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HEADER HYDROLASE 13-JUL-22 8AEV
TITLE HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH N,N,N-TRIMETHYL-2-OXO-2-(2-
TITLE 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 14-JUN-23 8AEV 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. 2.89 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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 63106
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3198
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 46.6400 - 8.2100 0.97 2738 155 0.1467 0.1651
REMARK 3 2 8.2000 - 6.5200 0.98 2728 151 0.1523 0.1700
REMARK 3 3 6.5200 - 5.7000 0.98 2683 179 0.1579 0.2146
REMARK 3 4 5.7000 - 5.1800 0.98 2694 150 0.1522 0.1930
REMARK 3 5 5.1800 - 4.8100 0.98 2737 149 0.1354 0.1569
REMARK 3 6 4.8100 - 4.5200 0.99 2699 163 0.1284 0.1525
REMARK 3 7 4.5200 - 4.3000 0.99 2709 163 0.1321 0.1456
REMARK 3 8 4.3000 - 4.1100 0.98 2693 154 0.1364 0.1583
REMARK 3 9 4.1100 - 3.9500 0.99 2708 138 0.1591 0.2019
REMARK 3 10 3.9500 - 3.8100 0.99 2739 129 0.1740 0.1833
REMARK 3 11 3.8100 - 3.7000 0.99 2713 150 0.1803 0.1886
REMARK 3 12 3.7000 - 3.5900 0.98 2693 131 0.1916 0.2361
REMARK 3 13 3.5900 - 3.5000 0.99 2714 146 0.2236 0.2734
REMARK 3 14 3.5000 - 3.4100 0.99 2706 142 0.2370 0.2702
REMARK 3 15 3.4100 - 3.3300 0.99 2752 129 0.2746 0.2791
REMARK 3 16 3.3300 - 3.2600 0.98 2707 120 0.2889 0.3487
REMARK 3 17 3.2600 - 3.2000 0.98 2712 121 0.2986 0.3320
REMARK 3 18 3.2000 - 3.1400 0.96 2677 104 0.3085 0.3763
REMARK 3 19 3.1400 - 3.0800 0.93 2544 135 0.3303 0.3524
REMARK 3 20 3.0800 - 3.0300 0.91 2510 130 0.3431 0.3334
REMARK 3 21 3.0300 - 2.9800 0.90 2436 141 0.3550 0.3782
REMARK 3 22 2.9800 - 2.9300 0.73 2002 121 0.3709 0.4076
REMARK 3 23 2.9300 - 2.8900 0.60 1614 97 0.3828 0.4063
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) : 0.442
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.611
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.45
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 8821
REMARK 3 ANGLE : 1.169 12076
REMARK 3 CHIRALITY : 0.063 1301
REMARK 3 PLANARITY : 0.011 1570
REMARK 3 DIHEDRAL : 9.605 1256
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): 192.5314 88.9527 7.9246
REMARK 3 T TENSOR
REMARK 3 T11: 0.4617 T22: 0.5511
REMARK 3 T33: 0.4046 T12: -0.0692
REMARK 3 T13: 0.1233 T23: -0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 3.1648 L22: 2.9076
REMARK 3 L33: 1.5611 L12: -0.9604
REMARK 3 L13: 0.8281 L23: -0.8812
REMARK 3 S TENSOR
REMARK 3 S11: -0.0520 S12: -0.0917 S13: -0.1166
REMARK 3 S21: 0.1878 S22: 0.0551 S23: 0.3836
REMARK 3 S31: -0.0446 S32: 0.1013 S33: -0.0118
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 156.5312 123.1120 -25.5268
REMARK 3 T TENSOR
REMARK 3 T11: 0.4320 T22: 0.5642
REMARK 3 T33: 0.7319 T12: -0.0471
REMARK 3 T13: -0.0211 T23: -0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 3.1247 L22: 2.9337
REMARK 3 L33: 2.7663 L12: -0.1966
REMARK 3 L13: 1.1327 L23: -0.3427
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: -0.2285 S13: -0.3381
REMARK 3 S21: -0.1303 S22: 0.1401 S23: 0.8752
REMARK 3 S31: -0.1147 S32: -0.4158 S33: -0.1071
