| content |
HEADER HYDROLASE 20-NOV-24 9HH0
TITLE CRYSTAL STRUCTURE OF RECOMBINANT SOMAN-AGED SWINE
TITLE 2 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: MATURE PROTEIN FORM (DEVOID OF SIGNAL PEPTIDE) AND
COMPND 7 DEVOID OF C-TERMINAL PART (STOP CODON AT RESIDUE POSITION 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, ORGANOPHOSPHORUS COMPOUND,
KEYWDS 2 AGING., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,F.NACHON
REVDAT 1 03-DEC-25 9HH0 0
JRNL AUTH X.BRAZZOLOTTO,F.NACHON
JRNL TITL CRYSTAL STRUCTURE OF RECOMBINANT SOMAN-AGED SWINE
JRNL TITL 2 BUTYRYLCHOLINESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.66 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) : 2.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 124.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 76123
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 3952
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1124.6900 - 8.0900 0.99 2646 121 0.1700 0.1756
REMARK 3 2 8.0900 - 6.4200 1.00 2603 140 0.1786 0.1824
REMARK 3 3 6.4200 - 5.6100 1.00 2577 157 0.1794 0.2005
REMARK 3 4 5.6100 - 5.1000 1.00 2597 144 0.1647 0.2222
REMARK 3 5 5.1000 - 4.7300 1.00 2562 173 0.1497 0.1848
REMARK 3 6 4.7300 - 4.4500 1.00 2554 152 0.1372 0.1996
REMARK 3 7 4.4500 - 4.2300 1.00 2562 158 0.1436 0.1784
REMARK 3 8 4.2300 - 4.0500 1.00 2624 127 0.1543 0.1774
REMARK 3 9 4.0500 - 3.8900 1.00 2598 112 0.1619 0.2120
REMARK 3 10 3.8900 - 3.7600 1.00 2550 176 0.1744 0.2288
REMARK 3 11 3.7600 - 3.6400 1.00 2641 93 0.1866 0.2187
REMARK 3 12 3.6400 - 3.5300 1.00 2583 131 0.1881 0.2286
REMARK 3 13 3.5300 - 3.4400 1.00 2573 141 0.1985 0.2897
REMARK 3 14 3.4400 - 3.3600 1.00 2570 132 0.2205 0.2605
REMARK 3 15 3.3600 - 3.2800 1.00 2591 136 0.2172 0.2677
REMARK 3 16 3.2800 - 3.2100 1.00 2589 136 0.2322 0.2744
REMARK 3 17 3.2100 - 3.1500 1.00 2581 135 0.2436 0.2918
REMARK 3 18 3.1500 - 3.0900 1.00 2577 170 0.2547 0.2743
REMARK 3 19 3.0900 - 3.0300 1.00 2526 147 0.2505 0.3169
REMARK 3 20 3.0300 - 2.9800 1.00 2592 133 0.2491 0.3110
REMARK 3 21 2.9800 - 2.9300 1.00 2594 120 0.2596 0.2963
REMARK 3 22 2.9300 - 2.8900 1.00 2569 155 0.2612 0.3285
REMARK 3 23 2.8900 - 2.8400 1.00 2541 156 0.2621 0.2965
REMARK 3 24 2.8400 - 2.8000 1.00 2580 155 0.2609 0.2951
REMARK 3 25 2.8000 - 2.7700 1.00 2513 145 0.2676 0.3340
REMARK 3 26 2.7700 - 2.7300 1.00 2614 129 0.2836 0.3176
REMARK 3 27 2.7300 - 2.7000 0.99 2556 128 0.2886 0.3156
REMARK 3 28 2.7000 - 2.6600 0.98 2508 150 0.2853 0.3402
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) : 0.362
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.34
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 17497
REMARK 3 ANGLE : 0.580 23724
REMARK 3 CHIRALITY : 0.044 2585
REMARK 3 PLANARITY : 0.005 3017
REMARK 3 DIHEDRAL : 16.124 6766
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): -11.7180 25.0013 8.1960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1638 T22: 0.2295
REMARK 3 T33: 0.1477 T12: 0.0209
REMARK 3 T13: -0.0096 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.2183 L22: 0.3211
REMARK 3 L33: 0.2380 L12: -0.0989
REMARK 3 L13: -0.1144 L23: 0.2591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0080 S12: 0.0791 S13: 0.0330
