 145 ALA L 151 -1 N ALA L 151 O SER L 154
SHEET 3 AA5 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148
SHEET 4 AA5 4 SER L 201 VAL L 207 -1 O SER L 201 N HIS L 198
SHEET 1 AA6 4 GLN H 3 GLU H 6 0
SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 AA6 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18
SHEET 4 AA6 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82
SHEET 1 AA7 6 GLY H 10 VAL H 12 0
SHEET 2 AA7 6 THR H 120 VAL H 124 1 O THR H 123 N GLY H 10
SHEET 3 AA7 6 ALA H 92 GLU H 99 -1 N TYR H 94 O THR H 120
SHEET 4 AA7 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95
SHEET 5 AA7 6 GLU H 46 ILE H 51 -1 O ILE H 51 N MET H 34
SHEET 6 AA7 6 LYS H 58 TYR H 60 -1 O PHE H 59 N VAL H 50
SHEET 1 AA8 4 GLY H 10 VAL H 12 0
SHEET 2 AA8 4 THR H 120 VAL H 124 1 O THR H 123 N GLY H 10
SHEET 3 AA8 4 ALA H 92 GLU H 99 -1 N TYR H 94 O THR H 120
SHEET 4 AA8 4 MET H 113 TRP H 116 -1 O VAL H 115 N ARG H 98
SHEET 1 AA9 4 VAL H 134 LEU H 137 0
SHEET 2 AA9 4 THR H 148 VAL H 155 -1 O GLY H 152 N LEU H 137
SHEET 3 AA9 4 SER H 192 PRO H 198 -1 O VAL H 197 N ALA H 149
SHEET 4 AA9 4 VAL H 176 THR H 178 -1 N HIS H 177 O VAL H 194
SHEET 1 AB1 3 THR H 164 TRP H 167 0
SHEET 2 AB1 3 ILE H 208 HIS H 213 -1 O ASN H 210 N SER H 166
SHEET 3 AB1 3 THR H 218 LYS H 223 -1 O VAL H 220 N VAL H 211
SHEET 1 AB2 6 VAL A 139 ALA A 141 0
SHEET 2 AB2 6 VAL A 25 VAL A 28 1 N LEU A 27 O ARG A 140
SHEET 3 AB2 6 VAL A 175 HIS A 180 1 O ILE A 178 N ILE A 26
SHEET 4 AB2 6 ILE A 203 LEU A 209 1 O ILE A 207 N LEU A 177
SHEET 5 AB2 6 GLU A 310 VAL A 317 1 O GLU A 310 N PHE A 206
SHEET 6 AB2 6 VAL A 367 HIS A 373 1 O HIS A 368 N VAL A 311
SHEET 1 AB3 3 PHE A 58 TRP A 61 0
SHEET 2 AB3 3 LEU A 36 LEU A 40 -1 N LEU A 36 O ILE A 60
SHEET 3 AB3 3 VAL A 96 ARG A 99 -1 O ARG A 99 N GLU A 37
SHEET 1 AB4 2 VAL A 81 ASN A 84 0
SHEET 2 AB4 2 LEU A 89 ASN A 92 -1 O LEU A 89 N ASN A 84
SHEET 1 AB5 4 ASN A 272 TYR A 273 0
SHEET 2 AB5 4 ILE A 266 SER A 267 -1 N ILE A 266 O TYR A 273
SHEET 3 AB5 4 LEU A 319 ILE A 326 1 O TYR A 325 N SER A 267
SHEET 4 AB5 4 GLY A 338 GLY A 344 -1 O GLY A 338 N ILE A 326
SHEET 1 AB6 2 SER G 9 VAL G 12 0
SHEET 2 AB6 2 LYS G 103 VAL G 106 1 O GLU G 105 N VAL G 12
SHEET 1 AB7 3 ALA G 18 SER G 23 0
SHEET 2 AB7 3 THR G 69 ILE G 74 -1 O ALA G 70 N CYS G 22
SHEET 3 AB7 3 PHE G 61 SER G 66 -1 N SER G 64 O THR G 71