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 8AEV 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_1292124302.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-17
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873127
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64879
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 46.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.18120
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.580
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 (%): 80.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LISO4, 100 MM HEPES PH7, 60 MM
REMARK 280 MGSO4, 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 38.87800
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 77.75600
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 58.31700
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 97.19500
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 19.43900
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 NH1 ARG A 224 O ALA A 484 2.12
REMARK 500 O ARG B 46 NH1 ARG B 274 2.15
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 CYS A 272 CA - CB - SG ANGL. DEV. = 6.7 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 ALA A 62 34.08 -93.27
REMARK 500 GLN A 66 -168.97 -76.12
REMARK 500 TIS A 203 -123.80 51.25
REMARK 500 ARG A 219 34.98 -79.12
REMARK 500 PHE A 295 50.25 -151.41
REMARK 500 ASP A 306 -77.40 -67.26
REMARK 500 ASN A 350 -161.59 -119.10
REMARK 500 GLN A 369 64.66 60.29
REMARK 500 PRO A 458 -19.53 -44.92
REMARK 500 ASN A 464 57.31 -97.64
REMARK 500 ARG A 493 57.95 -108.86
REMARK 500 ASP A 494 74.19 -164.99
REMARK 500 LEU A 518 131.98 -36.47
REMARK 500 GLU B 7 4.88 -69.30
REMARK 500 PHE B 47 -6.74 77.81
REMARK 500 ALA B 62 39.07 -93.66
REMARK 500 CYS B 96 13.34 -150.67
REMARK 500 ALA B 127 138.08 -173.32
REMARK 500 ASP B 134 109.97 -54.51
REMARK 500 ARG B 143 58.42 31.18
REMARK 500 ARG B 165 -6.11 69.57
REMARK 500 SER B 196 48.22 -151.83
REMARK 500 TIS B 203 -128.32 45.98
REMARK 500 ASN B 265 45.08 -69.13
REMARK 500 ASP B 266 -38.11 -150.06
REMARK 500 ASP B 306 -76.62 -89.79
REMARK 500 VAL B 367 70.97 -107.41
REMARK 500 TRP B 385 1.02 -60.59
REMARK 500 ARG B 395 -72.09 -56.09
REMARK 500 GLU B 491 107.38 -55.22
REMARK 500 ARG B 493 79.44 56.86
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 625 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 381 ND1
REMARK 620 2 HIS A 381 ND1 41.4
REMARK 620 3 HIS A 381 NE2 32.4 54.8
REMARK 620 4 HIS B 381 NE2 87.8 103.0 56.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 625 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 381 NE2
REMARK 620 2 HIS B 381 ND1 79.2
REMARK 620 3 HIS B 381 NE2 56.8 35.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 632 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 452 OE2
REMARK 620 2 HOH A 754 O 125.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 634 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 488 OD2
REMARK 620 2 HOH B 728 O 73.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 629 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SO4 B 603 O3
REMARK 620 2 SO4 B 603 O4 48.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 632 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 452 OE2
