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HEADER HYDROLASE/HYDROLASE INHIBITOR 29-JAN-19 6NTL
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY A-234
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, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BESTER,M.A.GUELTA,J.J.HEIGHT,S.D.PEGAN
REVDAT 1 01-JUL-20 6NTL 0
JRNL AUTH J.J.HEIGHT,S.M.BESTER,M.A.GUELTA,S.Y.BAE,J.CHEUNG,S.D.PEGAN
JRNL TITL INSIGHTS INTO INHIBITION OF HUMAN ACETYLCHOLINESTERASE BY
JRNL TITL 2 NOVICHOK, A-SERIES NERVE AGENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 3 NUMBER OF REFLECTIONS : 89717
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 4453
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 46.4196 - 6.9823 0.99 3380 174 0.1888 0.2118
REMARK 3 2 6.9823 - 5.5450 1.00 3257 165 0.1823 0.1912
REMARK 3 3 5.5450 - 4.8449 1.00 3240 164 0.1491 0.1757
REMARK 3 4 4.8449 - 4.4023 1.00 3196 152 0.1261 0.1443
REMARK 3 5 4.4023 - 4.0870 1.00 3178 187 0.1315 0.1615
REMARK 3 6 4.0870 - 3.8461 1.00 3122 191 0.1344 0.1645
REMARK 3 7 3.8461 - 3.6536 1.00 3148 164 0.1424 0.1857
REMARK 3 8 3.6536 - 3.4946 1.00 3139 164 0.1537 0.1812
REMARK 3 9 3.4946 - 3.3601 1.00 3147 169 0.1643 0.1846
REMARK 3 10 3.3601 - 3.2442 1.00 3167 148 0.1594 0.1502
REMARK 3 11 3.2442 - 3.1428 1.00 3143 158 0.1645 0.1950
REMARK 3 12 3.1428 - 3.0530 0.99 3135 156 0.1697 0.1651
REMARK 3 13 3.0530 - 2.9726 1.00 3125 169 0.1683 0.2162
REMARK 3 14 2.9726 - 2.9001 1.00 3092 170 0.1763 0.2061
REMARK 3 15 2.9001 - 2.8342 1.00 3078 185 0.1871 0.1954
REMARK 3 16 2.8342 - 2.7739 1.00 3108 184 0.1832 0.1991
REMARK 3 17 2.7739 - 2.7184 1.00 3111 185 0.1841 0.2144
REMARK 3 18 2.7184 - 2.6671 1.00 3141 143 0.1853 0.2146
REMARK 3 19 2.6671 - 2.6195 1.00 3077 149 0.1928 0.2142
REMARK 3 20 2.6195 - 2.5751 1.00 3137 165 0.1992 0.2563
REMARK 3 21 2.5751 - 2.5335 0.95 2976 140 0.2026 0.2493
REMARK 3 22 2.5335 - 2.4946 0.92 2833 125 0.2171 0.2302
REMARK 3 23 2.4946 - 2.4579 0.91 2839 151 0.2221 0.2834
REMARK 3 24 2.4579 - 2.4233 0.84 2627 142 0.2095 0.2434
REMARK 3 25 2.4233 - 2.3905 0.75 2322 117 0.2250 0.2297
REMARK 3 26 2.3905 - 2.3595 0.65 2019 130 0.2258 0.2662
REMARK 3 27 2.3595 - 2.3300 0.61 1888 72 0.2273 0.2482
REMARK 3 28 2.3300 - 2.3019 0.54 1682 101 0.2213 0.2531
REMARK 3 29 2.3019 - 2.2751 0.50 1563 66 0.2279 0.2703
REMARK 3 30 2.2751 - 2.2500 0.45 1394 67 0.2225 0.2250
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.100
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 8736
REMARK 3 ANGLE : 0.878 11948
REMARK 3 CHIRALITY : 0.047 1290
REMARK 3 PLANARITY : 0.005 1563
REMARK 3 DIHEDRAL : 4.673 6950
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2871 59.3544 358.7623
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.2284
REMARK 3 T33: 0.1679 T12: 0.0538
REMARK 3 T13: 0.0317 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.7328 L22: 1.0820
REMARK 3 L33: 2.2215 L12: 0.3874
REMARK 3 L13: -0.4354 L23: -0.0515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: -0.1510 S13: 0.0414
REMARK 3 S21: 0.0697 S22: 0.0383 S23: -0.0436
REMARK 3 S31: 0.2071 S32: 0.1892 S33: 0.0029
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 322:542)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5326 62.0762 334.9405
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2336
REMARK 3 T33: 0.1731 T12: -0.0178
REMARK 3 T13: 0.0164 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.3189 L22: 0.9336
REMARK 3 L33: 2.1876 L12: 0.3843
REMARK 3 L13: -1.0449 L23: -0.5927
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: 0.1469 S13: 0.0593
REMARK 3 S21: -0.1076 S22: 0.0390 S23: 0.0509
