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HEADER HYDROLASE 20-NOV-24 9HGZ
TITLE CRYSTAL STRUCTURE OF RECOMBINANT SWINE BUTYRYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: MATURATED PROTEIN (NO SIGNAL PEPTIDE) DEVOID OF THE C-
COMPND 7 TERMINAL PART (STOP CODON AT RESIDUE 530)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: BCHE;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227
KEYWDS BUTYRYLCHOLINESTERASE, SWINE, RECOMBINANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,F.NACHON
REVDAT 1 03-DEC-25 9HGZ 0
JRNL AUTH X.BRAZZOLOTTO,F.NACHON
JRNL TITL CRYSTAL STRUCTURE OF RECOMBINANT SWINE BUTYRYLCHOLINESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 124.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 97051
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 4837
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1124.5500 - 7.6400 0.99 3117 177 0.1760 0.1722
REMARK 3 2 7.6400 - 6.0600 1.00 3110 148 0.1918 0.2303
REMARK 3 3 6.0600 - 5.3000 1.00 3105 155 0.1748 0.2053
REMARK 3 4 5.2900 - 4.8100 1.00 3105 153 0.1645 0.2037
REMARK 3 5 4.8100 - 4.4700 1.00 3070 171 0.1484 0.1714
REMARK 3 6 4.4700 - 4.2000 1.00 3101 150 0.1494 0.1637
REMARK 3 7 4.2000 - 3.9900 1.00 3070 160 0.1608 0.2087
REMARK 3 8 3.9900 - 3.8200 1.00 3097 143 0.1721 0.1815
REMARK 3 9 3.8200 - 3.6700 1.00 3089 154 0.1765 0.2213
REMARK 3 10 3.6700 - 3.5400 1.00 3059 174 0.1853 0.2332
REMARK 3 11 3.5400 - 3.4300 1.00 3119 140 0.1947 0.2505
REMARK 3 12 3.4300 - 3.3400 1.00 3046 179 0.2132 0.2344
REMARK 3 13 3.3400 - 3.2500 1.00 3080 158 0.2173 0.2658
REMARK 3 14 3.2500 - 3.1700 1.00 3049 160 0.2231 0.2742
REMARK 3 15 3.1700 - 3.1000 1.00 3104 141 0.2324 0.2566
REMARK 3 16 3.1000 - 3.0300 1.00 3004 187 0.2340 0.2846
REMARK 3 17 3.0300 - 2.9700 1.00 3095 182 0.2314 0.2561
REMARK 3 18 2.9700 - 2.9100 1.00 3029 175 0.2287 0.2458
REMARK 3 19 2.9100 - 2.8600 1.00 3093 184 0.2365 0.2882
REMARK 3 20 2.8600 - 2.8100 1.00 3033 174 0.2365 0.2658
REMARK 3 21 2.8100 - 2.7700 1.00 3025 163 0.2398 0.2964
REMARK 3 22 2.7700 - 2.7300 1.00 3104 157 0.2536 0.2943
REMARK 3 23 2.7300 - 2.6900 1.00 3088 152 0.2762 0.3341
REMARK 3 24 2.6900 - 2.6500 1.00 3069 139 0.2794 0.3714
REMARK 3 25 2.6500 - 2.6100 1.00 3077 157 0.2816 0.3297
REMARK 3 26 2.6100 - 2.5800 1.00 3070 167 0.2804 0.2677
REMARK 3 27 2.5800 - 2.5500 1.00 3028 170 0.2787 0.2767
REMARK 3 28 2.5500 - 2.5100 1.00 3044 168 0.2790 0.3159
REMARK 3 29 2.5100 - 2.4900 1.00 3090 127 0.2979 0.3187
REMARK 3 30 2.4900 - 2.4600 0.99 3044 172 0.2977 0.2816
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.289
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.927
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.33
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 17318
REMARK 3 ANGLE : 0.570 23453
REMARK 3 CHIRALITY : 0.044 2544
REMARK 3 PLANARITY : 0.005 2979
REMARK 3 DIHEDRAL : 15.270 6657
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7075 24.8645 8.0432
REMARK 3 T TENSOR
REMARK 3 T11: 0.1220 T22: 0.2089
REMARK 3 T33: 0.1255 T12: 0.0332
REMARK 3 T13: 0.0064 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.0982 L22: 0.1611
REMARK 3 L33: 0.0772 L12: -0.0639
REMARK 3 L13: -0.0420 L23: 0.0750
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: 0.0745 S13: 0.0108
REMARK 3 S21: -0.1052 S22: 0.0094 S23: 0.0364
REMARK 3 S31: -0.0337 S32: -0.0366 S33: 0.0068
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1918 45.3952 32.6368