REMARK 3 S21: -0.0884 S22: 0.0300 S23: 0.0324
REMARK 3 S31: -0.0318 S32: -0.0052 S33: 0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1232 45.5587 32.4429
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.2343
REMARK 3 T33: 0.2408 T12: 0.0260
REMARK 3 T13: -0.0104 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.2822 L22: 0.1572
REMARK 3 L33: 0.1722 L12: -0.0848
REMARK 3 L13: -0.2021 L23: -0.0237
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: -0.0443 S13: -0.0015
REMARK 3 S21: -0.0216 S22: -0.0611 S23: -0.0192
REMARK 3 S31: -0.0216 S32: 0.0719 S33: -0.0004
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): -85.7143 47.9021 44.3119
REMARK 3 T TENSOR
REMARK 3 T11: 0.0126 T22: 0.5682
REMARK 3 T33: 0.2112 T12: -0.0667
REMARK 3 T13: -0.0141 T23: 0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 0.4315 L22: 0.5564
REMARK 3 L33: 0.2698 L12: 0.2222
REMARK 3 L13: -0.2182 L23: -0.0801
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: 0.4853 S13: -0.1042
REMARK 3 S21: 0.1097 S22: 0.1669 S23: -0.0147
REMARK 3 S31: -0.0927 S32: -0.3390 S33: 0.1910
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D'
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4465 -19.5859 -4.7950
REMARK 3 T TENSOR
REMARK 3 T11: 0.4825 T22: 0.2295
REMARK 3 T33: 0.3533 T12: -0.2802
REMARK 3 T13: 0.0330 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 0.1803 L22: 0.1537
REMARK 3 L33: 0.1554 L12: 0.0007
REMARK 3 L13: 0.0411 L23: 0.1126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0381 S12: 0.0860 S13: -0.0920
REMARK 3 S21: 0.0771 S22: 0.0136 S23: 0.1750
REMARK 3 S31: 0.4238 S32: -0.1065 S33: -0.0108
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 9HH0 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_1292143315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-12
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) : 0.872600
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 : 76253
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.660
REMARK 200 RESOLUTION RANGE LOW (A) : 124.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.15260
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 1.31100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.250
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 (%): 56.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
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 87.58650
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 43.79325
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 131.37975
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, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, H
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, I, J, K
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, L
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 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 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 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 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: 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 NE2 HIS D 438 O2 GB D 601 1.30
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 PHE A 43 -4.37 72.93
