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HEADER HYDROLASE 15-SEP-20 7K4O
TITLE TANNIN ACYL HYDROLASE FROM ASPERGILLUS NIGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5061
KEYWDS ESTERASE, TANNIN, SERINE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.REN
REVDAT 1 17-MAR-21 7K4O 0
JRNL AUTH L.DONG,W.J.MCKINSTRY,L.PAN,J.NEWMAN,B.REN
JRNL TITL CRYSTAL STRUCTURE OF FUNGAL TANNASE FROM ASPERGILLUS NIGER.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 77 267 2021
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 33559614
JRNL DOI 10.1107/S2059798320016484
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 114035
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.997
REMARK 3 FREE R VALUE TEST SET COUNT : 5698
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7951
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 410
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4280
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 337
REMARK 3 SOLVENT ATOMS : 775
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27200
REMARK 3 B22 (A**2) : -0.27200
REMARK 3 B33 (A**2) : 0.88100
REMARK 3 B12 (A**2) : -0.13600
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4856 ; 0.014 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4103 ; 0.035 ; 0.018
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6706 ; 1.880 ; 1.745
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9653 ; 3.165 ; 1.661
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 594 ; 6.247 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 228 ;33.105 ;24.035
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 676 ;11.745 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.133 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 712 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5368 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 975 ; 0.019 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 927 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 34 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2478 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 570 ; 0.232 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.123 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 2 ; 0.112 ; 0.200
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2257 ; 2.562 ; 2.954
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2256 ; 2.562 ; 2.954
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2830 ; 3.464 ; 4.423
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2831 ; 3.464 ; 4.423
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2597 ; 3.683 ; 3.489
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2598 ; 3.900 ; 3.487
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3855 ; 5.469 ; 5.139
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3856 ; 5.593 ; 5.138
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7K4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-20.
REMARK 100 THE DEPOSITION ID IS D_1000251864.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-19
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114035
