6cqx-pdb | HEADER HYDROLASE 16-MAR-18 6CQX
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY VX(+)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BESTER,M.A.GUELTA,S.D.PEGAN,J.J.HEIGHT
REVDAT 1 05-DEC-18 6CQX 0
JRNL AUTH S.M.BESTER,M.A.GUELTA,J.CHEUNG,M.D.WINEMILLER,S.Y.BAE,
JRNL AUTH 2 J.MYSLINSKI,S.D.PEGAN,J.J.HEIGHT
JRNL TITL STRUCTURAL INSIGHTS OF STEREOSPECIFIC INHIBITION OF HUMAN
JRNL TITL 2 ACETYLCHOLINESTERASE BY VX AND SUBSEQUENT REACTIVATION BY
JRNL TITL 3 HI-6.
JRNL REF CHEM. RES. TOXICOL. 2018
JRNL REFN ISSN 1520-5010
JRNL PMID 30462502
JRNL DOI 10.1021/ACS.CHEMRESTOX.8B00294
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 81623
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4059
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 41.2404 - 7.3611 0.96 2807 153 0.1651 0.1937
REMARK 3 2 7.3611 - 5.8480 1.00 2770 146 0.1623 0.1853
REMARK 3 3 5.8480 - 5.1103 1.00 2783 128 0.1471 0.1558
REMARK 3 4 5.1103 - 4.6438 1.00 2726 147 0.1208 0.1633
REMARK 3 5 4.6438 - 4.3113 1.00 2686 152 0.1142 0.1303
REMARK 3 6 4.3113 - 4.0574 1.00 2703 145 0.1229 0.1461
REMARK 3 7 4.0574 - 3.8543 1.00 2700 154 0.1246 0.1514
REMARK 3 8 3.8543 - 3.6867 1.00 2710 120 0.1353 0.1705
REMARK 3 9 3.6867 - 3.5448 1.00 2682 156 0.1447 0.1593
REMARK 3 10 3.5448 - 3.4226 1.00 2691 134 0.1559 0.1971
REMARK 3 11 3.4226 - 3.3156 1.00 2673 119 0.1519 0.2113
REMARK 3 12 3.3156 - 3.2209 1.00 2670 160 0.1589 0.2085
REMARK 3 13 3.2209 - 3.1361 1.00 2644 132 0.1721 0.1832
REMARK 3 14 3.1361 - 3.0596 1.00 2698 131 0.1679 0.1962
REMARK 3 15 3.0596 - 2.9901 1.00 2604 162 0.1597 0.1996
REMARK 3 16 2.9901 - 2.9265 1.00 2689 110 0.1711 0.2380
REMARK 3 17 2.9265 - 2.8679 1.00 2708 129 0.1752 0.2089
REMARK 3 18 2.8679 - 2.8138 1.00 2646 149 0.1776 0.2375
REMARK 3 19 2.8138 - 2.7636 1.00 2625 136 0.1776 0.2208
REMARK 3 20 2.7636 - 2.7167 1.00 2666 147 0.1832 0.2169
REMARK 3 21 2.7167 - 2.6729 1.00 2679 105 0.1776 0.2587
REMARK 3 22 2.6729 - 2.6318 1.00 2609 160 0.1888 0.2437
REMARK 3 23 2.6318 - 2.5931 1.00 2663 136 0.1875 0.2221
REMARK 3 24 2.5931 - 2.5566 1.00 2614 155 0.1856 0.2253
REMARK 3 25 2.5566 - 2.5220 1.00 2641 149 0.1932 0.2453
REMARK 3 26 2.5220 - 2.4893 1.00 2646 145 0.2004 0.2349
REMARK 3 27 2.4893 - 2.4582 1.00 2635 142 0.2063 0.2478
REMARK 3 28 2.4582 - 2.4286 1.00 2654 129 0.2154 0.2259
REMARK 3 29 2.4286 - 2.4003 0.95 2542 128 0.2307 0.2649
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 8781
REMARK 3 ANGLE : 0.990 12020
REMARK 3 CHIRALITY : 0.057 1301
REMARK 3 PLANARITY : 0.007 1576
REMARK 3 DIHEDRAL : 5.555 6976
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:257)
REMARK 3 ORIGIN FOR THE GROUP (A): -57.2108 32.8370 -18.0806
REMARK 3 T TENSOR
REMARK 3 T11: 0.2683 T22: 0.1846
REMARK 3 T33: 0.1798 T12: -0.0011
REMARK 3 T13: 0.0274 T23: -0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 2.0703 L22: 1.6226
REMARK 3 L33: 2.8808 L12: -0.5665
REMARK 3 L13: -0.4439 L23: 0.8959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: -0.1102 S13: 0.0220
REMARK 3 S21: 0.1610 S22: -0.0243 S23: 0.0166
REMARK 3 S31: 0.1590 S32: -0.2456 S33: 0.0353
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 258:315)
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3249 23.9844 -21.8544
REMARK 3 T TENSOR
REMARK 3 T11: 0.3970 T22: 0.3303
REMARK 3 T33: 0.3020 T12: 0.1371
REMARK 3 T13: 0.0420 T23: -0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 5.0519 L22: 4.3977
REMARK 3 L33: 3.7149 L12: 1.1255
REMARK 3 L13: 2.3323 L23: 2.0251
REMARK 3 S TENSOR
REMARK 3 S11: -0.1581 S12: 0.2635 S13: -0.0672
REMARK 3 S21: 0.0948 S22: 0.2399 S23: -0.3839