REMARK 500 ASP A 54 -158.05 -103.23
REMARK 500 ALA A 62 -168.11 -76.67
REMARK 500 ASN A 106 50.35 -146.59
REMARK 500 PHE A 153 19.48 -140.65
REMARK 500 ALA A 162 79.11 -157.13
REMARK 500 SER A 198 -112.60 59.84
REMARK 500 VAL A 288 90.23 -63.37
REMARK 500 ASP A 297 -76.34 -102.76
REMARK 500 ASP A 324 77.50 -117.05
REMARK 500 MET A 374 -66.60 -125.11
REMARK 500 ILE A 398 -59.16 -127.62
REMARK 500 GLU A 506 -76.67 -99.74
REMARK 500 LYS A 513 72.50 53.64
REMARK 500 PHE B 43 -2.24 72.28
REMARK 500 ASP B 54 -127.56 -113.94
REMARK 500 ASN B 106 50.46 -149.56
REMARK 500 SER B 198 -114.66 58.66
REMARK 500 HIS B 283 86.79 55.00
REMARK 500 VAL B 288 75.05 47.80
REMARK 500 ASP B 297 -73.74 -123.38
REMARK 500 ASP B 324 75.57 -118.65
REMARK 500 MET B 374 -63.97 -132.28
REMARK 500 ILE B 398 -61.42 -128.80
REMARK 500 GLU B 422 31.98 -140.45
REMARK 500 GLU B 506 -85.72 -94.05
REMARK 500 ASP C 54 -119.12 -79.72
REMARK 500 ASN C 106 62.76 60.22
REMARK 500 PHE C 118 12.22 59.52
REMARK 500 ALA C 162 72.45 -167.46
REMARK 500 LYS C 180 -70.48 -80.34
REMARK 500 ASN C 181 47.98 -99.35
REMARK 500 SER C 198 -112.51 59.04
REMARK 500 ASP C 297 -84.21 -84.00
REMARK 500 ASP C 324 69.25 -116.56
REMARK 500 THR C 377 -159.67 -112.99
REMARK 500 GLU C 383 32.59 -91.20
REMARK 500 ILE C 398 -59.52 -130.08
REMARK 500 PRO C 449 2.25 -62.32
REMARK 500 GLU C 506 -66.44 -96.07
REMARK 500 LYS D 12 80.59 -166.38
REMARK 500 LEU D 21 -108.12 55.26
REMARK 500 PHE D 43 -2.28 77.81
REMARK 500 PRO D 53 -84.38 -85.72
REMARK 500 THR D 59 5.81 -155.64
REMARK 500 ALA D 62 -133.64 34.64
REMARK 500 ASN D 63 -152.61 -147.55
REMARK 500 ASP D 91 97.42 -67.87
REMARK 500 PHE D 153 13.63 -146.82
REMARK 500 ALA D 162 63.64 -161.90
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9HH0 A 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HH0 A A0A4X1VEU5 29 557
DBREF1 9HH0 B 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HH0 B A0A4X1VEU5 29 557
DBREF1 9HH0 C 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HH0 C A0A4X1VEU5 29 557
DBREF1 9HH0 D 1 529 UNP A0A4X1VEU5_PIG
DBREF2 9HH0 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 FUC E 2 10
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET MAN F 4 11
HET FUC F 5 10
HET NAG G 1 14
HET FUC G 2 10
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET FUC J 4 10
HET NAG K 1 14
HET NAG K 2 14
HET FUC K 3 10
HET NAG L 1 14
HET NAG L 2 14
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET GOL A 604 6
HET GOL A 605 6
HET GOL A 606 6
HET GB A 607 4
HET GOL A 608 6
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 611 5
HET SO4 A 612 5
HET NAG B 601 14
HET NAG B 602 14
HET PEG B 603 7
HET GB B 604 4
HET GOL B 605 6
HET SO4 B 606 5
HET EDO B 607 4
HET EDO B 608 4
HET EDO B 609 4
HET GB C 601 4
HET GOL C 602 6
HET GOL C 603 6
HET SO4 C 604 5
HET SO4 C 605 5
HET GB D 601 4
HET EDO D 602 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM GB METHYLPHOSPHONIC ACID ESTER GROUP
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NAG 19(C8 H15 N O6)
FORMUL 5 FUC 5(C6 H12 O5)
FORMUL 6 BMA 2(C6 H12 O6)
FORMUL 6 MAN C6 H12 O6
FORMUL 16 GOL 7(C3 H8 O3)
FORMUL 19 GB 4(C H5 O3 P)
FORMUL 21 SO4 7(O4 S 2-)