REMARK 620 2 HOH B 740 O 135.1
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8AEN RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND
DBREF 8AEV A 1 543 UNP P22303 ACES_HUMAN 32 574
DBREF 8AEV 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 TIS 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 TIS 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
MODRES 8AEV TIS A 203 SER MODIFIED RESIDUE
MODRES 8AEV TIS B 203 SER MODIFIED RESIDUE
HET TIS A 203 10
HET TIS B 203 10
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 GAL E 1 12
HET SIA E 2 20
HET NAG F 1 14
HET NAG F 2 14
HET FUC F 3 10
HET LWU A 601 27
HET SO4 A 602 5
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 CL A 611 1
HET CL A 612 1
HET CL A 613 1
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 ZN A 625 1
HET ZN A 626 1
HET MG A 627 1
HET MG A 628 1
HET MG A 629 1
HET MG A 630 1
HET MG A 631 1
HET MG A 632 1
HET MG A 633 1
HET MG A 634 1
HET SO4 B 601 5
HET SO4 B 602 5
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 CL B 608 1
HET CL B 609 1
HET CL B 610 1
HET CL B 611 1
HET CL B 612 1
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 ZN B 625 1
HET ZN B 626 1
HET ZN B 627 1
HET MG B 628 1
HET MG B 629 1
HET MG B 630 1
HET MG B 631 1
HET MG B 632 1
HET MG B 633 1
HETNAM TIS O-(1,1-DIHYDROXYETHYL)-L-SERINE
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 LWU 1-(2-(2-((6-(DIHYDROXYMETHYL)-2-PHENYLPYRIMIDIN-4-YL)
HETNAM 2 LWU METHYLENE)HYDRAZINEYL)-2-OXOETHYL)PYRIDIN-1-IUM
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM ZN ZINC 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 LWU ~{N}'-[[6-[BIS(OXIDANYL)METHYL]-2-PHENYL-PYRIMIDIN-4-
HETSYN 2 LWU YL]METHYL]-2-PYRIDIN-1-YL-ETHANEHYDRAZIDE
FORMUL 1 TIS 2(C5 H11 N O5)
FORMUL 3 NAG 6(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 LWU C19 H20 N5 O3 1+
FORMUL 8 SO4 16(O4 S 2-)
FORMUL 17 CL 31(CL 1-)
FORMUL 31 ZN 5(ZN 2+)
FORMUL 33 MG 14(MG 2+)
FORMUL 74 HOH *183(H2 O)
HELIX 1 AA1 MET A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 ARG A 143 1 9
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 VAL A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 TIS A 203 LEU A 214 1 12
HELIX 9 AA9 GLY A 240 GLY A 256 1 17
HELIX 10 AB1 ASP A 266 THR A 275 1 10
HELIX 11 AB2 PRO A 277 ASN A 283 1 7
HELIX 12 AB3 HIS A 284 LEU A 289 5 6
HELIX 13 AB4 THR A 311 GLY A 319 1 9
HELIX 14 AB5 GLY A 335 VAL A 340 1 6
HELIX 15 AB6 SER A 355 VAL A 367 1 13
HELIX 16 AB7 SER A 371 THR A 383 1 13
HELIX 17 AB8 ASP A 390 VAL A 407 1 18
HELIX 18 AB9 VAL A 407 GLN A 421 1 15
HELIX 19 AC1 PRO A 440 GLY A 444 5 5
HELIX 20 AC2 GLU A 450 PHE A 455 1 6
HELIX 21 AC3 GLY A 456 ASP A 460 5 5
HELIX 22 AC4 THR A 466 GLY A 487 1 22
HELIX 23 AC5 ARG A 525 ARG A 534 1 10
HELIX 24 AC6 ARG A 534 ALA A 542 1 9
HELIX 25 AC7 ASP B 5 GLU B 7 5 3
HELIX 26 AC8 MET B 42 ARG B 46 5 5
HELIX 27 AC9 PHE B 80 MET B 85 1 6
HELIX 28 AD1 LEU B 130 ASP B 134 5 5
HELIX 29 AD2 GLY B 135 ARG B 143 1 9
HELIX 30 AD3 GLY B 154 LEU B 159 1 6
HELIX 31 AD4 ASN B 170 VAL B 187 1 18
HELIX 32 AD5 ALA B 188 PHE B 190 5 3
HELIX 33 AD6 TIS B 203 LEU B 214 1 12
HELIX 34 AD7 SER B 215 GLY B 220 1 6
