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HEADER HYDROLASE 16-MAR-18 6CQY
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH EMPA AND HI-6
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 CHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BESTER,M.A.GUELTA,S.D.PEGAN,J.J.HEIGHT
REVDAT 1 05-DEC-18 6CQY 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. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 77487
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3880
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 43.8439 - 7.4242 0.99 2856 149 0.1738 0.1904
REMARK 3 2 7.4242 - 5.8973 1.00 2733 149 0.1791 0.2224
REMARK 3 3 5.8973 - 5.1532 1.00 2714 117 0.1605 0.1929
REMARK 3 4 5.1532 - 4.6826 1.00 2685 152 0.1348 0.1509
REMARK 3 5 4.6826 - 4.3473 1.00 2636 142 0.1260 0.1389
REMARK 3 6 4.3473 - 4.0912 1.00 2662 151 0.1418 0.1750
REMARK 3 7 4.0912 - 3.8864 1.00 2624 143 0.1389 0.1617
REMARK 3 8 3.8864 - 3.7174 1.00 2626 132 0.1469 0.1885
REMARK 3 9 3.7174 - 3.5743 1.00 2649 148 0.1717 0.1717
REMARK 3 10 3.5743 - 3.4510 1.00 2648 123 0.1806 0.2133
REMARK 3 11 3.4510 - 3.3432 1.00 2652 116 0.1882 0.1963
REMARK 3 12 3.3432 - 3.2476 1.00 2585 167 0.1830 0.2135
REMARK 3 13 3.2476 - 3.1622 1.00 2626 121 0.1873 0.2292
REMARK 3 14 3.1622 - 3.0850 1.00 2599 130 0.1854 0.2182
REMARK 3 15 3.0850 - 3.0149 1.00 2596 160 0.1899 0.2545
REMARK 3 16 3.0149 - 2.9508 1.00 2653 111 0.1918 0.2480
REMARK 3 17 2.9508 - 2.8918 1.00 2604 139 0.2003 0.2113
REMARK 3 18 2.8918 - 2.8372 1.00 2582 130 0.2067 0.2440
REMARK 3 19 2.8372 - 2.7865 1.00 2619 148 0.2056 0.2480
REMARK 3 20 2.7865 - 2.7393 1.00 2589 137 0.2040 0.2685
REMARK 3 21 2.7393 - 2.6951 1.00 2610 107 0.2102 0.2833
REMARK 3 22 2.6951 - 2.6537 1.00 2612 155 0.2039 0.2509
REMARK 3 23 2.6537 - 2.6146 1.00 2570 147 0.2138 0.2424
REMARK 3 24 2.6146 - 2.5778 1.00 2569 154 0.2069 0.2640
REMARK 3 25 2.5778 - 2.5430 1.00 2593 146 0.2216 0.2571
REMARK 3 26 2.5430 - 2.5100 1.00 2594 134 0.2228 0.2472
REMARK 3 27 2.5100 - 2.4786 1.00 2614 135 0.2400 0.2914
REMARK 3 28 2.4786 - 2.4487 0.98 2507 137 0.2627 0.2956
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.200
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 : 0.004 8801
REMARK 3 ANGLE : 0.806 12051
REMARK 3 CHIRALITY : 0.072 1300
REMARK 3 PLANARITY : 0.006 1581
REMARK 3 DIHEDRAL : 15.209 5153
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 4:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9984 -44.1099 49.8250
REMARK 3 T TENSOR
REMARK 3 T11: 0.8465 T22: 0.6717
REMARK 3 T33: 0.5311 T12: -0.1070
REMARK 3 T13: 0.1024 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 2.3268 L22: 9.4913
REMARK 3 L33: 7.0912 L12: -0.6393
REMARK 3 L13: 2.3258 L23: -1.0763
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: -0.8153 S13: -0.0326
REMARK 3 S21: 0.6944 S22: -0.1626 S23: 0.9475
REMARK 3 S31: 0.6987 S32: -0.7624 S33: 0.1812
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 14:256)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1365 -32.8993 35.5450
REMARK 3 T TENSOR
REMARK 3 T11: 0.4107 T22: 0.3980
REMARK 3 T33: 0.3080 T12: 0.0485
REMARK 3 T13: 0.0388 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 2.2413 L22: 1.4400
REMARK 3 L33: 3.0787 L12: 0.2225
REMARK 3 L13: -0.9429 L23: -0.4222
REMARK 3 S TENSOR
REMARK 3 S11: -0.0770 S12: -0.3281 S13: -0.0349
REMARK 3 S21: 0.1272 S22: 0.0155 S23: -0.0018
REMARK 3 S31: 0.4313 S32: 0.1374 S33: 0.0557
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 257:313)
REMARK 3 ORIGIN FOR THE GROUP (A): 65.2127 -21.5372 32.8128
REMARK 3 T TENSOR
REMARK 3 T11: 0.3670 T22: 0.6389
REMARK 3 T33: 0.4419 T12: -0.0339
REMARK 3 T13: 0.0130 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 2.2740 L22: 2.7826
REMARK 3 L33: 4.1385 L12: -0.5598
REMARK 3 L13: -0.1047 L23: 0.5242
REMARK 3 S TENSOR
REMARK 3 S11: -0.1451 S12: -0.4387 S13: 0.2498
REMARK 3 S21: 0.0985 S22: 0.0560 S23: -0.1756
REMARK 3 S31: -0.3781 S32: 0.7376 S33: 0.0719
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 314:490)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1704 -27.4348 13.1121
REMARK 3 T TENSOR
REMARK 3 T11: 0.3666 T22: 0.3877
REMARK 3 T33: 0.3034 T12: -0.0165
REMARK 3 T13: 0.0054 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 1.8067 L22: 1.3777