FORMUL 27 PEG C4 H10 O3
FORMUL 31 EDO 4(C2 H6 O2)
FORMUL 41 HOH *324(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 VAL A 148 LEU A 154 1 7
HELIX 6 AA6 ASN A 165 GLY A 186 1 22
HELIX 7 AA7 SER A 198 LEU A 208 1 11
HELIX 8 AA8 LEU A 209 PHE A 217 5 9
HELIX 9 AA9 SER A 235 GLY A 251 1 17
HELIX 10 AB1 ASN A 256 ASN A 266 1 11
HELIX 11 AB2 ASP A 268 VAL A 277 1 10
HELIX 12 AB3 PHE A 278 VAL A 280 5 3
HELIX 13 AB4 LEU A 302 LEU A 309 1 8
HELIX 14 AB5 GLY A 326 VAL A 331 1 6
HELIX 15 AB6 THR A 346 PHE A 358 1 13
HELIX 16 AB7 SER A 362 MET A 374 1 13
HELIX 17 AB8 GLU A 383 ILE A 398 1 16
HELIX 18 AB9 ILE A 398 MET A 412 1 15
HELIX 19 AC1 PRO A 431 GLY A 435 5 5
HELIX 20 AC2 GLU A 441 PHE A 446 1 6
HELIX 21 AC3 GLY A 447 ASN A 455 5 9
HELIX 22 AC4 THR A 457 GLY A 478 1 22
HELIX 23 AC5 ARG A 515 PHE A 525 1 11
HELIX 24 AC6 PHE A 526 VAL A 529 5 4
HELIX 25 AC7 LEU B 38 ARG B 42 5 5
HELIX 26 AC8 PHE B 76 MET B 81 1 6
HELIX 27 AC9 LEU B 125 ASP B 129 5 5
HELIX 28 AD1 GLY B 130 ARG B 138 1 9
HELIX 29 AD2 VAL B 148 LEU B 154 1 7
HELIX 30 AD3 ASN B 165 ILE B 182 1 18
HELIX 31 AD4 ALA B 183 PHE B 185 5 3
HELIX 32 AD5 SER B 198 LEU B 208 1 11
HELIX 33 AD6 SER B 210 PHE B 217 5 8
HELIX 34 AD7 SER B 235 GLY B 251 1 17
HELIX 35 AD8 ASN B 256 ARG B 265 1 10
HELIX 36 AD9 ASP B 268 VAL B 277 1 10
HELIX 37 AE1 LEU B 302 LEU B 309 1 8
HELIX 38 AE2 GLY B 326 VAL B 331 1 6
HELIX 39 AE3 THR B 346 PHE B 358 1 13
HELIX 40 AE4 SER B 362 MET B 374 1 13
HELIX 41 AE5 GLU B 383 ILE B 398 1 16
HELIX 42 AE6 ILE B 398 GLU B 411 1 14
HELIX 43 AE7 PRO B 431 GLY B 435 5 5
HELIX 44 AE8 GLU B 441 PHE B 446 1 6
HELIX 45 AE9 GLY B 447 ASN B 455 5 9
HELIX 46 AF1 THR B 457 GLY B 478 1 22
HELIX 47 AF2 ARG B 515 PHE B 525 1 11
HELIX 48 AF3 PHE B 526 VAL B 529 5 4
HELIX 49 AF4 LEU C 38 ARG C 42 5 5
HELIX 50 AF5 PHE C 76 MET C 81 1 6
HELIX 51 AF6 LEU C 125 ASP C 129 5 5
HELIX 52 AF7 GLY C 130 ARG C 138 1 9
HELIX 53 AF8 GLY C 149 LEU C 154 1 6
HELIX 54 AF9 ASN C 165 ILE C 182 1 18
HELIX 55 AG1 ALA C 183 PHE C 185 5 3
HELIX 56 AG2 SER C 198 LEU C 208 1 11
HELIX 57 AG3 SER C 210 PHE C 217 5 8
HELIX 58 AG4 SER C 235 ILE C 250 1 16
HELIX 59 AG5 GLU C 257 ASN C 266 1 10
HELIX 60 AG6 ASP C 268 GLU C 276 1 9
HELIX 61 AG7 VAL C 277 VAL C 279 5 3
HELIX 62 AG8 LEU C 302 LEU C 309 1 8
HELIX 63 AG9 GLY C 326 ALA C 334 1 9
HELIX 64 AH1 THR C 346 PHE C 358 1 13
HELIX 65 AH2 SER C 362 MET C 374 1 13
HELIX 66 AH3 GLU C 383 ILE C 398 1 16
HELIX 67 AH4 ILE C 398 MET C 412 1 15
HELIX 68 AH5 PRO C 431 GLY C 435 5 5
HELIX 69 AH6 GLU C 441 PHE C 446 1 6
HELIX 70 AH7 GLY C 447 GLU C 451 5 5
HELIX 71 AH8 THR C 457 GLY C 478 1 22
HELIX 72 AH9 ARG C 515 PHE C 525 1 11
HELIX 73 AI1 PHE C 526 VAL C 529 5 4
HELIX 74 AI2 LEU D 38 ARG D 42 5 5
HELIX 75 AI3 PHE D 76 MET D 81 1 6
HELIX 76 AI4 LEU D 125 ASP D 129 5 5
HELIX 77 AI5 GLY D 130 ARG D 138 1 9
HELIX 78 AI6 GLY D 149 LEU D 154 1 6
HELIX 79 AI7 ASN D 165 ILE D 182 1 18
HELIX 80 AI8 ALA D 183 PHE D 185 5 3
HELIX 81 AI9 SER D 198 LEU D 208 1 11
HELIX 82 AJ1 SER D 210 PHE D 217 5 8
HELIX 83 AJ2 SER D 235 PHE D 249 1 15
HELIX 84 AJ3 ASN D 256 LYS D 267 1 12
HELIX 85 AJ4 ASP D 268 ASN D 275 1 8
HELIX 86 AJ5 LEU D 302 LEU D 309 1 8
HELIX 87 AJ6 GLY D 326 VAL D 331 1 6
