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HEADER HYDROLASE 13-JUL-22 8AEN
TITLE HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH ZINC AND N,N,N-TRIMETHYL-2-
TITLE 2 OXO-2-(2-(PYRIDIN-2-YLMETHYLENE)HYDRAZINEYL)ETHAN-1-AMINIUM
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: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS INHIBITOR, COMPLEX, ZINC, ACETYLCHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,J.DIAS,X.BRAZZOLOTTO
REVDAT 1 21-JUN-23 8AEN 0
JRNL AUTH F.NACHON,X.BRAZZOLOTTO,J.DIAS,C.COURAGEUX,W.DROZDZ,X.Y.CAO,
JRNL AUTH 2 A.R.STEFANKIEWICZ,J.M.LEHN
JRNL TITL GRID-TYPE QUATERNARY METALLOSUPRAMOLECULAR COMPOUNDS INHIBIT
JRNL TITL 2 HUMAN CHOLINESTERASES THROUGH DYNAMIC MULTIVALENT
JRNL TITL 3 INTERACTIONS.
JRNL REF CHEMBIOCHEM V. 23 00456 2022
JRNL REFN ESSN 1439-7633
JRNL PMID 36193860
JRNL DOI 10.1002/CBIC.202200456
REMARK 2
REMARK 2 RESOLUTION. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 57675
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2831
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 91.3000 - 8.1600 0.99 2839 119 0.1572 0.2034
REMARK 3 2 8.1600 - 6.4800 1.00 2758 147 0.1593 0.1959
REMARK 3 3 6.4800 - 5.6600 1.00 2776 155 0.1685 0.1757
REMARK 3 4 5.6600 - 5.1400 1.00 2746 124 0.1507 0.1776
REMARK 3 5 5.1400 - 4.7700 1.00 2766 130 0.1261 0.1542
REMARK 3 6 4.7700 - 4.4900 1.00 2729 156 0.1153 0.1483
REMARK 3 7 4.4900 - 4.2700 0.99 2738 144 0.1199 0.1393
REMARK 3 8 4.2700 - 4.0800 1.00 2730 140 0.1379 0.1744
REMARK 3 9 4.0800 - 3.9200 1.00 2734 147 0.1469 0.1806
REMARK 3 10 3.9200 - 3.7900 1.00 2773 120 0.1532 0.1670
REMARK 3 11 3.7900 - 3.6700 1.00 2732 147 0.1520 0.2098
REMARK 3 12 3.6700 - 3.5700 1.00 2742 138 0.1680 0.2423
REMARK 3 13 3.5700 - 3.4700 1.00 2683 168 0.1792 0.2312
REMARK 3 14 3.4700 - 3.3900 1.00 2742 116 0.1964 0.2062
REMARK 3 15 3.3900 - 3.3100 1.00 2773 118 0.2336 0.2280
REMARK 3 16 3.3100 - 3.2400 1.00 2705 140 0.2395 0.2854
REMARK 3 17 3.2400 - 3.1700 1.00 2712 183 0.2399 0.2964
REMARK 3 18 3.1700 - 3.1100 1.00 2692 135 0.2425 0.2765
REMARK 3 19 3.1100 - 3.0600 1.00 2725 155 0.2761 0.3279
REMARK 3 20 3.0600 - 3.0100 1.00 2749 149 0.2942 0.3620
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) : 0.333
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.43
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 : 0.010 8841
REMARK 3 ANGLE : 1.125 12100
REMARK 3 CHIRALITY : 0.060 1305
REMARK 3 PLANARITY : 0.011 1570
REMARK 3 DIHEDRAL : 7.819 1259
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A):-191.7306 -88.3987 9.7217
REMARK 3 T TENSOR
REMARK 3 T11: 0.4561 T22: 0.5373
REMARK 3 T33: 0.4846 T12: -0.0466
REMARK 3 T13: -0.0708 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 2.7421 L22: 1.8137
REMARK 3 L33: 1.2976 L12: -0.8470
REMARK 3 L13: -0.6400 L23: 0.4240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0908 S12: -0.0571 S13: -0.1118
REMARK 3 S21: 0.0561 S22: 0.0144 S23: -0.2766
REMARK 3 S31: -0.0052 S32: -0.0568 S33: 0.0772
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A):-155.6845-122.4805 -23.0072
REMARK 3 T TENSOR
REMARK 3 T11: 0.4052 T22: 0.5764
REMARK 3 T33: 0.5256 T12: -0.0419
REMARK 3 T13: 0.0364 T23: 0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 2.8047 L22: 2.4692
REMARK 3 L33: 2.0725 L12: 0.0852
REMARK 3 L13: -0.6390 L23: 0.0963
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: -0.1340 S13: 0.2094