REMARK 3 L33: 2.8624 L12: 0.2657
REMARK 3 L13: -1.0828 L23: -0.6718
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.1881 S13: 0.0519
REMARK 3 S21: -0.1504 S22: 0.0550 S23: 0.0759
REMARK 3 S31: 0.2247 S32: -0.2590 S33: -0.0258
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 491:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9106 -36.8334 6.4169
REMARK 3 T TENSOR
REMARK 3 T11: 0.6314 T22: 0.4428
REMARK 3 T33: 0.3287 T12: -0.0329
REMARK 3 T13: 0.0670 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 3.3593 L22: 2.0065
REMARK 3 L33: 2.7842 L12: -0.8227
REMARK 3 L13: 0.3370 L23: -0.0697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0264 S12: 0.4679 S13: -0.3342
REMARK 3 S21: -0.1038 S22: -0.0655 S23: 0.0672
REMARK 3 S31: 0.5802 S32: -0.1198 S33: 0.1131
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 4:257)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9285 -32.9378 40.0538
REMARK 3 T TENSOR
REMARK 3 T11: 0.3139 T22: 0.3649
REMARK 3 T33: 0.3562 T12: -0.1169
REMARK 3 T13: -0.0022 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 1.1578 L22: 1.4206
REMARK 3 L33: 2.5251 L12: -0.4566
REMARK 3 L13: 0.0000 L23: 0.1510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0597 S12: -0.1037 S13: 0.0444
REMARK 3 S21: 0.1942 S22: -0.0456 S23: 0.0458
REMARK 3 S31: -0.0798 S32: -0.2273 S33: -0.0098
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 258:542)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7048 -46.1203 23.0265
REMARK 3 T TENSOR
REMARK 3 T11: 0.3591 T22: 0.4352
REMARK 3 T33: 0.3832 T12: -0.0811
REMARK 3 T13: 0.0107 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.7250 L22: 0.8442
REMARK 3 L33: 2.2645 L12: 0.0343
REMARK 3 L13: -0.0099 L23: 0.2537
REMARK 3 S TENSOR
REMARK 3 S11: 0.0540 S12: 0.1337 S13: -0.0778
REMARK 3 S21: -0.0344 S22: -0.1192 S23: 0.0552
REMARK 3 S31: 0.2381 S32: -0.2006 S33: 0.0586
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 6CQY 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_1000233254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-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-ID
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 : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77545
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.449
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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 (%): 71.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
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 108.10700
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 216.21400
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 216.21400
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 108.10700
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: 6160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 34.0 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 -0.500000 0.866025 0.000000 105.15200
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
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 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 NH1 ARG A 516 O HOH A 701 1.50
REMARK 500 O7 NAG B 602 O HOH B 701 1.51
REMARK 500 OE1 GLN B 291 NE2 GLN B 369 1.65
REMARK 500 OD1 ASN A 265 O7 NAG A 604 1.70
REMARK 500 ND2 ASN B 350 C1 NAG B 602 1.72
REMARK 500 OD1 ASP A 514 O HOH A 701 1.77
REMARK 500 OD1 ASP A 304 O HOH A 702 2.13
REMARK 500 O HOH B 793 O HOH B 901 2.16
REMARK 500 OD1 ASN B 350 N SER B 352 2.19
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 -5.66 70.70
REMARK 500 SER A 203 -122.88 60.59
REMARK 500 ASP A 306 -86.12 -99.84
REMARK 500 VAL A 407 -65.41 -125.83
REMARK 500 PHE B 47 -5.77 75.33
REMARK 500 ALA B 62 52.66 -115.99
REMARK 500 SER B 203 -123.63 56.96
REMARK 500 PRO B 258 -178.33 -45.71
REMARK 500 ASP B 306 -85.42 -95.90
REMARK 500 VAL B 407 -60.07 -124.39
REMARK 500 SER B 462 20.77 -79.81
REMARK 500 ASN B 464 33.85 -95.84
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 A 946 DISTANCE = 7.90 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 NAG B 602
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue VX B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 601 through NAG A 603 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800 601 through NAG B 603