REMARK 3 T TENSOR
REMARK 3 T11: -0.0423 T22: 0.2270
REMARK 3 T33: 0.1915 T12: 0.0725
REMARK 3 T13: 0.0007 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.0887 L22: 0.0590
REMARK 3 L33: 0.0717 L12: -0.0300
REMARK 3 L13: -0.0645 L23: 0.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.0761 S13: -0.0437
REMARK 3 S21: -0.0353 S22: -0.0854 S23: -0.0681
REMARK 3 S31: -0.0289 S32: 0.0926 S33: -0.0745
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): -85.5871 47.6945 44.3272
REMARK 3 T TENSOR
REMARK 3 T11: -0.0804 T22: 0.5150
REMARK 3 T33: 0.1798 T12: -0.1022
REMARK 3 T13: -0.0425 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.2581 L22: 0.1168
REMARK 3 L33: 0.1528 L12: 0.1641
REMARK 3 L13: -0.0028 L23: -0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: 0.3901 S13: -0.1344
REMARK 3 S21: 0.0385 S22: 0.1271 S23: 0.0584
REMARK 3 S31: -0.0413 S32: -0.3025 S33: 0.2423
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D'
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3972 -19.6909 -4.6269
REMARK 3 T TENSOR
REMARK 3 T11: 0.4158 T22: 0.0934
REMARK 3 T33: 0.3655 T12: -0.4432
REMARK 3 T13: 0.0805 T23: -0.1138
REMARK 3 L TENSOR
REMARK 3 L11: 0.0445 L22: 0.0534
REMARK 3 L33: 0.0109 L12: 0.0272
REMARK 3 L13: 0.0082 L23: 0.0347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: 0.0284 S13: -0.1474
REMARK 3 S21: 0.1843 S22: -0.0601 S23: 0.2093
REMARK 3 S31: 0.2168 S32: -0.1228 S33: -0.0036
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 9HGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1292143241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-11
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) : 0.87260
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 300 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97104
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.458
REMARK 200 RESOLUTION RANGE LOW (A) : 124.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.00
REMARK 200 R MERGE (I) : 0.30800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4540
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.44
REMARK 200 R MERGE FOR SHELL (I) : 2.10900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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 (%): 56.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.85300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.92650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 131.77950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, G
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, I
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 281
REMARK 465 ASN A 282
REMARK 465 HIS A 283
REMARK 465 MET A 284
REMARK 465 LEU A 285
REMARK 465 LEU A 286
REMARK 465 SER A 287
REMARK 465 GLY A 482
REMARK 465 THR A 483
REMARK 465 GLN A 484
REMARK 465 GLU B 1
REMARK 465 GLU B 2
REMARK 465 PRO B 281
REMARK 465 ASN B 282
REMARK 465 HIS B 283
REMARK 465 MET B 284
REMARK 465 LEU B 285
REMARK 465 LEU B 286
REMARK 465 GLY B 482
REMARK 465 THR B 483
REMARK 465 GLN B 484
REMARK 465 ASN B 485
REMARK 465 ASN B 486
REMARK 465 GLU C 1
REMARK 465 GLU C 2
REMARK 465 ASP C 3
REMARK 465 PRO C 281
REMARK 465 ASN C 282
REMARK 465 HIS C 283
REMARK 465 MET C 284
REMARK 465 LEU C 285
REMARK 465 LEU C 286
REMARK 465 SER C 287
REMARK 465 GLY C 482
REMARK 465 THR C 483
REMARK 465 GLN C 484
REMARK 465 ASN C 485
REMARK 465 ASN C 486
REMARK 465 GLU D 1
REMARK 465 GLU D 2
REMARK 465 ASP D 3