HELIX 88 AJ7 THR D 346 PHE D 358 1 13
HELIX 89 AJ8 SER D 362 MET D 374 1 13
HELIX 90 AJ9 GLU D 383 ILE D 398 1 16
HELIX 91 AK1 ILE D 398 GLU D 411 1 14
HELIX 92 AK2 PRO D 431 GLY D 435 5 5
HELIX 93 AK3 GLU D 441 PHE D 446 1 6
HELIX 94 AK4 GLY D 447 ASN D 455 5 9
HELIX 95 AK5 THR D 457 GLY D 478 1 22
HELIX 96 AK6 ARG D 515 PHE D 525 1 11
HELIX 97 AK7 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 ASN A 57 1 O TRP A 56 N ARG A 14
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 7 0
SHEET 2 AA3 3 LYS B 12 ARG B 14 -1 O VAL B 13 N VAL B 6
SHEET 3 AA3 3 ILE B 55 TRP B 56 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 ASN B 17 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
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 ARG B 219 N LEU B 194
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 417 N VAL B 319
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 8 0
SHEET 2 AA5 3 GLY C 11 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 LEU C 95 N ILE C 31
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 LEU D 95 N ILE D 31
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 417 N VAL D 319
SHEET 10 AA711 LYS D 499 LEU D 503 1 O LEU D 501 N PHE D 418
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 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
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 2.04
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.05
SSBOND 7 CYS C 65 CYS C 92 1555 1555 2.03
SSBOND 8 CYS C 252 CYS C 263 1555 1555 2.04
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 E 1 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 601 1555 1555 1.44
LINK OG SER A 198 P1 GB A 607 1555 1555 1.70
LINK ND2 ASN A 241 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 455 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN B 57 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN B 106 C1 NAG B 601 1555 1555 1.44
LINK OG SER B 198 P1 GB B 604 1555 1555 1.71
LINK ND2 ASN B 241 C1 NAG B 602 1555 1555 1.45
LINK ND2 ASN B 341 C1 NAG H 1 1555 1555 1.45
LINK OG SER C 198 P1 GB C 601 1555 1555 1.71
LINK ND2 ASN C 241 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN C 341 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN C 455 C1 NAG K 1 1555 1555 1.44
LINK OG SER D 198 P1 GB D 601 1555 1555 1.73
LINK ND2 ASN D 341 C1 NAG L 1 1555 1555 1.44
LINK O6 NAG E 1 C1 FUC E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O6 NAG F 1 C1 FUC F 5 1555 1555 1.44
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.45
LINK O6 NAG G 1 C1 FUC G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O6 NAG J 1 C1 FUC J 4 1555 1555 1.44
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O6 NAG K 1 C1 FUC K 3 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 -0.06
CISPEP 2 ALA B 101 PRO B 102 0 -0.02
CISPEP 3 ALA C 101 PRO C 102 0 1.41
CISPEP 4 ALA D 101 PRO D 102 0 4.04
CRYST1 124.692 124.692 175.173 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 0.008020 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005709 0.00000
TER 4189 VAL A 529
TER 8363 VAL B 529
TER 12536 VAL C 529
TER 16594 VAL D 529
MASTER 423 0 50 97 53 0 0 617365 4 506 164
END |