REMARK 900
REMARK 900 RELATED ENTRIES
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
REMARK 900 RELATED ID: 6CQX RELATED DB: PDB
DBREF 6CQY A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6CQY 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 FUC A 601 10
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET HI6 A 605 21
HET VX A 606 7
HET FUC B 601 10
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET HI6 B 605 21
HET VX B 606 7
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETSYN HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-
HETSYN 2 HI6 PYRIDINIUM DIMETHYLETHER
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 5 HI6 2(C14 H16 N4 O3 2+)
FORMUL 6 VX 2(C3 H9 O3 P)
FORMUL 11 HOH *510(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 SER A 215 1 13
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 MET A 241 VAL A 255 1 15
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 ARG A 534 ALA A 542 1 9
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 GLY B 240 GLY B 256 1 17
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 ALA B 542 1 9
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 THR A 103 N SER A 30
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 TRP A 117 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
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 PHE A 430 N VAL A 330
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 2 VAL A 239 GLY A 240 0
SHEET 2 AA4 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA5 3 LEU B 9 VAL B 12 0
SHEET 2 AA5 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA5 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA611 ILE B 20 LEU B 22 0
SHEET 2 AA611 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA611 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA611 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA611 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 AA611 GLY B 192 GLU B 202 1 O SER B 196 N VAL B 114
SHEET 7 AA611 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA611 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA611 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA611 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA611 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA7 2 VAL B 68 CYS B 69 0
SHEET 2 AA7 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.03
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.03
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
LINK ND2 ASN A 265 C1 NAG A 604 1555 1555 1.50
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.56
LINK ND2 ASN B 464 C1 NAG B 604 1555 1555 1.44
LINK C1 FUC A 601 O6 NAG A 602 1555 1555 1.44
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.44
LINK C1 FUC B 601 O6 NAG B 602 1555 1555 1.44
LINK O4 NAG B 602 C1 NAG B 603 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -1.43
CISPEP 2 CYS A 257 PRO A 258 0 -15.69
CISPEP 3 TYR B 105 PRO B 106 0 -2.52
CISPEP 4 PRO B 258 PRO B 259 0 -13.50
CISPEP 5 ALA B 497 PRO B 498 0 -0.12
SITE 1 AC1 12 TYR A 72 ASP A 74 TYR A 124 VAL A 282
SITE 2 AC1 12 GLU A 285 TRP A 286 VAL A 294 PHE A 295
SITE 3 AC1 12 TYR A 337 TYR A 341 HOH A 765 HOH A 786
SITE 1 AC2 9 TRP A 86 GLY A 120 GLY A 121 GLU A 202
SITE 2 AC2 9 SER A 203 TYR A 337 HIS A 447 GLY A 448
SITE 3 AC2 9 HOH A 709
SITE 1 AC3 13 TYR B 72 ASP B 74 TYR B 124 VAL B 282
SITE 2 AC3 13 GLU B 285 TRP B 286 VAL B 294 PHE B 295
SITE 3 AC3 13 TYR B 337 TYR B 341 VX B 606 HOH B 827
SITE 4 AC3 13 HOH B 830
SITE 1 AC4 7 TRP B 86 GLY B 121 GLU B 202 SER B 203
SITE 2 AC4 7 TYR B 337 GLY B 448 HI6 B 605
SITE 1 AC5 5 ASN A 265 THR A 267 HOH A 708 HOH A 717
SITE 2 AC5 5 HOH A 781
SITE 1 AC6 5 PRO A 344 GLY A 345 SER A 347 ASN A 350
SITE 2 AC6 5 HOH A 733
SITE 1 AC7 1 ASN B 464
SITE 1 AC8 5 PRO B 344 GLY B 345 SER B 347 ASN B 350
SITE 2 AC8 5 HOH B 701
CRYST1 105.152 105.152 324.321 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 0.009510 0.005491 0.000000 0.00000
SCALE2 0.000000 0.010981 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003083 0.00000
TER 4166 ALA A 542
TER 8320 ALA B 542
MASTER 479 0 12 52 34 0 19 6 8917 2 175 84
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