REMARK 465 ILE D 4
REMARK 465 ILE D 5
REMARK 465 VAL D 6
REMARK 465 THR D 7
REMARK 465 THR D 8
REMARK 465 LYS D 9
REMARK 465 MET D 49
REMARK 465 TRP D 56
REMARK 465 ASN D 57
REMARK 465 VAL D 280
REMARK 465 PRO D 281
REMARK 465 ASN D 282
REMARK 465 HIS D 283
REMARK 465 MET D 284
REMARK 465 LEU D 285
REMARK 465 LEU D 286
REMARK 465 SER D 287
REMARK 465 ASN D 481
REMARK 465 GLY D 482
REMARK 465 THR D 483
REMARK 465 GLN D 484
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 PHE A 43 -1.23 67.93
REMARK 500 PHE A 153 18.09 -141.77
REMARK 500 ALA A 162 81.21 -153.42
REMARK 500 SER A 198 -115.04 60.09
REMARK 500 ARG A 242 -52.54 76.56
REMARK 500 ASP A 297 -70.43 -109.00
REMARK 500 ASP A 324 67.57 -119.19
REMARK 500 MET A 374 -70.93 -121.86
REMARK 500 ILE A 398 -57.34 -132.12
REMARK 500 GLU A 506 -68.53 -97.88
REMARK 500 LYS A 513 74.07 53.39
REMARK 500 PHE B 43 -2.37 69.94
REMARK 500 ASP B 54 -125.47 -104.16
REMARK 500 ALA B 58 67.32 -101.80
REMARK 500 ASN B 106 57.48 -149.76
REMARK 500 PHE B 153 18.10 -142.17
REMARK 500 ALA B 162 75.85 -161.95
REMARK 500 SER B 198 -118.94 61.90
REMARK 500 ASP B 297 -68.73 -108.50
REMARK 500 ASP B 324 68.77 -119.70
REMARK 500 MET B 374 -68.54 -131.45
REMARK 500 ILE B 398 -62.58 -127.13
REMARK 500 GLU B 506 -88.99 -87.85
REMARK 500 ASP C 54 -151.21 -78.05
REMARK 500 ALA C 162 72.27 -158.88
REMARK 500 SER C 198 -120.08 62.01
REMARK 500 ASP C 297 -73.81 -89.25
REMARK 500 ASP C 324 67.90 -119.90
REMARK 500 THR C 377 -163.31 -106.42
REMARK 500 ILE C 398 -61.28 -128.36
REMARK 500 PRO C 449 9.52 -66.55
REMARK 500 GLU C 506 -73.39 -91.00
REMARK 500 LYS D 12 97.45 -168.32
REMARK 500 LEU D 21 -119.07 49.88
REMARK 500 PHE D 43 -1.58 73.46
REMARK 500 THR D 59 11.39 -149.26
REMARK 500 ALA D 62 -82.43 -29.57
REMARK 500 ASN D 63 -142.62 172.76
REMARK 500 ASN D 106 85.67 -151.24
REMARK 500 PHE D 118 18.68 57.55
REMARK 500 PHE D 153 17.29 -151.36
REMARK 500 ALA D 162 61.73 -155.85
REMARK 500 SER D 198 -117.82 61.44
REMARK 500 ASP D 297 -73.85 -103.34
REMARK 500 MET D 374 -62.18 -132.88
REMARK 500 ILE D 398 -61.11 -128.38
REMARK 500 VAL D 436 99.41 -68.01
REMARK 500 GLN D 498 65.74 61.15
REMARK 500 GLU D 506 -95.23 -91.22
REMARK 500 LYS D 513 70.42 58.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 858 DISTANCE = 6.15 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 605
DBREF1 9HGZ A 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HGZ A A0A4X1VEU5 29 557
DBREF1 9HGZ B 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HGZ B A0A4X1VEU5 29 557
DBREF1 9HGZ C 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HGZ C A0A4X1VEU5 29 557
DBREF1 9HGZ D 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HGZ D A0A4X1VEU5 29 557
SEQRES 1 A 529 GLU GLU ASP ILE ILE VAL THR THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET ASN LEU PRO VAL LEU GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER MET THR LYS TRP
SEQRES 5 A 529 PRO ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 TYR GLN ASN THR ASP GLN SER PHE PRO GLY PHE VAL GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR GLU LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL MET ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU SER ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO ARG SER HIS PRO LEU PHE ALA ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER SER ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU THR LEU ALA