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 19.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.39600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
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: 3WMT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ZINC SULFATE, POLYETHYLENE GLYCOL
REMARK 280 MONOMETHYL ETHER 500 AND 0.1 M SODIUM MES AT PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 74.04067
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 37.02033
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 55.53050
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 18.51017
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 92.55083
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.04067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 37.02033
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 18.51017
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 55.53050
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 92.55083
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A 605 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN A 606 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN A 607 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 740 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 842 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 873 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 945 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 971 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1304 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1371 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1389 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1421 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1461 LIES ON A SPECIAL POSITION.
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 O2 MAN C 4 H1 MAN C 5 1.08
REMARK 500 O3 MAN B 4 H1 MAN B 7 1.12
REMARK 500 O4 NAG D 1 H1 NAG D 2 1.19
REMARK 500 O3 BMA C 3 H1 MAN C 4 1.20
REMARK 500 O4 NAG B 1 H1 NAG B 2 1.20
REMARK 500 HH21 ARG A 285 HG SER A 558 1.21
REMARK 500 O4 NAG C 1 H1 NAG C 2 1.24
REMARK 500 O4 NAG B 2 H1 BMA B 3 1.24
REMARK 500 O4 NAG F 1 H1 NAG F 2 1.26
REMARK 500 O2 MAN B 5 H1 MAN B 6 1.27
REMARK 500 HG SER A 54 H ALA A 83 1.28
REMARK 500 O4 NAG G 1 H1 NAG G 2 1.29
REMARK 500 O HOH A 713 O HOH A 1212 1.43
REMARK 500 C4 NAG F 1 H1 NAG F 2 1.48
REMARK 500 C4 NAG D 1 H1 NAG D 2 1.48
REMARK 500 C4 NAG B 1 H1 NAG B 2 1.50
REMARK 500 C4 NAG G 1 H1 NAG G 2 1.52
REMARK 500 C4 NAG C 1 H1 NAG C 2 1.54
REMARK 500 C2 MAN B 5 H1 MAN B 6 1.57
REMARK 500 C3 BMA C 3 H1 MAN C 4 1.58
REMARK 500 C4 NAG B 2 H1 BMA B 3 1.59
REMARK 500 O HOH A 1314 O HOH A 1362 1.72
REMARK 500 O HOH A 1252 O HOH A 1280 1.81
REMARK 500 O HOH A 1407 O HOH A 1434 1.84
REMARK 500 O HOH A 1284 O HOH A 1385 1.85
REMARK 500 O HOH A 1260 O HOH A 1376 1.88
REMARK 500 O HOH A 1285 O HOH A 1306 1.89
REMARK 500 O HOH A 1436 O HOH A 1442 1.92
REMARK 500 O HOH A 1236 O HOH A 1270 1.93
REMARK 500 O HOH A 1235 O HOH A 1362 1.94
REMARK 500 O HOH A 832 O HOH A 935 1.94
REMARK 500 O HOH A 1048 O HOH A 1224 1.98
