| 6ntk-pdb | HEADER HYDROLASE/HYDROLASE INHIBITOR 29-JAN-19 6NTK
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY A-232
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 6NTK 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. 2.41 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) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 75891
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3795
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 46.4952 - 7.2107 0.95 2985 159 0.1733 0.1933
REMARK 3 2 7.2107 - 5.7267 0.97 2871 162 0.1758 0.1849
REMARK 3 3 5.7267 - 5.0038 0.97 2850 166 0.1593 0.1896
REMARK 3 4 5.0038 - 4.5467 0.98 2867 123 0.1299 0.1462
REMARK 3 5 4.5467 - 4.2211 0.99 2868 146 0.1338 0.1462
REMARK 3 6 4.2211 - 3.9723 0.99 2856 166 0.1357 0.1557
REMARK 3 7 3.9723 - 3.7735 0.98 2823 164 0.1421 0.1740
REMARK 3 8 3.7735 - 3.6093 0.99 2806 171 0.1567 0.1628
REMARK 3 9 3.6093 - 3.4704 0.99 2838 172 0.1661 0.2005
REMARK 3 10 3.4704 - 3.3507 0.99 2861 140 0.1745 0.1965
REMARK 3 11 3.3507 - 3.2459 0.99 2835 148 0.1724 0.2276
REMARK 3 12 3.2459 - 3.1532 1.00 2840 148 0.1855 0.2361
REMARK 3 13 3.1532 - 3.0702 0.99 2856 140 0.1839 0.2273
REMARK 3 14 3.0702 - 2.9953 1.00 2813 155 0.1915 0.2152
REMARK 3 15 2.9953 - 2.9272 1.00 2837 152 0.1957 0.2511
REMARK 3 16 2.9272 - 2.8649 0.99 2861 129 0.1955 0.2465
REMARK 3 17 2.8649 - 2.8076 0.99 2843 141 0.1988 0.2172
REMARK 3 18 2.8076 - 2.7547 0.98 2721 161 0.2020 0.2286
REMARK 3 19 2.7547 - 2.7055 0.97 2779 137 0.1993 0.2183
REMARK 3 20 2.7055 - 2.6596 0.95 2759 129 0.2018 0.2270
REMARK 3 21 2.6596 - 2.6167 0.93 2637 118 0.1991 0.2393
REMARK 3 22 2.6167 - 2.5765 0.90 2563 132 0.2079 0.2208
REMARK 3 23 2.5765 - 2.5386 0.85 2456 127 0.2152 0.2730
REMARK 3 24 2.5386 - 2.5028 0.78 2174 121 0.2168 0.2682
REMARK 3 25 2.5028 - 2.4690 0.71 2016 109 0.2375 0.2794
REMARK 3 26 2.4690 - 2.4369 0.66 1857 98 0.2370 0.2820
REMARK 3 27 2.4369 - 2.4065 0.57 1624 81 0.2328 0.2919
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.180
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 : 0.003 8677
REMARK 3 ANGLE : 0.695 11846
REMARK 3 CHIRALITY : 0.045 1273
REMARK 3 PLANARITY : 0.005 1548
REMARK 3 DIHEDRAL : 3.553 5046
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3286 59.2811 359.4564
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.1979
REMARK 3 T33: 0.1794 T12: 0.0336
REMARK 3 T13: 0.0179 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.5166 L22: 0.2593
REMARK 3 L33: 1.1729 L12: 0.1551
REMARK 3 L13: -0.3752 L23: 0.1592
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: -0.1168 S13: 0.0268
REMARK 3 S21: 0.0478 S22: 0.0200 S23: -0.0220
REMARK 3 S31: 0.1493 S32: 0.1113 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 322:542)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4902 62.1931 335.6959
REMARK 3 T TENSOR
REMARK 3 T11: 0.2005 T22: 0.2215
REMARK 3 T33: 0.2162 T12: -0.0117
REMARK 3 T13: 0.0240 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.2149 L22: -0.0060
REMARK 3 L33: 0.7567 L12: 0.0629
REMARK 3 L13: -0.2640 L23: -0.1213
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: 0.1223 S13: 0.0834
REMARK 3 S21: -0.0863 S22: 0.0050 S23: 0.0298
REMARK 3 S31: 0.0780 S32: -0.1445 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 4:36)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7322 55.7887 381.9516
REMARK 3 T TENSOR
REMARK 3 T11: 0.3936 T22: 0.2708
REMARK 3 T33: 0.2763 T12: -0.0716
REMARK 3 T13: -0.0518 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.0420 L22: 0.0164
REMARK 3 L33: 0.0161 L12: -0.0043
REMARK 3 L13: 0.0137 L23: 0.0127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.1753 S13: 0.0096
REMARK 3 S21: 0.2710 S22: 0.0034 S23: -0.0256
REMARK 3 S31: -0.0081 S32: 0.1358 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 37:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.0918 50.8831 353.8375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.1786
REMARK 3 T33: 0.1772 T12: -0.0417
REMARK 3 T13: -0.0029 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.3805 L22: 0.5753
REMARK 3 L33: 0.9134 L12: -0.0833
REMARK 3 L13: -0.0975 L23: 0.1199
REMARK 3 S TENSOR
REMARK 3 S11: 0.0432 S12: 0.0663 S13: 0.0354
REMARK 3 S21: 0.0559 S22: -0.0622 S23: -0.0308
REMARK 3 S31: 0.0371 S32: -0.0503 S33: -0.0000
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 6NTK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000239399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-15
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 : 81004
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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 (%): 71.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