SEQRES 20 A 529 LYS PHE ILE GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 GLN ASN GLU VAL PHE VAL VAL PRO ASN HIS MET LEU LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP LEU PRO ASP THR LEU LEU GLN LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLU
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR MET ASP TRP THR
SEQRES 30 A 529 ASP ASP GLN ARG ALA GLU ASN TYR ARG ASP ALA LEU ASP
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASP ILE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU MET GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ALA ASN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE MET
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 529 GLY THR GLN ASN ASN SER THR ARG TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER ASN GLU GLN LYS TYR LEU THR LEU ASN ALA GLU SER
SEQRES 40 A 529 PRO ARG VAL TYR THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR LEU PHE PHE PRO LYS VAL
SEQRES 1 B 529 GLU GLU ASP ILE ILE VAL THR THR LYS ASN GLY LYS VAL
SEQRES 2 B 529 ARG GLY MET ASN LEU PRO VAL LEU GLY GLY THR VAL THR
SEQRES 3 B 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 529 ARG LEU ARG PHE LYS LYS PRO GLN SER MET THR LYS TRP
SEQRES 5 B 529 PRO ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 529 TYR GLN ASN THR ASP GLN SER PHE PRO GLY PHE VAL GLY
SEQRES 7 B 529 SER GLU MET TRP ASN PRO ASN THR GLU LEU SER GLU ASP
SEQRES 8 B 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 529 LYS ASN ALA THR VAL MET ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 529 LYS PHE LEU SER ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 529 GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS LEU
SEQRES 17 B 529 LEU SER PRO ARG SER HIS PRO LEU PHE ALA ARG ALA ILE
SEQRES 18 B 529 LEU GLN SER GLY SER SER ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU THR LEU ALA
SEQRES 20 B 529 LYS PHE ILE GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 529 GLN ASN GLU VAL PHE VAL VAL PRO ASN HIS MET LEU LEU
SEQRES 23 B 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 529 THR ASP LEU PRO ASP THR LEU LEU GLN LEU GLY GLN PHE
SEQRES 25 B 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLU
SEQRES 28 B 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 529 GLY LYS GLU SER ILE LEU PHE HIS TYR MET ASP TRP THR
SEQRES 30 B 529 ASP ASP GLN ARG ALA GLU ASN TYR ARG ASP ALA LEU ASP
SEQRES 31 B 529 ASP VAL VAL GLY ASP TYR ASP ILE ILE CYS PRO ALA LEU
SEQRES 32 B 529 GLU PHE THR LYS LYS PHE SER GLU MET GLY ASN ASN ALA
SEQRES 33 B 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ALA ASN
SEQRES 36 B 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE MET
SEQRES 37 B 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 529 GLY THR GLN ASN ASN SER THR ARG TRP PRO VAL PHE LYS
SEQRES 39 B 529 SER ASN GLU GLN LYS TYR LEU THR LEU ASN ALA GLU SER
SEQRES 40 B 529 PRO ARG VAL TYR THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 529 PHE TRP THR LEU PHE PHE PRO LYS VAL
SEQRES 1 C 529 GLU GLU ASP ILE ILE VAL THR THR LYS ASN GLY LYS VAL
SEQRES 2 C 529 ARG GLY MET ASN LEU PRO VAL LEU GLY GLY THR VAL THR
SEQRES 3 C 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 C 529 ARG LEU ARG PHE LYS LYS PRO GLN SER MET THR LYS TRP
SEQRES 5 C 529 PRO ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 C 529 TYR GLN ASN THR ASP GLN SER PHE PRO GLY PHE VAL GLY
SEQRES 7 C 529 SER GLU MET TRP ASN PRO ASN THR GLU LEU SER GLU ASP