REMARK 500 O HOH A 1283 O HOH A 1307 1.99
REMARK 500 O HOH A 1283 O HOH A 1357 2.03
REMARK 500 O HOH A 1207 O HOH A 1368 2.05
REMARK 500 O HOH A 705 O HOH A 1090 2.07
REMARK 500 O HOH A 1135 O HOH A 1232 2.15
REMARK 500 O HOH A 1112 O HOH A 1217 2.15
REMARK 500 O HOH A 1217 O HOH A 1318 2.17
REMARK 500 O HOH A 701 O HOH A 1106 2.17
REMARK 500 O HOH A 1018 O HOH A 1410 2.18
REMARK 500 O HOH A 1186 O HOH A 1345 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1075 O HOH A 1075 10555 2.13
REMARK 500 O HOH A 1208 O HOH A 1433 9555 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 172 -18.03 -161.95
REMARK 500 SER A 206 -120.86 69.47
REMARK 500 SER A 206 -121.91 70.88
REMARK 500 ALA A 230 69.16 24.28
REMARK 500 ALA A 232 45.12 -80.54
REMARK 500 ASP A 280 12.03 -148.16
REMARK 500 THR A 348 -14.01 91.35
REMARK 500 VAL A 381 -60.62 -103.27
REMARK 500 ASN A 384 26.56 -149.63
REMARK 500 THR A 413 -77.29 -126.42
REMARK 500 TRP A 474 -15.20 -143.61
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 A1459 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A1461 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A1462 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1465 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1467 DISTANCE = 7.02 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 MAN B 7
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 NA A 611 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 57 O
REMARK 620 2 THR A 57 OG1 70.5
REMARK 620 3 HOH A 823 O 106.4 157.3
REMARK 620 4 HOH A 907 O 75.1 73.2 84.2
REMARK 620 5 HOH A1077 O 71.5 85.8 115.0 144.9
REMARK 620 6 HOH A1145 O 151.1 80.7 101.1 99.4 104.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 607 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 58 OE2
REMARK 620 2 GLU A 58 OE2 0.0
REMARK 620 3 HOH A 948 O 92.2 92.2
REMARK 620 4 HOH A 948 O 171.1 171.1 87.9
REMARK 620 5 HOH A1087 O 85.4 85.4 78.9 103.4
REMARK 620 6 HOH A1087 O 92.4 92.4 103.4 78.8 177.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 606 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 196 OD2
REMARK 620 2 ASP A 196 OD2 0.0
REMARK 620 3 HOH A 925 O 87.2 87.2
REMARK 620 4 HOH A 925 O 168.1 168.1 83.6
REMARK 620 5 HOH A1066 O 86.0 86.0 92.3 86.8
REMARK 620 6 HOH A1066 O 94.7 94.7 86.8 92.3 178.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 273 O
REMARK 620 2 ASP A 273 OD1 72.1
REMARK 620 3 ASP A 276 OD1 75.6 140.4
REMARK 620 4 ASP A 276 OD2 75.2 133.0 55.4
REMARK 620 5 LYS A 278 O 88.3 82.3 74.5 129.6
REMARK 620 6 ASP A 280 OD1 142.7 71.2 133.4 137.6 80.6
REMARK 620 7 VAL A 282 O 97.6 78.7 128.3 73.1 157.2 81.5
REMARK 620 8 HOH A 813 O 145.8 141.5 75.2 73.7 100.6 71.5 86.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 608 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 425 NE2
REMARK 620 2 HOH A 935 O 89.4
REMARK 620 3 HOH A1250 O 104.8 165.5
REMARK 620 4 HOH A1275 O 111.1 88.8 88.7
REMARK 620 5 HOH A1300 O 114.0 94.3 77.5 134.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 605 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 469 OE1
REMARK 620 2 GLU A 469 OE2 55.9