REMARK 3 S21: -0.0935 S22: 0.0536 S23: -0.4448
REMARK 3 S31: -0.0317 S32: 0.2942 S33: -0.0972
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 8AEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1292124279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980004
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57675
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.010
REMARK 200 RESOLUTION RANGE LOW (A) : 91.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.12
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.60370
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: 6ZWE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LISO4, 100 MM HEPES PH7, 60 MM
REMARK 280 MGSO4, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 38.25333
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 76.50667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.38000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 95.63333
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 19.12667
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLU B 4
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
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 O PRO B 44 NH1 ARG B 274 2.15
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 ALA A 62 43.12 -95.08
REMARK 500 PRO A 106 88.92 -64.33
REMARK 500 SER A 203 -126.98 53.39
REMARK 500 ASP A 306 -94.40 -99.50
REMARK 500 ASP A 333 78.20 -118.46
REMARK 500 TYR A 341 50.26 -92.23
REMARK 500 ALA A 343 131.44 -35.97
REMARK 500 SER A 347 135.65 -176.13
REMARK 500 LYS A 348 -6.38 -58.50
REMARK 500 VAL A 367 78.62 -115.76
REMARK 500 SER A 371 -179.99 -62.23
REMARK 500 HIS A 447 115.82 -39.34
REMARK 500 ASP A 494 143.79 -172.11
REMARK 500 LYS A 496 59.99 39.14
REMARK 500 ASP A 514 -159.44 -163.37
REMARK 500 SER A 541 -74.49 -60.15
REMARK 500 PHE B 47 -4.92 77.91
REMARK 500 ALA B 62 51.50 -98.78
REMARK 500 ASP B 95 86.59 -69.10
REMARK 500 TYR B 105 -73.42 -58.96
REMARK 500 ARG B 165 -14.99 72.53
REMARK 500 ASN B 170 17.99 56.67
REMARK 500 SER B 196 52.98 -144.65
REMARK 500 SER B 203 -125.44 52.00
REMARK 500 SER B 293 -127.30 -126.36
REMARK 500 ASP B 306 -78.97 -99.26
REMARK 500 VAL B 367 76.02 -111.91
REMARK 500 VAL B 407 -63.17 -122.73
REMARK 500 THR B 486 14.58 -146.63
REMARK 500 GLU B 491 108.98 -57.43
REMARK 500 PRO B 495 56.89 -100.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 203 OG
REMARK 620 2 HIS A 447 NE2 111.0
REMARK 620 3 LWL A 601 N09 128.5 113.9
REMARK 620 4 LWL A 601 N16 97.7 123.0 78.0
REMARK 620 5 LWL A 601 O07 87.3 82.1 75.3 149.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 631 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 381 ND1
REMARK 620 2 HIS B 381 NE2 104.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 636 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 426 OH
REMARK 620 2 ASP A 488 OD2 80.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 635 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 747 O
REMARK 620 2 HOH A 761 O 100.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 637 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 764 O
REMARK 620 2 HOH A 770 O 169.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 203 OG
REMARK 620 2 HIS B 447 NE2 112.0
REMARK 620 3 LWL B 601 N09 122.2 116.1
REMARK 620 4 LWL B 601 N16 102.1 116.2 83.9