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 108.13967
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 216.27933
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 216.27933
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 108.13967
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: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 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 648.83800
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 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 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 P09 L0S A 606 1.13
REMARK 500 ND2 ASN A 265 C1 NAG A 604 1.16
REMARK 500 OG SER B 203 P09 L0S B 605 1.25
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 PRO B 258 C - N - CA ANGL. DEV. = 12.3 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 -3.04 73.31
REMARK 500 SER A 203 -131.18 57.60
REMARK 500 ASP A 306 -83.56 -103.23
REMARK 500 VAL A 407 -62.40 -126.93
REMARK 500 PHE B 47 -6.57 72.03
REMARK 500 ALA B 62 50.43 -111.27
REMARK 500 SER B 203 -131.93 60.69
REMARK 500 ASP B 306 -80.40 -101.69
REMARK 500 ASN B 350 -169.97 -126.56
REMARK 500 VAL B 407 -59.22 -125.37
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 A1118 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B1166 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B1167 DISTANCE = 6.34 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 A 604
REMARK 610 L0S A 606
REMARK 610 L0S B 605
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PE A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L0S A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PE B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L0S B 605
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 Poly-Saccharide residues FUC B
REMARK 800 602 through NAG B 604 bound to ASN B 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6NTG RELATED DB: PDB
REMARK 900 RELATED ID: 6NTH RELATED DB: PDB
DBREF 6NTK A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6NTK 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 7PE A 605 21
HET L0S A 606 12
HET 7PE B 601 21
HET FUC B 602 10
HET NAG B 603 14
HET NAG B 604 14
HET L0S B 605 12
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 L0S METHYL (R)-N-[(1E)-1-(DIETHYLAMINO)ETHYLIDENE]-P-
HETNAM 2 L0S METHYLPHOSPHONAMIDATE
HETSYN 7PE POLYETHYLENE GLYCOL FRAGMENT
HETSYN L0S A-232
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 5 7PE 2(C14 H30 O7)
FORMUL 6 L0S 2(C8 H19 N2 O2 P)
FORMUL 10 HOH *885(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 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 ARG B 274 1 9
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 ALA B 420 1 14
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 GLY A 15 N VAL A 12
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 VAL A 101 N PHE A 32
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 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 VAL B 101 N PHE B 32
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 ASP B 193 N THR B 112
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
SHEET 1 AA7 2 VAL B 239 GLY B 240 0
SHEET 2 AA7 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 2.04
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 1.85
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.01
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B 603 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 B 602 O6 NAG B 603 1555 1555 1.43
LINK O4 NAG B 603 C1 NAG B 604 1555 1555 1.46
CISPEP 1 TYR A 105 PRO A 106 0 4.09
CISPEP 2 CYS A 257 PRO A 258 0 -3.48
CISPEP 3 TYR B 105 PRO B 106 0 -0.68
SITE 1 AC1 3 ASN A 265 HOH A 888 HOH A 974
SITE 1 AC2 9 GLY A 163 ASP A 304 GLY A 305 SER A 309
SITE 2 AC2 9 HOH A 812 HOH A 930 HOH A 956 HOH A1027
SITE 3 AC2 9 ASN B 283
SITE 1 AC3 11 TRP A 86 GLY A 121 GLY A 122 TYR A 133
SITE 2 AC3 11 GLU A 202 SER A 203 ALA A 204 PHE A 295
SITE 3 AC3 11 PHE A 297 TYR A 337 HIS A 447
SITE 1 AC4 7 GLY B 163 MET B 241 ASP B 304 GLY B 305
SITE 2 AC4 7 ASP B 306 SER B 309 ASP B 310
SITE 1 AC5 12 TRP B 86 GLY B 121 GLY B 122 TYR B 133
SITE 2 AC5 12 GLU B 202 SER B 203 ALA B 204 PHE B 295
SITE 3 AC5 12 PHE B 297 TYR B 337 PHE B 338 HIS B 447
SITE 1 AC6 6 GLY A 345 SER A 347 ASN A 350 HOH A 783
SITE 2 AC6 6 HOH A 908 HOH A 942
SITE 1 AC7 3 GLY B 345 ASN B 350 HOH B 990
CRYST1 105.104 105.104 324.419 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 0.009514 0.005493 0.000000 0.00000
SCALE2 0.000000 0.010986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003082 0.00000
TER 4131 ALA A 542
TER 8236 ALA B 542
MASTER 441 0 11 52 34 0 15 6 9275 2 170 84
END
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