REMARK 620 3 GLU A 469 OE1 0.0 55.9
REMARK 620 4 GLU A 469 OE2 55.9 0.0 55.9
REMARK 620 5 GLU A 473 OE1 99.6 121.7 99.6 121.7
REMARK 620 6 GLU A 473 OE1 99.6 121.7 99.6 121.7 0.0
REMARK 620 N 1 2 3 4 5
DBREF 7K4O A 21 574 UNP A2QIR3 A2QIR3_ASPNC 21 574
SEQRES 1 A 554 ALA THR PRO SER THR LEU ALA GLU LEU CYS THR ASP SER
SEQRES 2 A 554 ILE VAL LYS ALA ALA LEU PRO PRO SER GLU PHE ILE GLN
SEQRES 3 A 554 GLY ILE THR ILE ASP SER ASP SER VAL THR THR GLU VAL
SEQRES 4 A 554 VAL THR ASN SER SER VAL SER SER GLU PHE TYR PRO SER
SEQRES 5 A 554 ALA THR ILE ASN TYR CYS ASN VAL THR PHE ALA TYR SER
SEQRES 6 A 554 HIS ASP GLY ILE ASP GLY ASP GLN VAL LEU LEU GLU ILE
SEQRES 7 A 554 TRP LEU PRO ALA PRO THR ASP PHE GLN ASN ARG TRP LEU
SEQRES 8 A 554 SER THR GLY GLY GLY GLY TYR ALA ILE ASN SER GLY ASP
SEQRES 9 A 554 GLN SER LEU PRO GLY GLY VAL MET TYR GLY ALA ALA SER
SEQRES 10 A 554 GLY MET THR ASP GLY GLY PHE GLY GLY PHE SER ASN ASN
SEQRES 11 A 554 ALA ASP THR ALA MET LEU LEU ALA ASN GLY THR LEU ASP
SEQRES 12 A 554 TYR GLU THR LEU TYR MET PHE ALA TYR LYS ALA HIS ARG
SEQRES 13 A 554 GLU LEU SER LEU ILE GLY LYS ALA LEU THR ARG ASN VAL
SEQRES 14 A 554 TYR GLY MET SER ASP SER ASP LYS LEU TYR ALA TYR TYR
SEQRES 15 A 554 GLN GLY CYS SER GLU GLY GLY ARG GLU GLY TRP SER GLN
SEQRES 16 A 554 VAL GLN ARG PHE GLY ASP GLU TRP ASP GLY ALA ILE ILE
SEQRES 17 A 554 GLY ALA PRO ALA PHE ARG TRP SER PHE GLN GLN THR GLN
SEQRES 18 A 554 HIS LEU TYR SER ASN VAL VAL GLU LYS THR LEU ASP TYR
SEQRES 19 A 554 TYR PRO PRO PRO CYS GLU LEU ASP LYS ILE VAL ASN GLU
SEQRES 20 A 554 THR ILE ALA ALA CYS ASP ALA MET ASP GLY LYS VAL ASP
SEQRES 21 A 554 TRP VAL VAL ALA ARG THR ASP LEU CYS LEU LEU ASP PHE
SEQRES 22 A 554 ASP ILE SER THR ILE GLU GLY LYS PRO TYR SER CYS ALA
SEQRES 23 A 554 ALA SER ARG GLY THR PRO ALA GLN ASN GLY THR VAL SER
SEQRES 24 A 554 ALA LYS GLY ILE GLU VAL ALA LYS THR ILE ILE ASN GLY
SEQRES 25 A 554 LEU HIS ASP SER GLN GLY ARG ARG VAL TYR PHE SER TYR
SEQRES 26 A 554 GLN PRO THR ALA ALA PHE ASP ASP ALA GLU THR GLN TYR
SEQRES 27 A 554 ASN SER THR THR GLY GLN TRP GLY LEU ASP ILE ASP GLN
SEQRES 28 A 554 LEU GLY GLY GLU TYR ILE ALA LEU LEU VAL ASP LYS ASN
SEQRES 29 A 554 GLY THR THR LEU ASP SER LEU ASP GLY VAL THR TYR ASP
SEQRES 30 A 554 THR LEU LYS ASP TRP MET ILE SER GLY LEU GLN GLU TYR
SEQRES 31 A 554 TYR SER THR LEU GLN THR THR TRP PRO ASP LEU THR PRO
SEQRES 32 A 554 PHE HIS GLU ALA GLY GLY LYS VAL ILE HIS PHE HIS GLY
SEQRES 33 A 554 ASP ALA ASP PHE SER ILE PRO THR ALA ALA SER ILE ARG
SEQRES 34 A 554 TYR TRP GLU SER VAL ARG SER ILE MET TYR PRO ASN GLN
SEQRES 35 A 554 ASP TYR ASN SER SER ALA GLU ALA LEU ASN GLU TRP TYR
SEQRES 36 A 554 ARG LEU TYR THR VAL PRO GLY ALA GLY HIS CYS ALA THR
SEQRES 37 A 554 ASN ASP ALA MET PRO ASN GLY PRO PHE PRO GLN THR ASN
SEQRES 38 A 554 MET ALA VAL MET ILE ASP TRP VAL GLU ASN GLY VAL VAL
SEQRES 39 A 554 PRO THR THR LEU ASN ALA THR VAL LEU GLN GLY GLU ASN
SEQRES 40 A 554 GLU GLY GLN ASN GLN GLN LEU CYS ALA TRP PRO LEU ARG
SEQRES 41 A 554 PRO LEU TRP THR ASN ASN GLY THR THR MET GLU CYS VAL
SEQRES 42 A 554 TYR ASN GLN ARG SER ILE ASP SER TRP HIS TYR ASP LEU
