| content |
HEADER HYDROLASE 22-MAR-18 6G21
TITLE CRYSTAL STRUCTURE OF AN ESTERASE FROM ASPERGILLUS ORYZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE FERULOYL ESTERASE B-2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FERULIC ACID ESTERASE B-2,FAEB-2;
COMPND 5 EC: 3.1.1.73;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE (STRAIN ATCC 42149 / RIB
SOURCE 3 40);
SOURCE 4 ORGANISM_COMMON: YELLOW KOJI MOLD;
SOURCE 5 ORGANISM_TAXID: 510516;
SOURCE 6 STRAIN: ATCC 42149 / RIB 40;
SOURCE 7 GENE: FAEB-2, AO090001000582;
SOURCE 8 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.V.MOROZ,E.BLAGOVA,G.J.DAVIES,K.S.WILSON
REVDAT 1 23-MAY-18 6G21 0
SPRSDE 23-MAY-18 6G21 D_1200009248
JRNL AUTH O.V.MOROZ,E.BLAGOVA,G.J.DAVIES,K.S.WILSON
JRNL TITL CRYSTAL STRUCTURE OF AN ESTERASE FROM ASPERGILLUS ORYZAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0218
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 64050
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3246
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4681
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7777
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 213
REMARK 3 SOLVENT ATOMS : 436
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : -0.84000
REMARK 3 B12 (A**2) : 0.13000
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): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.811
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8235 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7071 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11238 ; 1.743 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16473 ; 0.916 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1010 ; 6.695 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 377 ;33.368 ;24.483
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1203 ;14.281 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;23.671 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1206 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9349 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1724 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): 4040 ; 2.329 ; 2.944
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4039 ; 2.329 ; 2.944
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5050 ; 3.083 ; 4.399
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5051 ; 3.083 ; 4.400
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4195 ; 3.014 ; 3.264
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4184 ; 2.982 ; 3.258
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6171 ; 4.323 ; 4.799
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9406 ; 5.287 ;35.426
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9349 ; 5.263 ;35.363
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 507 B 4 507 16667 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6G21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-12; 21-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : DIAMOND; DIAMOND
REMARK 200 BEAMLINE : I04-1; I04
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920; 1.072
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL; PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F; DECTRIS
REMARK 200 PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67326
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 37.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 18.50
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.20
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: CRANK
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, TRIS BUFFER, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K. LITHIUM
REMARK 280 SULPHATE, TRIS BUFFER,CRYSTALS SOAKED IN 5MM KPTCL4, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
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 71.42500
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 71.42500
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 71.42500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 SER A 1
REMARK 465 GLN A 2
REMARK 465 ASP A 3
REMARK 465 SER B 1
REMARK 465 GLN B 2
REMARK 465 ASP B 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 15 CD CE NZ
REMARK 470 ARG A 22 CZ NH1 NH2
REMARK 470 THR A 46 OG1 CG2
REMARK 470 GLU A 157 CG CD OE1 OE2
REMARK 470 LYS A 231 CD CE NZ
REMARK 470 LYS A 339 CE NZ
REMARK 470 ARG A 343 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 350 CE NZ