HELIX 35 AD8 MET B 241 VAL B 255 1 15
HELIX 36 AD9 ASP B 266 ARG B 274 1 9
HELIX 37 AE1 PRO B 277 HIS B 284 1 8
HELIX 38 AE2 THR B 311 ALA B 318 1 8
HELIX 39 AE3 GLY B 335 VAL B 340 1 6
HELIX 40 AE4 SER B 355 VAL B 367 1 13
HELIX 41 AE5 SER B 371 THR B 383 1 13
HELIX 42 AE6 ASP B 390 VAL B 407 1 18
HELIX 43 AE7 VAL B 407 GLN B 421 1 15
HELIX 44 AE8 PRO B 440 GLY B 444 5 5
HELIX 45 AE9 GLU B 450 PHE B 455 1 6
HELIX 46 AF1 GLY B 456 ASP B 460 5 5
HELIX 47 AF2 THR B 466 GLY B 487 1 22
HELIX 48 AF3 ARG B 525 ARG B 534 1 10
HELIX 49 AF4 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 SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O SER A 196 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N ALA A 225
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 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 2 VAL A 68 CYS A 69 0
SHEET 2 AA4 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
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 THR B 198 N VAL B 114
SHEET 7 AA611 ARG B 224 GLN B 228 1 O VAL B 226 N LEU B 199
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 TYR B 426 N VAL B 328
SHEET 10 AA611 GLN B 509 LEU B 513 1 O VAL B 511 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
SHEET 1 AA8 2 VAL B 239 GLY B 240 0
SHEET 2 AA8 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 2.08
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.08
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.08
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.07
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK C GLU A 202 N TIS A 203 1555 1555 1.33
LINK C TIS A 203 N ALA A 204 1555 1555 1.34
LINK ND2 ASN A 265 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.45
LINK C GLU B 202 N TIS B 203 1555 1555 1.33
LINK C TIS B 203 N ALA B 204 1555 1555 1.33
LINK ND2 ASN B 350 C1 NAG F 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O3 GAL E 1 C2 SIA E 2 1555 1555 1.47
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.49
LINK O6 NAG F 1 C1 FUC F 3 1555 1555 1.46
LINK NE2 HIS A 284 ZN ZN A 626 1555 1555 2.33
LINK ND1AHIS A 381 ZN ZN A 625 1555 1555 2.31
LINK ND1BHIS A 381 ZN ZN A 625 1555 1555 2.34
LINK NE2BHIS A 381 ZN ZN A 625 1555 1555 2.31
LINK NE2BHIS A 381 ZN ZN B 625 1555 1555 2.29
LINK OE2 GLU A 452 MG MG A 632 1555 1555 2.99
LINK OD2 ASP A 488 MG MG A 634 1555 1555 2.37
LINK O4 SO4 A 602 MG MG A 630 1555 1555 3.00
LINK ZN ZN A 625 NE2AHIS B 381 1555 1555 2.32
LINK MG MG A 629 O3 SO4 B 603 1555 1555 2.92
LINK MG MG A 629 O4 SO4 B 603 1555 1555 2.86
LINK MG MG A 631 O HOH A 782 1555 1555 2.76
LINK MG MG A 632 O HOH A 754 1555 1555 2.66
LINK MG MG A 634 O HOH B 728 1555 4765 2.59
LINK NE2 HIS B 322 ZN ZN B 626 1555 1555 2.32
LINK ND1BHIS B 381 ZN ZN B 625 1555 1555 2.33
LINK NE2AHIS B 381 ZN ZN B 625 1555 1555 2.31
LINK OE2 GLU B 452 MG MG B 632 1555 1555 2.59
LINK MG MG B 632 O HOH B 740 1555 1555 2.65
CRYST1 211.833 211.833 116.634 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 0.004721 0.002725 0.000000 0.00000
SCALE2 0.000000 0.005451 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008574 0.00000
TER 4162 THR A 543
TER 8335 THR B 543
MASTER 403 0 79 49 36 0 0 6 8795 2 305 84
END |