REMARK 3 S31: 0.1051 S32: -0.2044 S33: -0.0137
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 4:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6977 57.3295 371.4611
REMARK 3 T TENSOR
REMARK 3 T11: 0.2308 T22: 0.2245
REMARK 3 T33: 0.1806 T12: -0.0808
REMARK 3 T13: 0.0417 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 1.2867 L22: 1.5177
REMARK 3 L33: 1.3232 L12: -0.2138
REMARK 3 L13: 0.2627 L23: -0.1587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: -0.1907 S13: 0.0406
REMARK 3 S21: 0.3255 S22: -0.0629 S23: 0.0574
REMARK 3 S31: 0.0050 S32: -0.2418 S33: 0.0836
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 110:312)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5967 60.0290 355.3899
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.1897
REMARK 3 T33: 0.1930 T12: -0.0535
REMARK 3 T13: 0.0164 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 1.5504 L22: 1.2597
REMARK 3 L33: 1.6594 L12: -0.4915
REMARK 3 L13: 0.0212 L23: 0.1124
REMARK 3 S TENSOR
REMARK 3 S11: 0.1089 S12: 0.1464 S13: 0.1080
REMARK 3 S21: -0.0080 S22: -0.1027 S23: 0.0383
REMARK 3 S31: -0.1009 S32: -0.1634 S33: -0.0045
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 313:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.4325 40.4558 346.4905
REMARK 3 T TENSOR
REMARK 3 T11: 0.1867 T22: 0.2017
REMARK 3 T33: 0.1963 T12: -0.0270
REMARK 3 T13: 0.0274 T23: -0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 1.0081 L22: 0.8785
REMARK 3 L33: 2.4455 L12: 0.2681
REMARK 3 L13: 0.4249 L23: 0.5265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0306 S12: 0.1015 S13: -0.1169
REMARK 3 S21: -0.0158 S22: -0.0809 S23: 0.0060
REMARK 3 S31: 0.3250 S32: -0.1126 S33: 0.0347
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 6NTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99121
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-21% POLYETHYLENE GLYCOL 3350 (PEG)
REMARK 280 AND 0.17- 0.21M POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
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 107.94800
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 215.89600
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 215.89600
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 107.94800
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: 4630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 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 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 647.68800
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 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
REMARK 465 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
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 P04 L1M A 605 1.23
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 -2.94 75.70
REMARK 500 ALA A 62 63.38 -104.09
REMARK 500 SER A 203 -124.46 61.95
REMARK 500 ASP A 306 -83.41 -97.67
REMARK 500 VAL A 407 -62.46 -126.27
REMARK 500 PHE B 47 -3.15 75.75
REMARK 500 ALA B 62 57.32 -109.44
REMARK 500 SER B 203 -124.89 60.92
REMARK 500 ASP B 306 -80.48 -97.99
REMARK 500 VAL B 407 -62.79 -126.27
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 A1189 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH B1249 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B1250 DISTANCE = 7.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PE A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L1M A 605
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 800 606 through NAG A 608 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 FUC A