REMARK 3 S31: 0.4680 S32: 0.5799 S33: -0.0737
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 316:542)
REMARK 3 ORIGIN FOR THE GROUP (A): -54.3431 35.6317 -42.7376
REMARK 3 T TENSOR
REMARK 3 T11: 0.2931 T22: 0.2729
REMARK 3 T33: 0.1954 T12: 0.0446
REMARK 3 T13: -0.0082 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 2.1556 L22: 1.1750
REMARK 3 L33: 2.8368 L12: -0.2718
REMARK 3 L13: -1.3541 L23: 0.6246
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: 0.1685 S13: 0.0503
REMARK 3 S21: -0.1802 S22: -0.0318 S23: -0.0602
REMARK 3 S31: -0.1737 S32: -0.1847 S33: -0.0160
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 4:254)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8711 -13.6224 -13.9388
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.2821
REMARK 3 T33: 0.2147 T12: 0.0594
REMARK 3 T13: -0.0103 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 0.9317 L22: 1.8261
REMARK 3 L33: 1.9697 L12: 0.1218
REMARK 3 L13: 0.1533 L23: 0.0626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: -0.1912 S13: 0.0220
REMARK 3 S21: 0.0388 S22: -0.0538 S23: -0.0373
REMARK 3 S31: -0.1098 S32: -0.0361 S33: -0.0104
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 255:322)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9037 -3.4255 -29.9567
REMARK 3 T TENSOR
REMARK 3 T11: 0.4355 T22: 0.3089
REMARK 3 T33: 0.2126 T12: 0.0646
REMARK 3 T13: -0.0128 T23: 0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 1.8416 L22: 7.7543
REMARK 3 L33: 2.2463 L12: -1.8132
REMARK 3 L13: -0.7892 L23: 3.1634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0340 S12: 0.1859 S13: 0.0607
REMARK 3 S21: -0.8443 S22: -0.1401 S23: 0.1492
REMARK 3 S31: -0.3860 S32: 0.0287 S33: 0.1185
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 323:542)
REMARK 3 ORIGIN FOR THE GROUP (A): -44.7606 -25.1480 -30.9171
REMARK 3 T TENSOR
REMARK 3 T11: 0.2397 T22: 0.2728
REMARK 3 T33: 0.2379 T12: 0.0183
REMARK 3 T13: -0.0314 T23: -0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 2.0020 L22: 1.0685
REMARK 3 L33: 4.1261 L12: -0.5606
REMARK 3 L13: 1.1691 L23: -0.7235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: 0.0152 S13: -0.0201
REMARK 3 S21: -0.1530 S22: -0.0326 S23: 0.1490
REMARK 3 S31: 0.0433 S32: -0.4391 S33: 0.0197
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 6CQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81653
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.200
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: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 TO 21% PEG 3350, 0.17 - 0.21M
REMARK 280 POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-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 107.96767
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 215.93533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 215.93533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 107.96767
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -107.96767
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 GLY A 2
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 PRO A 492
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 PRO B 492
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 ALA B 497
REMARK 465 THR B 543
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 OG SER A 203 P1 VX A 601 1.32
REMARK 500 ND2 ASN A 350 O5 NAG A 603 1.77
REMARK 500 O3 FUC A 607 O4 NAG A 609 2.04
REMARK 500 OG SER A 203 O1 VX A 601 2.06
REMARK 500 CG ASN A 265 C1 NAG A 608 2.17
REMARK 500 OG SER A 203 O2 VX A 601 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 GLU B 166 N - CA - C ANGL. DEV. = 16.4 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 PHE A 47 -4.37 79.25