SEQRES 8 C 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 C 529 LYS ASN ALA THR VAL MET ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 C 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 C 529 LYS PHE LEU SER ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 C 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 C 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 C 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 C 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 C 529 GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS LEU
SEQRES 17 C 529 LEU SER PRO ARG SER HIS PRO LEU PHE ALA ARG ALA ILE
SEQRES 18 C 529 LEU GLN SER GLY SER SER ASN ALA PRO TRP ALA VAL THR
SEQRES 19 C 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU THR LEU ALA
SEQRES 20 C 529 LYS PHE ILE GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 C 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 C 529 GLN ASN GLU VAL PHE VAL VAL PRO ASN HIS MET LEU LEU
SEQRES 23 C 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 C 529 THR ASP LEU PRO ASP THR LEU LEU GLN LEU GLY GLN PHE
SEQRES 25 C 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 C 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 C 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLU
SEQRES 28 C 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 C 529 GLY LYS GLU SER ILE LEU PHE HIS TYR MET ASP TRP THR
SEQRES 30 C 529 ASP ASP GLN ARG ALA GLU ASN TYR ARG ASP ALA LEU ASP
SEQRES 31 C 529 ASP VAL VAL GLY ASP TYR ASP ILE ILE CYS PRO ALA LEU
SEQRES 32 C 529 GLU PHE THR LYS LYS PHE SER GLU MET GLY ASN ASN ALA
SEQRES 33 C 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 C 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 C 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ALA ASN
SEQRES 36 C 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE MET
SEQRES 37 C 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 C 529 GLY THR GLN ASN ASN SER THR ARG TRP PRO VAL PHE LYS
SEQRES 39 C 529 SER ASN GLU GLN LYS TYR LEU THR LEU ASN ALA GLU SER
SEQRES 40 C 529 PRO ARG VAL TYR THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 C 529 PHE TRP THR LEU PHE PHE PRO LYS VAL
SEQRES 1 D 529 GLU GLU ASP ILE ILE VAL THR THR LYS ASN GLY LYS VAL
SEQRES 2 D 529 ARG GLY MET ASN LEU PRO VAL LEU GLY GLY THR VAL THR
SEQRES 3 D 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 D 529 ARG LEU ARG PHE LYS LYS PRO GLN SER MET THR LYS TRP
SEQRES 5 D 529 PRO ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 D 529 TYR GLN ASN THR ASP GLN SER PHE PRO GLY PHE VAL GLY
SEQRES 7 D 529 SER GLU MET TRP ASN PRO ASN THR GLU LEU SER GLU ASP
SEQRES 8 D 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 D 529 LYS ASN ALA THR VAL MET ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 D 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 D 529 LYS PHE LEU SER ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 D 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 D 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 D 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 D 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 D 529 GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS LEU
SEQRES 17 D 529 LEU SER PRO ARG SER HIS PRO LEU PHE ALA ARG ALA ILE
SEQRES 18 D 529 LEU GLN SER GLY SER SER ASN ALA PRO TRP ALA VAL THR
SEQRES 19 D 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU THR LEU ALA