REMARK 620 5 LWL B 601 O07 96.1 70.5 72.5 155.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 637 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 747 O
REMARK 620 2 HOH B 749 O 107.8
REMARK 620 N 1
DBREF 8AEN A 1 543 UNP P22303 ACES_HUMAN 32 574
DBREF 8AEN B 1 543 UNP P22303 ACES_HUMAN 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG
SEQRES 2 A 543 GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO
SEQRES 5 A 543 LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE
SEQRES 6 A 543 GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG
SEQRES 12 A 543 THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU
SEQRES 37 A 543 GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP
SEQRES 39 A 543 PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG
SEQRES 2 B 543 GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO
SEQRES 5 B 543 LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE
SEQRES 6 B 543 GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG
SEQRES 12 B 543 THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU
SEQRES 37 B 543 GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP
SEQRES 39 B 543 PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 15
HET GAL E 2 11
HET SIA E 3 20
HET NAG F 1 14
HET NAG F 2 14
HET FUC F 3 10
HET LWL A 601 16
HET ZN A 602 1
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 606 5
HET SO4 A 607 5
HET SO4 A 608 5
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 611 5
HET SO4 A 612 5
HET SO4 A 613 5
HET CL A 614 1
HET CL A 615 1
HET CL A 616 1
HET CL A 617 1
HET CL A 618 1
HET CL A 619 1
HET CL A 620 1
HET CL A 621 1
HET CL A 622 1
HET CL A 623 1
HET CL A 624 1
HET CL A 625 1
HET CL A 626 1
HET CL A 627 1
HET CL A 628 1
HET CL A 629 1
HET CL A 630 1
HET ZN A 631 1
HET ZN A 632 1
HET MG A 633 1
HET MG A 634 1
HET MG A 635 1
HET MG A 636 1
HET MG A 637 1
HET LWL B 601 16
HET ZN B 602 1
HET SO4 B 603 5
HET SO4 B 604 5
HET SO4 B 605 5
HET SO4 B 606 5
HET SO4 B 607 5
HET SO4 B 608 5
HET SO4 B 609 5
HET SO4 B 610 5
HET SO4 B 611 5
HET SO4 B 612 5
HET CL B 613 1
HET CL B 614 1
HET CL B 615 1
HET CL B 616 1
HET CL B 617 1
HET CL B 618 1
HET CL B 619 1
HET CL B 620 1
HET CL B 621 1
HET CL B 622 1
HET CL B 623 1
HET CL B 624 1
HET CL B 625 1
HET CL B 626 1
HET CL B 627 1
HET CL B 628 1
HET CL B 629 1
HET CL B 630 1
HET CL B 631 1
HET MG B 632 1
HET MG B 633 1
HET MG B 634 1
HET MG B 635 1
HET MG B 636 1
HET MG B 637 1
HET MG B 638 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
HETNAM LWL N,N,N-TRIMETHYL-2-OXO-2-(2-(PYRIDIN-2-YLMETHYLENE)
HETNAM 2 LWL HYDRAZINEYL)ETHAN-1-AMINIUM
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC
HETSYN 2 SIA ACID; O-SIALIC ACID
HETSYN LWL ~{N}-[(~{E})-PYRIDIN-2-YLMETHYLIDENEAMINO]-2-
HETSYN 2 LWL (TRIMETHYL-$L^{4}-AZANYL)ETHANAMIDE
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 GAL C6 H12 O6
FORMUL 5 SIA C11 H19 N O9
FORMUL 7 LWL 2(C11 H17 N4 O 1+)
FORMUL 8 ZN 4(ZN 2+)
FORMUL 9 SO4 21(O4 S 2-)
FORMUL 20 CL 36(CL 1-)
FORMUL 39 MG 12(MG 2+)
FORMUL 82 HOH *136(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 GLY A 240 VAL A 255 1 16
HELIX 12 AB3 ASP A 266 ARG A 274 1 9
HELIX 13 AB4 PRO A 277 TRP A 286 1 10
HELIX 14 AB5 THR A 311 ASN A 317 1 7
HELIX 15 AB6 GLY A 335 TYR A 341 1 7
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 GLN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASP A 460 5 5
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 ALA A 542 1 9