SHEET 1 AB8 3 VAL G 44 ILE G 47 0
SHEET 2 AB8 3 PHE G 31 ARG G 37 -1 N GLN G 36 O VAL G 44
SHEET 3 AB8 3 ASP G 84 TRP G 90 -1 O GLN G 88 N SER G 33
SHEET 1 AB9 4 SER G 115 PHE G 119 0
SHEET 2 AB9 4 ALA G 131 PHE G 140 -1 O SER G 138 N SER G 115
SHEET 3 AB9 4 SER G 177 LEU G 181 -1 O LEU G 181 N ALA G 131
SHEET 4 AB9 4 VAL G 160 THR G 162 -1 N GLU G 161 O TYR G 178
SHEET 1 AC1 4 SER G 115 PHE G 119 0
SHEET 2 AC1 4 ALA G 131 PHE G 140 -1 O SER G 138 N SER G 115
SHEET 3 AC1 4 TYR G 173 ALA G 175 -1 O TYR G 173 N PHE G 140
SHEET 4 AC1 4 SER G 166 LYS G 167 -1 N SER G 166 O ALA G 174
SHEET 1 AC2 4 SER G 154 PRO G 155 0
SHEET 2 AC2 4 THR G 146 ALA G 151 -1 N ALA G 151 O SER G 154
SHEET 3 AC2 4 TYR G 192 HIS G 198 -1 O THR G 197 N THR G 146
SHEET 4 AC2 4 SER G 201 VAL G 207 -1 O SER G 201 N HIS G 198
SHEET 1 AC3 4 GLN E 3 SER E 7 0
SHEET 2 AC3 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3
SHEET 3 AC3 4 THR E 78 MET E 83 -1 O LEU E 79 N CYS E 22
SHEET 4 AC3 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82
SHEET 1 AC4 6 GLY E 10 VAL E 12 0
SHEET 2 AC4 6 THR E 120 VAL E 124 1 O THR E 123 N VAL E 12
SHEET 3 AC4 6 ALA E 92 GLU E 99 -1 N TYR E 94 O THR E 120
SHEET 4 AC4 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95
SHEET 5 AC4 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38
SHEET 6 AC4 6 LYS E 58 TYR E 60 -1 O PHE E 59 N VAL E 50
SHEET 1 AC5 4 GLY E 10 VAL E 12 0
SHEET 2 AC5 4 THR E 120 VAL E 124 1 O THR E 123 N VAL E 12
SHEET 3 AC5 4 ALA E 92 GLU E 99 -1 N TYR E 94 O THR E 120
SHEET 4 AC5 4 MET E 113 TRP E 116 -1 O VAL E 115 N ARG E 98
SHEET 1 AC6 4 SER E 133 LEU E 137 0
SHEET 2 AC6 4 ALA E 149 TYR E 158 -1 O GLY E 152 N LEU E 137
SHEET 3 AC6 4 LEU E 188 VAL E 197 -1 O TYR E 189 N TYR E 158
SHEET 4 AC6 4 VAL E 176 THR E 178 -1 N HIS E 177 O VAL E 194
SHEET 1 AC7 4 SER E 133 LEU E 137 0
SHEET 2 AC7 4 ALA E 149 TYR E 158 -1 O GLY E 152 N LEU E 137
SHEET 3 AC7 4 LEU E 188 VAL E 197 -1 O TYR E 189 N TYR E 158
SHEET 4 AC7 4 VAL E 182 GLN E 184 -1 N VAL E 182 O SER E 190
SHEET 1 AC8 3 THR E 164 TRP E 167 0
SHEET 2 AC8 3 ILE E 208 ASN E 212 -1 O ASN E 210 N SER E 166
SHEET 3 AC8 3 LYS E 219 LYS E 223 -1 O LYS E 222 N CYS E 209
SHEET 1 AC9 4 VAL B 139 ALA B 141 0
SHEET 2 AC9 4 VAL B 25 VAL B 28 1 N VAL B 25 O ARG B 140