REMARK 500 ALA A 62 68.52 -100.08
REMARK 500 ALA A 167 71.84 -151.51
REMARK 500 SER A 203 -118.60 53.64
REMARK 500 PHE A 295 -63.22 -105.43
REMARK 500 ASP A 306 -84.96 -103.22
REMARK 500 VAL A 407 -62.87 -126.52
REMARK 500 PHE B 47 -6.94 79.53
REMARK 500 ALA B 62 50.85 -111.03
REMARK 500 PHE B 158 10.41 -141.58
REMARK 500 SER B 203 -120.29 56.13
REMARK 500 ARG B 296 37.40 -90.38
REMARK 500 ASP B 306 -85.21 -103.15
REMARK 500 TYR B 341 32.84 -90.07
REMARK 500 VAL B 367 77.74 -118.59
REMARK 500 VAL B 407 -60.30 -127.19
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 A1127 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B1190 DISTANCE = 5.99 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 VX A 601
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PE A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 607 through NAG A 609 bound to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through FUC A 604 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800 to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800 602 through NAG B 604 bound to ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VX B 601 and SER B
REMARK 800 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6CQY RELATED DB: PDB
REMARK 900 RELATED ID: 6CQZ RELATED DB: PDB
REMARK 900 RELATED ID: 6CQT RELATED DB: PDB
REMARK 900 RELATED ID: 6CQU RELATED DB: PDB
REMARK 900 RELATED ID: 6CQV RELATED DB: PDB
REMARK 900 RELATED ID: 6CQW RELATED DB: PDB
DBREF 6CQX A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6CQX B 2 543 UNP P22303 ACES_HUMAN 33 574
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 B 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 B 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 B 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 B 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 B 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 B 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 B 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 B 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 B 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 B 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 B 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 B 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 B 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 B 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 B 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 B 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 B 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 B 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 B 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 B 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 B 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 B 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 B 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 B 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 B 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 B 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 B 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 B 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 B 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 B 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 B 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 B 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 B 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 B 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 B 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 B 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 B 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 B 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 B 542 PHE LEU PRO LYS LEU LEU SER ALA THR