SEQRES 43 A 554 ASP ALA VAL PRO MET PRO VAL TYR
HET NAG B 1 27
HET NAG B 2 27
HET BMA B 3 20
HET MAN B 4 20
HET MAN B 5 21
HET MAN B 6 22
HET MAN B 7 20
HET MAN B 8 22
HET NAG C 1 27
HET NAG C 2 27
HET BMA C 3 20
HET MAN C 4 21
HET MAN C 5 22
HET MAN C 6 22
HET NAG D 1 27
HET NAG D 2 28
HET NAG E 1 27
HET NAG E 2 28
HET NAG F 1 27
HET NAG F 2 28
HET NAG G 1 27
HET NAG G 2 28
HET NAG A 601 28
HET NAG A 602 28
HET GDE A 603 17
HET CA A 604 1
HET ZN A 605 1
HET ZN A 606 1
HET ZN A 607 1
HET ZN A 608 1
HET CL A 609 1
HET CL A 610 1
HET NA A 611 1
HET FWN A 612 29
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GDE 3,4,5-TRIHYDROXYBENZOIC ACID
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM FWN 2-[2-(2-ETHOXYETHOXY)ETHOXY]ETHANOL
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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GDE GALLATE
FORMUL 2 NAG 14(C8 H15 N O6)
FORMUL 2 BMA 2(C6 H12 O6)
FORMUL 2 MAN 8(C6 H12 O6)
FORMUL 10 GDE C7 H6 O5
FORMUL 11 CA CA 2+
FORMUL 12 ZN 4(ZN 2+)
FORMUL 16 CL 2(CL 1-)
FORMUL 18 NA NA 1+
FORMUL 19 FWN C8 H18 O4
FORMUL 20 HOH *775(H2 O)
HELIX 1 AA1 THR A 25 CYS A 30 1 6
HELIX 2 AA2 THR A 31 LEU A 39 1 9
HELIX 3 AA3 PRO A 103 PHE A 106 5 4
HELIX 4 AA4 LEU A 127 MET A 132 1 6
HELIX 5 AA5 ALA A 151 ALA A 154 5 4
HELIX 6 AA6 ASP A 163 TYR A 172 1 10
HELIX 7 AA7 TYR A 172 TYR A 190 1 19
HELIX 8 AA8 SER A 206 GLN A 217 1 12
HELIX 9 AA9 ARG A 234 HIS A 242 1 9
HELIX 10 AB1 LEU A 243 ASP A 253 1 11
HELIX 11 AB2 PRO A 257 ASP A 273 1 17
HELIX 12 AB3 ALA A 274 GLY A 277 5 4
HELIX 13 AB4 ARG A 285 PHE A 293 1 9
HELIX 14 AB5 ASP A 294 GLU A 299 5 6
HELIX 15 AB6 SER A 319 ASN A 331 1 13
HELIX 16 AB7 ASP A 370 VAL A 381 1 12
HELIX 17 AB8 THR A 395 TYR A 411 1 17
HELIX 18 AB9 LEU A 421 ALA A 427 1 7
HELIX 19 AC1 THR A 444 TYR A 459 1 16
HELIX 20 AC2 ASP A 463 GLU A 473 1 11
HELIX 21 AC3 THR A 500 GLY A 512 1 13
HELIX 22 AC4 ASN A 555 TRP A 562 1 8
SHEET 1 AA1 9 ILE A 48 SER A 67 0
SHEET 2 AA1 9 TYR A 70 HIS A 86 -1 O ASN A 79 N GLU A 58
SHEET 3 AA1 9 VAL A 94 PRO A 101 -1 O VAL A 94 N TYR A 84
SHEET 4 AA1 9 ALA A 135 THR A 140 -1 O SER A 137 N TRP A 99
SHEET 5 AA1 9 ARG A 109 THR A 113 1 N LEU A 111 O GLY A 138
SHEET 6 AA1 9 TYR A 199 CYS A 205 1 O TYR A 201 N SER A 112
SHEET 7 AA1 9 GLY A 225 GLY A 229 1 O ILE A 227 N TYR A 202
SHEET 8 AA1 9 LYS A 430 GLY A 436 1 O ILE A 432 N ILE A 228
SHEET 9 AA1 9 TYR A 475 VAL A 480 1 O ARG A 476 N HIS A 433
SHEET 1 AA2 2 LEU A 156 ALA A 158 0
SHEET 2 AA2 2 THR A 161 LEU A 162 -1 O THR A 161 N LEU A 157
SHEET 1 AA3 2 PRO A 302 CYS A 305 0
SHEET 2 AA3 2 GLN A 314 THR A 317 -1 O GLN A 314 N CYS A 305
SHEET 1 AA4 2 GLN A 357 ASN A 359 0
SHEET 2 AA4 2 GLN A 364 GLY A 366 -1 O GLY A 366 N GLN A 357
SHEET 1 AA5 2 LEU A 518 THR A 521 0
SHEET 2 AA5 2 ASN A 531 LEU A 534 -1 O LEU A 534 N LEU A 518
SHEET 1 AA6 2 ARG A 540 THR A 544 0
SHEET 2 AA6 2 THR A 549 VAL A 553 -1 O VAL A 553 N ARG A 540
SSBOND 1 CYS A 30 CYS A 78 1555 1555 2.24
SSBOND 2 CYS A 205 CYS A 486 1555 1555 2.07
SSBOND 3 CYS A 259 CYS A 305 1555 1555 2.07
SSBOND 4 CYS A 272 CYS A 289 1555 1555 2.29
SSBOND 5 CYS A 535 CYS A 552 1555 1555 2.16