SHEET 3 AC9 4 VAL B 175 HIS B 180 1 O ILE B 178 N ILE B 26
SHEET 4 AC9 4 ILE B 203 LEU B 209 1 O ILE B 207 N LEU B 177
SHEET 1 AD1 3 PHE B 58 TRP B 61 0
SHEET 2 AD1 3 LEU B 36 LYS B 39 -1 N ALA B 38 O PHE B 58
SHEET 3 AD1 3 GLN B 97 ARG B 99 -1 O ARG B 99 N GLU B 37
SHEET 1 AD2 2 VAL B 81 TYR B 83 0
SHEET 2 AD2 2 VAL B 90 ASN B 92 -1 O SER B 91 N VAL B 82
SHEET 1 AD3 4 ASN B 272 TYR B 273 0
SHEET 2 AD3 4 ILE B 266 SER B 267 -1 N ILE B 266 O TYR B 273
SHEET 3 AD3 4 LEU B 319 TYR B 327 1 O TYR B 327 N SER B 267
SHEET 4 AD3 4 PRO B 336 GLY B 344 -1 O GLU B 342 N THR B 321
SHEET 1 AD4 2 VAL B 311 VAL B 317 0
SHEET 2 AD4 2 VAL B 367 HIS B 373 1 O LEU B 370 N CYS B 313
SHEET 1 AD5 3 THR O 21 CYS O 22 0
SHEET 2 AD5 3 THR O 69 LEU O 72 -1 O ALA O 70 N CYS O 22
SHEET 3 AD5 3 GLY O 63 SER O 66 -1 N SER O 64 O THR O 71
SHEET 1 AD6 3 SER O 33 ARG O 37 0
SHEET 2 AD6 3 ASP O 84 ALA O 89 -1 O GLN O 88 N SER O 33
SHEET 3 AD6 3 VAL O 97 PHE O 98 -1 O VAL O 97 N ALA O 89
SHEET 1 AD7 3 SER O 33 ARG O 37 0
SHEET 2 AD7 3 ASP O 84 ALA O 89 -1 O GLN O 88 N SER O 33
SHEET 3 AD7 3 THR O 102 LYS O 103 -1 O THR O 102 N TYR O 85
SHEET 1 AD8 3 GLU M 46 ILE M 51 0
SHEET 2 AD8 3 MET M 34 GLN M 39 -1 N MET M 34 O ILE M 51
SHEET 3 AD8 3 ALA M 97 ARG M 98 -1 O ALA M 97 N HIS M 35
SHEET 1 AD9 4 GLU M 46 ILE M 51 0
SHEET 2 AD9 4 MET M 34 GLN M 39 -1 N MET M 34 O ILE M 51
SHEET 3 AD9 4 ALA M 92 TYR M 94 -1 O VAL M 93 N GLN M 39
SHEET 4 AD9 4 THR M 120 VAL M 122 -1 O VAL M 122 N ALA M 92
SHEET 1 AE1 2 PHE M 68 ARG M 72 0
SHEET 2 AE1 2 LEU M 79 MET M 83 -1 O GLN M 82 N THR M 69
SHEET 1 AE2 6 VAL J 139 ALA J 141 0
SHEET 2 AE2 6 VAL J 25 VAL J 28 1 N VAL J 25 O ARG J 140
SHEET 3 AE2 6 VAL J 175 HIS J 180 1 O PHE J 176 N ILE J 26
SHEET 4 AE2 6 ILE J 203 LEU J 209 1 O ILE J 207 N LEU J 177
SHEET 5 AE2 6 GLU J 310 VAL J 317 1 O LEU J 314 N SER J 208
SHEET 6 AE2 6 VAL J 367 HIS J 373 1 O LEU J 372 N TYR J 315
SHEET 1 AE3 2 LEU J 36 ALA J 38 0
SHEET 2 AE3 2 PHE J 58 TRP J 61 -1 O TRP J 61 N LEU J 36
SHEET 1 AE4 2 VAL J 81 TYR J 83 0
SHEET 2 AE4 2 VAL J 90 ASN J 92 -1 O SER J 91 N VAL J 82
SHEET 1 AE5 4 ASN J 272 TYR J 273 0
SHEET 2 AE5 4 ILE J 266 SER J 267 -1 N ILE J 266 O TYR J 273
SHEET 3 AE5 4 LEU J 319 ILE J 326 1 O TYR J 325 N SER J 267
SHEET 4 AE5 4 GLY J 338 GLY J 344 -1 O GLU J 342 N THR J 321
SSBOND 1 CYS L 22 CYS L 87 1555 1555 2.03