HELIX 26 AC8 ASP B 5 GLU B 7 5 3
HELIX 27 AC9 MET B 42 ARG B 46 5 5
HELIX 28 AD1 PHE B 80 MET B 85 1 6
HELIX 29 AD2 LEU B 130 ASP B 134 5 5
HELIX 30 AD3 GLY B 135 ARG B 143 1 9
HELIX 31 AD4 VAL B 153 LEU B 159 1 7
HELIX 32 AD5 ASN B 170 VAL B 187 1 18
HELIX 33 AD6 ALA B 188 PHE B 190 5 3
HELIX 34 AD7 SER B 203 LEU B 214 1 12
HELIX 35 AD8 SER B 215 GLY B 220 1 6
HELIX 36 AD9 GLY B 240 VAL B 255 1 16
HELIX 37 AE1 ASN B 265 ARG B 276 1 12
HELIX 38 AE2 PRO B 277 GLU B 285 1 9
HELIX 39 AE3 TRP B 286 VAL B 288 5 3
HELIX 40 AE4 THR B 311 ALA B 318 1 8
HELIX 41 AE5 GLY B 335 TYR B 341 1 7
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 THR B 383 1 13
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 GLN B 421 1 15
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASP B 460 5 5
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 ARG B 534 1 10
HELIX 51 AF6 ARG B 534 THR B 543 1 10
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 LEU A 146 N TRP A 102
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 THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O VAL A 226 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 ALA A 38 GLU A 39 0
SHEET 2 AA3 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SHEET 1 AA4 3 LEU B 9 THR B 11 0
SHEET 2 AA4 3 ARG B 16 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 TRP B 117 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O PHE B 200 N VAL B 116
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 ARG B 424 N VAL B 326
SHEET 10 AA511 GLN B 509 LEU B 513 1 O VAL B 511 N ALA B 427
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.08
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.07
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 265 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG F 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG E 1 C1 GAL E 2 1555 1555 1.46
LINK O3 GAL E 2 C2 SIA E 3 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.48
LINK O6 NAG F 1 C1 FUC F 3 1555 1555 1.48
LINK OG SER A 203 ZN ZN A 602 1555 1555 2.05
LINK NE2 HIS A 287 ZN ZN A 632 1555 1555 2.39
LINK ND1 HIS A 381 ZN ZN A 631 1555 1555 2.26
LINK OH TYR A 426 MG MG B 636 1555 4345 2.80
LINK NE2 HIS A 447 ZN ZN A 602 1555 1555 2.28
LINK OD2 ASP A 488 MG MG B 636 1555 4345 2.51
LINK N09 LWL A 601 ZN ZN A 602 1555 1555 2.21
LINK N16 LWL A 601 ZN ZN A 602 1555 1555 2.24
LINK O07 LWL A 601 ZN ZN A 602 1555 1555 2.18
LINK O4 SO4 A 613 MG MG A 633 1555 1555 2.98
LINK ZN ZN A 631 NE2 HIS B 381 1555 1555 2.31
LINK MG MG A 635 O HOH A 747 1555 1555 2.34
LINK MG MG A 635 O HOH A 761 1555 1555 2.52
LINK MG MG A 637 O HOH A 764 1555 1555 2.56
LINK MG MG A 637 O HOH A 770 1555 1555 2.14
LINK OG SER B 203 ZN ZN B 602 1555 1555 2.21
LINK NE2 HIS B 447 ZN ZN B 602 1555 1555 2.30
LINK N09 LWL B 601 ZN ZN B 602 1555 1555 2.57
LINK N16 LWL B 601 ZN ZN B 602 1555 1555 2.51
LINK O07 LWL B 601 ZN ZN B 602 1555 1555 1.83
LINK MG MG B 637 O HOH B 747 1555 1555 2.52
LINK MG MG B 637 O HOH B 749 1555 1555 2.84
CRYST1 210.850 210.850 114.760 90.00 90.00 120.00 P 61 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 0.004743 0.002738 0.000000 0.00000
SCALE2 0.000000 0.005476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008714 0.00000
TER 4159 THR A 543
TER 8321 THR B 543
MASTER 386 0 86 51 30 0 0 6 8786 2 325 84
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