SEQRES 20 D 529 LYS PHE ILE GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 D 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 D 529 GLN ASN GLU VAL PHE VAL VAL PRO ASN HIS MET LEU LEU
SEQRES 23 D 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 D 529 THR ASP LEU PRO ASP THR LEU LEU GLN LEU GLY GLN PHE
SEQRES 25 D 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 D 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 D 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLU
SEQRES 28 D 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 D 529 GLY LYS GLU SER ILE LEU PHE HIS TYR MET ASP TRP THR
SEQRES 30 D 529 ASP ASP GLN ARG ALA GLU ASN TYR ARG ASP ALA LEU ASP
SEQRES 31 D 529 ASP VAL VAL GLY ASP TYR ASP ILE ILE CYS PRO ALA LEU
SEQRES 32 D 529 GLU PHE THR LYS LYS PHE SER GLU MET GLY ASN ASN ALA
SEQRES 33 D 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 D 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 D 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ALA ASN
SEQRES 36 D 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE MET
SEQRES 37 D 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 D 529 GLY THR GLN ASN ASN SER THR ARG TRP PRO VAL PHE LYS
SEQRES 39 D 529 SER ASN GLU GLN LYS TYR LEU THR LEU ASN ALA GLU SER
SEQRES 40 D 529 PRO ARG VAL TYR THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 D 529 PHE TRP THR LEU PHE PHE PRO LYS VAL
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET FUC E 5 10
HET NAG F 1 14
HET FUC F 2 10
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET FUC H 3 10
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET FUC I 5 10
HET NAG J 1 14
HET FUC J 2 10
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET GOL A 604 6
HET PG4 A 605 10
HET PG4 A 606 13
HET GOL A 607 6
HET SO4 A 608 5
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 611 5
HET SO4 A 612 5
HET PEG B 601 7
HET NAG B 602 14
HET NAG B 603 14
HET PEG B 604 7
HET EDO B 605 4
HET GOL B 606 6
HET SO4 B 607 5
HET EDO B 608 4
HET EDO B 609 4
HET EDO B 610 4
HET EDO B 611 4
HET EDO B 612 4
HET EDO B 613 4
HET NAG C 601 14
HET GOL C 602 6
HET PEG C 603 7
HET GOL C 604 6
HET SO4 C 605 5
HET SO4 C 606 5
HET SO4 C 607 5
HET EDO C 608 4
HET EDO C 609 4
HET GOL D 601 6
HET EDO D 602 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 5 MAN 2(C6 H12 O6)
FORMUL 5 FUC 5(C6 H12 O5)
FORMUL 14 GOL 6(C3 H8 O3)
FORMUL 15 PG4 2(C8 H18 O5)
FORMUL 18 SO4 9(O4 S 2-)
FORMUL 23 PEG 3(C4 H10 O3)
FORMUL 27 EDO 10(C2 H6 O2)
FORMUL 47 HOH *464(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 LEU A 208 1 11
HELIX 9 AA9 LEU A 209 PHE A 217 5 9
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 THR A 258 5 3
HELIX 12 AB3 GLU A 259 ASN A 266 1 8
HELIX 13 AB4 ASP A 268 VAL A 277 1 10
HELIX 14 AB5 PHE A 278 VAL A 280 5 3
HELIX 15 AB6 LEU A 302 LEU A 309 1 8
HELIX 16 AB7 GLY A 326 VAL A 331 1 6
HELIX 17 AB8 THR A 346 PHE A 358 1 13
HELIX 18 AB9 SER A 362 MET A 374 1 13
HELIX 19 AC1 GLU A 383 ILE A 398 1 16
HELIX 20 AC2 ILE A 398 MET A 412 1 15
HELIX 21 AC3 PRO A 431 GLY A 435 5 5
HELIX 22 AC4 GLU A 441 PHE A 446 1 6
HELIX 23 AC5 GLY A 447 ASN A 455 5 9
HELIX 24 AC6 THR A 457 GLY A 478 1 22
HELIX 25 AC7 ARG A 515 PHE A 525 1 11
HELIX 26 AC8 PHE A 526 VAL A 529 5 4
HELIX 27 AC9 LEU B 38 ARG B 42 5 5
HELIX 28 AD1 PHE B 76 MET B 81 1 6
HELIX 29 AD2 LEU B 125 ASP B 129 5 5
HELIX 30 AD3 GLY B 130 GLU B 137 1 8
HELIX 31 AD4 GLY B 149 LEU B 154 1 6
HELIX 32 AD5 ASN B 165 ILE B 182 1 18