SSBOND 2 CYS L 135 CYS L 194 1555 1555 2.05
SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 4 CYS H 153 CYS H 209 1555 1555 2.05
SSBOND 5 CYS A 50 CYS A 74 1555 1555 2.04
SSBOND 6 CYS A 313 CYS A 356 1555 1555 2.05
SSBOND 7 CYS G 22 CYS G 87 1555 1555 2.04
SSBOND 8 CYS G 135 CYS G 194 1555 1555 2.04
SSBOND 9 CYS E 22 CYS E 96 1555 1555 2.04
SSBOND 10 CYS E 153 CYS E 209 1555 1555 2.05
SSBOND 11 CYS B 50 CYS B 74 1555 1555 2.04
SSBOND 12 CYS B 313 CYS B 356 1555 1555 2.05
SSBOND 13 CYS O 22 CYS O 87 1555 1555 2.03
SSBOND 14 CYS M 22 CYS M 96 1555 1555 2.04
SSBOND 15 CYS J 50 CYS J 74 1555 1555 2.04
SSBOND 16 CYS J 313 CYS J 356 1555 1555 2.04
LINK ND2 ASN A 84 C1 NAG A 501 1555 1555 1.44
LINK ND2 ASN A 272 C1 NAG A 502 1555 1555 1.43
LINK ND2 ASN A 384 C1 NAG A 503 1555 1555 1.44
LINK ND2 ASN B 84 C1 NAG B 501 1555 1555 1.45
LINK ND2 ASN B 272 C1 NAG B 502 1555 1555 1.43
LINK ND2 ASN B 384 C1 NAG B 503 1555 1555 1.46
LINK ND2 ASN J 84 C1 NAG J 501 1555 1555 1.44
LINK ND2 ASN J 272 C1 NAG J 502 1555 1555 1.44
LINK ND2 ASN J 384 C1 NAG J 503 1555 1555 1.44
CISPEP 1 TYR L 141 PRO L 142 0 -0.88
CISPEP 2 PHE H 159 PRO H 160 0 -2.74
CISPEP 3 GLU H 161 PRO H 162 0 4.04
CISPEP 4 TRP A 61 LEU A 62 0 1.54
CISPEP 5 PHE A 331 PRO A 332 0 4.92
CISPEP 6 TYR G 141 PRO G 142 0 -0.48
CISPEP 7 PHE E 159 PRO E 160 0 -2.74
CISPEP 8 GLU E 161 PRO E 162 0 -1.12
CISPEP 9 TRP B 61 LEU B 62 0 5.29
CISPEP 10 PHE B 331 PRO B 332 0 0.41
CISPEP 11 TRP J 61 LEU J 62 0 2.24
CISPEP 12 PHE J 331 PRO J 332 0 1.12
SITE 1 AC1 4 ASN A 84 SER A 87 LEU A 89 ASP H 84
SITE 1 AC2 3 SER A 267 PRO A 269 ASN A 272
SITE 1 AC3 2 ASN A 384 GLU A 388
SITE 1 AC4 2 ASN B 84 SER B 87
SITE 1 AC5 1 ASN B 272
SITE 1 AC6 1 ASN B 384
SITE 1 AC7 3 ASN J 84 SER J 86 SER J 87
SITE 1 AC8 3 SER J 267 PRO J 269 ASN J 272
SITE 1 AC9 2 ASN J 384 GLU J 388
CRYST1 166.419 166.419 97.660 90.00 90.00 120.00 P 32 9
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 0.006009 0.003469 0.000000 0.00000
SCALE2 0.000000 0.006939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010240 0.00000
TER 1578 THR L 210
TER 3247 LYS H 227
TER 6218 GLY A 396
TER 7796 THR G 210
TER 9467 SER E 228
TER 12438 GLY B 396
TER 13232 VAL O 106
TER 14206 SER M 126
TER 17116 LEU J 395
MASTER 834 0 9 61 147 0 9 617233 9 167 207
END |