REMARK 800 601 through NAG A 603 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800 601 through NAG B 603 bound to ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide L1M B 604 and SER B
REMARK 800 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6NTG RELATED DB: PDB
REMARK 900 RELATED ID: 6NTH RELATED DB: PDB
REMARK 900 RELATED ID: 6NTK RELATED DB: PDB
DBREF 6NTL A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6NTL 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 7PE A 604 21
HET L1M A 605 13
HET FUC A 606 10
HET NAG A 607 14
HET NAG A 608 14
HET FUC B 601 10
HET NAG B 602 14
HET NAG B 603 14
HET L1M B 604 13
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)
HETNAM 2 7PE ETHOXY)ETHANOL
HETNAM L1M ETHYL (R)-N-[(1E)-1-(DIETHYLAMINO)
HETNAM 2 L1M ETHYLIDENE]PHOSPHONAMIDATE
HETSYN 7PE POLYETHYLENE GLYCOL FRAGMENT
FORMUL 3 FUC 3(C6 H12 O5)
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 4 7PE C14 H30 O7
FORMUL 5 L1M 2(C8 H19 N2 O2 P)
FORMUL 9 HOH *1039(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 HIS A 284 1 8
HELIX 14 AB5 GLU A 285 LEU A 289 5 5
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 SER A 541 1 8
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 VAL B 255 1 16
HELIX 38 AE2 ASN B 265 ARG B 276 1 12
HELIX 39 AE3 PRO B 277 HIS B 284 1 8
HELIX 40 AE4 GLU B 285 LEU B 289 5 5
HELIX 41 AE5 THR B 311 ALA B 318 1 8
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 THR B 383 1 13
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 VAL A 29 N LEU A 22
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 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 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 VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
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 145
SHEET 6 AA511 GLY B 192 GLU B 202 1 O SER B 196 N VAL B 114
SHEET 7 AA511 ARG B 224 GLN B 228 1 O ARG B 224 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 68 CYS B 69 0
SHEET 2 AA6 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 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
LINK ND2 ASN A 265 C1 NAG A 607 1555 1555 1.43
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.44
LINK OG SER B 203 P04 L1M B 604 1555 1555 1.40
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.45
LINK C1 FUC A 601 O6 NAG A 602 1555 1555 1.44
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.45
LINK C1 FUC A 606 O6 NAG A 607 1555 1555 1.45
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.43
LINK C1 FUC B 601 O6 NAG B 602 1555 1555 1.44
LINK O4 NAG B 602 C1 NAG B 603 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 1.39
CISPEP 2 CYS A 257 PRO A 258 0 -17.10
CISPEP 3 TYR B 105 PRO B 106 0 1.94
SITE 1 AC1 9 GLY A 163 MET A 241 ASP A 304 GLY A 305
SITE 2 AC1 9 ASP A 306 SER A 309 HOH A 709 HOH A 772
SITE 3 AC1 9 ASN B 283
SITE 1 AC2 12 TRP A 86 GLY A 120 GLY A 121 GLY A 122
SITE 2 AC2 12 TYR A 133 GLU A 202 SER A 203 ALA A 204
SITE 3 AC2 12 TRP A 236 PHE A 295 PHE A 297 HIS A 447
SITE 1 AC3 1 ASN A 265
SITE 1 AC4 7 GLY A 345 SER A 347 ASN A 350 HOH A 707
SITE 2 AC4 7 HOH A 799 HOH A 810 HOH A 992
SITE 1 AC5 5 PRO B 344 GLY B 345 SER B 347 ASN B 350
SITE 2 AC5 5 HOH B 886
SITE 1 AC6 16 TRP B 86 GLY B 121 GLY B 122 TYR B 133
SITE 2 AC6 16 GLU B 202 ALA B 204 GLY B 205 ALA B 206
SITE 3 AC6 16 ALA B 207 GLN B 228 SER B 229 TRP B 236
SITE 4 AC6 16 PHE B 295 PHE B 297 PHE B 338 HIS B 447
CRYST1 104.966 104.966 323.844 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 0.009527 0.005500 0.000000 0.00000
SCALE2 0.000000 0.011001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003088 0.00000
TER 4149 ALA A 542
TER 8297 ALA B 542
MASTER 425 0 12 52 32 0 15 6 9452 2 177 84
END |