HELIX 33 AD6 ALA B 183 PHE B 185 5 3
HELIX 34 AD7 SER B 198 LEU B 209 1 12
HELIX 35 AD8 SER B 210 PHE B 217 5 8
HELIX 36 AD9 SER B 235 GLY B 251 1 17
HELIX 37 AE1 ASN B 256 ASN B 266 1 11
HELIX 38 AE2 ASP B 268 VAL B 277 1 10
HELIX 39 AE3 LEU B 302 LEU B 309 1 8
HELIX 40 AE4 GLY B 326 VAL B 331 1 6
HELIX 41 AE5 THR B 346 PHE B 358 1 13
HELIX 42 AE6 SER B 362 MET B 374 1 13
HELIX 43 AE7 GLU B 383 ILE B 398 1 16
HELIX 44 AE8 ILE B 398 GLU B 411 1 14
HELIX 45 AE9 PRO B 431 GLY B 435 5 5
HELIX 46 AF1 GLU B 441 PHE B 446 1 6
HELIX 47 AF2 GLY B 447 GLU B 451 5 5
HELIX 48 AF3 THR B 457 GLY B 478 1 22
HELIX 49 AF4 ARG B 515 PHE B 525 1 11
HELIX 50 AF5 PHE B 526 VAL B 529 5 4
HELIX 51 AF6 LEU C 38 ARG C 42 5 5
HELIX 52 AF7 PHE C 76 MET C 81 1 6
HELIX 53 AF8 LEU C 125 ASP C 129 5 5
HELIX 54 AF9 GLY C 130 ARG C 138 1 9
HELIX 55 AG1 GLY C 149 LEU C 154 1 6
HELIX 56 AG2 ASN C 165 ILE C 182 1 18
HELIX 57 AG3 ALA C 183 PHE C 185 5 3
HELIX 58 AG4 SER C 198 LEU C 208 1 11
HELIX 59 AG5 LEU C 209 PHE C 217 5 9
HELIX 60 AG6 SER C 235 GLY C 251 1 17
HELIX 61 AG7 GLU C 257 ASN C 266 1 10
HELIX 62 AG8 ASP C 268 VAL C 277 1 10
HELIX 63 AG9 LEU C 302 GLY C 310 1 9
HELIX 64 AH1 GLY C 326 ALA C 334 1 9
HELIX 65 AH2 THR C 346 PHE C 358 1 13
HELIX 66 AH3 SER C 362 MET C 374 1 13
HELIX 67 AH4 GLU C 383 ILE C 398 1 16
HELIX 68 AH5 ILE C 398 MET C 412 1 15
HELIX 69 AH6 PRO C 431 GLY C 435 5 5
HELIX 70 AH7 GLU C 441 PHE C 446 1 6
HELIX 71 AH8 GLY C 447 GLU C 451 5 5
HELIX 72 AH9 THR C 457 GLY C 478 1 22
HELIX 73 AI1 ARG C 515 PHE C 525 1 11
HELIX 74 AI2 PHE C 526 VAL C 529 5 4
HELIX 75 AI3 PHE D 76 MET D 81 1 6
HELIX 76 AI4 GLY D 130 GLU D 137 1 8
HELIX 77 AI5 GLY D 149 LEU D 154 1 6
HELIX 78 AI6 ASN D 165 GLY D 186 1 22
HELIX 79 AI7 SER D 198 SER D 210 1 13
HELIX 80 AI8 PRO D 211 PHE D 217 5 7
HELIX 81 AI9 SER D 235 PHE D 249 1 15
HELIX 82 AJ1 ASN D 256 ASN D 266 1 11
HELIX 83 AJ2 ASP D 268 VAL D 277 1 10
HELIX 84 AJ3 LEU D 302 LEU D 309 1 8
HELIX 85 AJ4 GLY D 326 VAL D 331 1 6
HELIX 86 AJ5 THR D 346 PHE D 358 1 13
HELIX 87 AJ6 SER D 362 MET D 374 1 13
HELIX 88 AJ7 GLU D 383 ILE D 398 1 16
HELIX 89 AJ8 ILE D 398 GLU D 411 1 14
HELIX 90 AJ9 PRO D 431 GLY D 435 5 5
HELIX 91 AK1 GLU D 441 GLY D 447 1 7
HELIX 92 AK2 LEU D 448 ASN D 455 5 8
HELIX 93 AK3 THR D 457 GLY D 478 1 22
HELIX 94 AK4 ARG D 515 PHE D 525 1 11
HELIX 95 AK5 PHE D 526 VAL D 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 7 0
SHEET 2 AA1 3 LYS A 12 ARG A 14 -1 O VAL A 13 N VAL A 6
SHEET 3 AA1 3 ILE A 55 TRP A 56 1 O TRP A 56 N LYS A 12
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O ILE A 99 N THR A 26
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N TRP A 112 O VAL A 142
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 421 N VAL A 321
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 501 N PHE A 418
SHEET 11 AA211 VAL A 510 THR A 512 -1 O TYR A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 THR B 8 0
SHEET 2 AA3 3 GLY B 11 ARG B 14 -1 O GLY B 11 N THR B 8
SHEET 3 AA3 3 ILE B 55 ASN B 57 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 MET B 16 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O ALA B 27 N MET B 16
SHEET 3 AA411 TYR B 94 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 4 AA411 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 7 AA411 ARG B 219 GLN B 223 1 O GLN B 223 N GLY B 196
SHEET 8 AA411 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA411 ALA B 416 PHE B 421 1 O PHE B 421 N VAL B 321