HET VX A 601 6
HET NAG A 602 14
HET NAG A 603 14
HET FUC A 604 10
HET NAG A 605 14
HET 7PE A 606 21
HET FUC A 607 10
HET NAG A 608 14
HET NAG A 609 14
HET VX B 601 6
HET FUC B 602 10
HET NAG B 603 14
HET NAG B 604 14
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM 7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)
HETNAM 2 7PE ETHOXY)ETHANOL
HETSYN 7PE POLYETHYLENE GLYCOL FRAGMENT
FORMUL 3 VX 2(C3 H9 O3 P)
FORMUL 4 NAG 7(C8 H15 N O6)
FORMUL 4 FUC 3(C6 H12 O5)
FORMUL 6 7PE C14 H30 O7
FORMUL 10 HOH *917(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 LEU A 214 1 12
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 GLY A 240 VAL A 255 1 16
HELIX 12 AB3 ASN A 265 THR A 275 1 11
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 ALA A 318 1 8
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 PHE A 535 SER A 541 1 7
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 MET B 241 VAL B 255 1 15
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 GLU B 285 1 9
HELIX 40 AE4 TRP B 286 LEU B 289 5 4
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 TYR B 382 1 12
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 LEU A 22 0
SHEET 2 AA211 VAL A 29 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O SER A 196 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA511 ILE B 20 LEU B 22 0
SHEET 2 AA511 VAL B 29 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA511 ARG B 224 GLN B 228 1 O VAL B 226 N LEU B 199
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 239 GLY B 240 0
SHEET 2 AA6 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 1.93
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 1.96
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 265 C1 NAG A 608 1555 1555 1.45
LINK ND2 ASN A 350 C1 NAG A 603 1555 1555 1.47
LINK ND2 ASN A 464 C1 NAG A 605 1555 1555 1.55
LINK OG SER B 203 P1 VX B 601 1555 1555 1.41
LINK ND2 ASN B 350 C1 NAG B 603 1555 1555 1.28
LINK ND2 ASN B 350 O5 NAG B 603 1555 1555 1.32
LINK C1 NAG A 602 O4 NAG A 603 1555 1555 1.44
LINK O6 NAG A 603 C1 FUC A 604 1555 1555 1.44
LINK C1 FUC A 607 O6 NAG A 608 1555 1555 1.44
LINK O4 NAG A 608 C1 NAG A 609 1555 1555 1.44
LINK C1 FUC B 602 O6 NAG B 603 1555 1555 1.44
LINK O4 NAG B 603 C1 NAG B 604 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 2.33
CISPEP 2 CYS A 257 PRO A 258 0 -19.08
CISPEP 3 TYR B 105 PRO B 106 0 -3.85
SITE 1 AC1 8 GLY A 121 GLY A 122 SER A 203 ALA A 204
SITE 2 AC1 8 TRP A 236 PHE A 295 PHE A 297 HIS A 447
SITE 1 AC2 5 ASP A 304 GLY A 305 ASP A 306 SER A 309
SITE 2 AC2 5 ASN B 283
SITE 1 AC3 4 ASN A 265 HOH A 701 HOH A 761 HOH B 977
SITE 1 AC4 5 GLY A 345 SER A 347 ASN A 350 HOH A 764
SITE 2 AC4 5 HOH A 921
SITE 1 AC5 3 SER A 462 ASN A 464 HOH A 709
SITE 1 AC6 7 PRO B 344 GLY B 345 SER B 347 ASN B 350
SITE 2 AC6 7 HOH B 856 HOH B 909 HOH B1074
SITE 1 AC7 14 GLY B 121 GLY B 122 GLU B 202 ALA B 204
SITE 2 AC7 14 GLY B 205 ALA B 206 ALA B 207 GLN B 228
SITE 3 AC7 14 SER B 229 GLY B 230 TRP B 236 PHE B 297
SITE 4 AC7 14 PHE B 338 HIS B 447
CRYST1 104.934 104.934 323.903 90.00 90.00 120.00 P 31 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009530 0.005502 0.000000 0.00000
SCALE2 0.000000 0.011004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003087 0.00000
TER 4145 ALA A 542
TER 8325 ALA B 542
MASTER 484 0 13 52 32 0 14 6 9324 2 178 84
END
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