LINK ND2 ASN A 62 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 79 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN A 159 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 266 C1 NAG G 1 1555 1555 1.48
LINK ND2 ASN A 359 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 384 C1 NAG E 1 1555 1555 1.42
LINK ND2 ASN A 465 C1 NAG D 1 1555 1555 1.42
LINK ND2 ASN A 519 C1 NAG B 1 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.41
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.49
LINK O6 BMA B 3 C1 MAN B 4 1555 1555 1.44
LINK O3 BMA B 3 C1 MAN B 8 1555 1555 1.48
LINK O6 MAN B 4 C1 MAN B 5 1555 1555 1.46
LINK O3 MAN B 4 C1 MAN B 7 1555 1555 1.50
LINK O2 MAN B 5 C1 MAN B 6 1555 1555 1.48
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.46
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.46
LINK O6 BMA C 3 C1 MAN C 6 1555 1555 1.48
LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.48
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.48
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.48
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O THR A 57 NA NA A 611 1555 1555 2.64
LINK OG1 THR A 57 NA NA A 611 1555 1555 2.60
LINK OE2 GLU A 58 ZN ZN A 607 1555 1555 2.07
LINK OE2 GLU A 58 ZN ZN A 607 1555 12544 2.07
LINK OD2 ASP A 196 ZN ZN A 606 1555 1555 2.07
LINK OD2 ASP A 196 ZN ZN A 606 1555 10555 2.07
LINK O ASP A 273 CA CA A 604 1555 1555 2.41
LINK OD1 ASP A 273 CA CA A 604 1555 1555 2.42
LINK OD1 ASP A 276 CA CA A 604 1555 1555 2.32
LINK OD2 ASP A 276 CA CA A 604 1555 1555 2.44
LINK O LYS A 278 CA CA A 604 1555 1555 2.34
LINK OD1 ASP A 280 CA CA A 604 1555 1555 2.50
LINK O VAL A 282 CA CA A 604 1555 1555 2.38
LINK NE2 HIS A 425 ZN ZN A 608 1555 1555 2.08
LINK OE1 GLU A 469 ZN ZN A 605 1555 1555 2.69
LINK OE2 GLU A 469 ZN ZN A 605 1555 1555 1.86
LINK OE1 GLU A 469 ZN ZN A 605 1555 10555 2.69
LINK OE2 GLU A 469 ZN ZN A 605 1555 10555 1.86
LINK OE1 GLU A 473 ZN ZN A 605 1555 1555 2.01
LINK OE1 GLU A 473 ZN ZN A 605 1555 10555 2.01
LINK CA CA A 604 O HOH A 813 1555 1555 2.59
LINK ZN ZN A 606 O HOH A 925 1555 1555 2.21
LINK ZN ZN A 606 O HOH A 925 1555 10555 2.21
LINK ZN ZN A 606 O HOH A1066 1555 1555 2.13
LINK ZN ZN A 606 O HOH A1066 1555 10555 2.13
LINK ZN ZN A 607 O HOH A 948 1555 1555 2.10
LINK ZN ZN A 607 O HOH A 948 1555 12544 2.10
LINK ZN ZN A 607 O HOH A1087 1555 1555 2.17
LINK ZN ZN A 607 O HOH A1087 1555 12544 2.17
LINK ZN ZN A 608 O HOH A 935 1555 1555 2.25
LINK ZN ZN A 608 O HOH A1250 1555 1555 2.34
LINK ZN ZN A 608 O HOH A1275 1555 1555 2.44
LINK ZN ZN A 608 O HOH A1300 1555 1555 2.53
LINK NA NA A 611 O HOH A 823 1555 12544 2.16
LINK NA NA A 611 O HOH A 907 1555 1555 2.70
LINK NA NA A 611 O HOH A1077 1555 1555 2.82
LINK NA NA A 611 O HOH A1145 1555 1555 2.67
CISPEP 1 TRP A 537 PRO A 538 0 2.83
CRYST1 170.920 170.920 111.061 90.00 90.00 120.00 P 65 2 2 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 0.005851 0.003378 0.000000 0.00000
SCALE2 0.000000 0.006756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009004 0.00000
TER 8478 TYR A 574
MASTER 481 0 34 22 19 0 0 6 5392 1 694 43
END |