SHEET 10 AA411 LYS B 499 LEU B 503 1 O LEU B 501 N PHE B 418
SHEET 11 AA411 VAL B 510 THR B 512 -1 O TYR B 511 N TYR B 500
SHEET 1 AA5 3 ILE C 5 THR C 7 0
SHEET 2 AA5 3 LYS C 12 ARG C 14 -1 O VAL C 13 N VAL C 6
SHEET 3 AA5 3 TRP C 56 ASN C 57 1 O TRP C 56 N ARG C 14
SHEET 1 AA611 MET C 16 PRO C 19 0
SHEET 2 AA611 THR C 24 PRO C 32 -1 O ALA C 27 N MET C 16
SHEET 3 AA611 TYR C 94 PRO C 100 -1 O ILE C 99 N THR C 26
SHEET 4 AA611 ILE C 140 MET C 144 -1 O SER C 143 N ASN C 96
SHEET 5 AA611 ALA C 107 ILE C 113 1 N TRP C 112 O VAL C 142
SHEET 6 AA611 GLY C 187 GLU C 197 1 O ASN C 188 N ALA C 107
SHEET 7 AA611 ARG C 219 GLN C 223 1 O ARG C 219 N LEU C 194
SHEET 8 AA611 ILE C 317 ASN C 322 1 O LEU C 318 N LEU C 222
SHEET 9 AA611 ALA C 416 PHE C 421 1 O PHE C 421 N VAL C 321
SHEET 10 AA611 LYS C 499 LEU C 503 1 O LEU C 501 N PHE C 418
SHEET 11 AA611 VAL C 510 THR C 512 -1 O TYR C 511 N TYR C 500
SHEET 1 AA711 MET D 16 VAL D 20 0
SHEET 2 AA711 GLY D 23 PRO D 32 -1 O VAL D 25 N LEU D 18
SHEET 3 AA711 TYR D 94 PRO D 100 -1 O ILE D 99 N THR D 26
SHEET 4 AA711 ILE D 140 MET D 144 -1 O SER D 143 N ASN D 96
SHEET 5 AA711 ALA D 107 ILE D 113 1 N MET D 110 O ILE D 140
SHEET 6 AA711 GLY D 187 GLU D 197 1 O PHE D 195 N ILE D 111
SHEET 7 AA711 ARG D 219 GLN D 223 1 O ARG D 219 N LEU D 194
SHEET 8 AA711 ILE D 317 ASN D 322 1 O LEU D 318 N LEU D 222
SHEET 9 AA711 ALA D 416 PHE D 421 1 O PHE D 421 N VAL D 321
SHEET 10 AA711 LYS D 499 LEU D 503 1 O LEU D 503 N TYR D 420
SHEET 11 AA711 VAL D 510 THR D 512 -1 O TYR D 511 N TYR D 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.03
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.04
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.03
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.03
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.04
SSBOND 7 CYS C 65 CYS C 92 1555 1555 2.03
SSBOND 8 CYS C 252 CYS C 263 1555 1555 2.03
SSBOND 9 CYS C 400 CYS C 519 1555 1555 2.04
SSBOND 10 CYS D 65 CYS D 92 1555 1555 2.03
SSBOND 11 CYS D 252 CYS D 263 1555 1555 2.03
SSBOND 12 CYS D 400 CYS D 519 1555 1555 2.04
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 57 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 106 C1 NAG B 602 1555 1555 1.44
LINK ND2 ASN B 241 C1 NAG B 603 1555 1555 1.44
LINK ND2 ASN B 341 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN C 241 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN C 341 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN C 455 C1 NAG C 601 1555 1555 1.44
LINK ND2 ASN D 341 C1 NAG J 1 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O6 NAG E 1 C1 FUC E 5 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45
LINK O6 NAG F 1 C1 FUC F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O6 NAG H 1 C1 FUC H 3 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O6 NAG I 1 C1 FUC I 5 1555 1555 1.45
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45
LINK O6 NAG J 1 C1 FUC J 2 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 1.88
CISPEP 2 ALA B 101 PRO B 102 0 1.01
CISPEP 3 ALA C 101 PRO C 102 0 0.98
CISPEP 4 ALA D 101 PRO D 102 0 3.36
CRYST1 124.553 124.553 175.706 90.00 90.00 90.00 P 41 16
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 0.008029 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005691 0.00000
TER 4134 VAL A 529
TER 8259 VAL B 529
TER 12377 VAL C 529
TER 16413 VAL D 529
MASTER 456 0 55 95 53 0 0 617342 4 519 164
END |