REMARK 470 GLU A 462 CG CD OE1 OE2
REMARK 470 SER B 93 CB OG
REMARK 470 GLU B 157 CG CD OE1 OE2
REMARK 470 LYS B 493 CE NZ
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 LEU A 258 CA - CB - CG ANGL. DEV. = -14.4 DEGREES
REMARK 500 ARG B 139 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 139 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP B 238 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 395 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 481 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 488 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ASN A 20 19.71 58.83
REMARK 500 SER A 116 -8.18 83.22
REMARK 500 HIS A 138 -30.66 -150.12
REMARK 500 SER A 169 -122.88 73.57
REMARK 500 ALA A 193 61.00 34.29
REMARK 500 ALA A 195 31.98 -80.77
REMARK 500 THR A 269 -18.21 -49.71
REMARK 500 ASN A 292 -1.04 71.57
REMARK 500 VAL A 328 -51.87 -120.75
REMARK 500 ASN A 352 63.86 32.64
REMARK 500 ALA A 420 -150.67 -83.26
REMARK 500 CYS A 422 -34.83 67.51
REMARK 500 ASP A 440 163.32 71.22
REMARK 500 ASN A 471 56.82 -153.97
REMARK 500 SER B 116 -10.05 83.43
REMARK 500 HIS B 138 -28.40 -151.34
REMARK 500 SER B 169 -121.47 70.86
REMARK 500 ALA B 193 64.74 29.14
REMARK 500 ALA B 195 32.64 -83.20
REMARK 500 ASN B 268 106.71 -53.88
REMARK 500 ILE B 311 -78.08 -120.34
REMARK 500 ASN B 352 63.51 33.81
REMARK 500 ALA B 420 -153.09 -85.32
REMARK 500 CYS B 422 -29.39 68.51
REMARK 500 ASN B 439 -75.22 -99.02
REMARK 500 ASN B 471 56.17 -152.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 93 GLY A 94 146.88
REMARK 500 SER B 93 GLY B 94 146.08
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 CA A 611 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 238 O
REMARK 620 2 ASP A 238 OD1 69.6
REMARK 620 3 ASP A 241 OD1 79.5 139.3
REMARK 620 4 ASP A 241 OD2 76.4 135.7 54.5
REMARK 620 5 ALA A 243 O 79.6 74.5 74.5 126.4
REMARK 620 6 ASP A 245 OD1 139.9 72.1 126.0 142.6 79.3
REMARK 620 7 ILE A 247 O 97.4 77.1 134.1 80.1 150.6 85.1
REMARK 620 8 HOH A 746 O 150.3 138.9 77.9 74.9 112.1 69.7 85.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 608 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 238 O
REMARK 620 2 ASP B 238 OD1 71.1
REMARK 620 3 ASP B 241 OD1 77.3 140.5
REMARK 620 4 ASP B 241 OD2 75.1 135.4 52.0
REMARK 620 5 ALA B 243 O 80.5 75.8 76.2 126.1
REMARK 620 6 ASP B 245 OD1 142.3 73.3 127.2 141.7 79.3
REMARK 620 7 ILE B 247 O 100.0 79.4 130.0 78.7 153.6 85.0
REMARK 620 8 HOH B 810 O 145.6 141.0 76.7 71.2 114.1 72.0 80.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FER A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FER B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 34
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 603 through NAG A 604 bound to ASN A 119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800 to ASN A 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound
REMARK 800 to ASN A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 607 bound
REMARK 800 to ASN A 497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 34
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound
REMARK 800 to ASN B 292
DBREF 6G21 A 1 507 UNP Q2UMX6 FAEB2_ASPOR 20 526
DBREF 6G21 B 1 507 UNP Q2UMX6 FAEB2_ASPOR 20 526
SEQRES 1 A 507 SER GLN ASP THR PHE GLN GLY LYS CYS THR GLY PHE ALA
SEQRES 2 A 507 ASP LYS ILE ASN LEU PRO ASN VAL ARG VAL ASN PHE VAL
SEQRES 3 A 507 ASN TYR VAL PRO GLY GLY THR ASN LEU SER LEU PRO ASP
SEQRES 4 A 507 ASN PRO THR SER CYS GLY THR THR SER GLN VAL VAL SER
SEQRES 5 A 507 GLU ASP VAL CYS ARG ILE ALA MET ALA VAL ALA THR SER
SEQRES 6 A 507 ASN SER SER GLU ILE THR LEU GLU ALA TRP LEU PRO GLN
SEQRES 7 A 507 ASN TYR THR GLY ARG PHE LEU SER THR GLY ASN GLY GLY
SEQRES 8 A 507 LEU SER GLY CYS ILE GLN TYR TYR ASP LEU ALA TYR THR
SEQRES 9 A 507 SER GLY LEU GLY PHE ALA THR VAL GLY ALA ASN SER GLY
SEQRES 10 A 507 HIS ASN GLY THR SER GLY GLU PRO PHE TYR HIS HIS PRO
SEQRES 11 A 507 GLU VAL LEU GLU ASP PHE VAL HIS ARG SER VAL HIS THR
SEQRES 12 A 507 GLY VAL VAL VAL GLY LYS GLN LEU THR LYS LEU PHE TYR
SEQRES 13 A 507 GLU GLU GLY PHE LYS LYS SER TYR TYR LEU GLY CYS SER
SEQRES 14 A 507 THR GLY GLY ARG GLN GLY PHE LYS SER VAL GLN LYS TYR
SEQRES 15 A 507 PRO ASN ASP PHE ASP GLY VAL VAL ALA GLY ALA PRO ALA
SEQRES 16 A 507 PHE ASN MET ILE ASN LEU MET SER TRP SER ALA HIS PHE
SEQRES 17 A 507 TYR SER ILE THR GLY PRO VAL GLY SER ASP THR TYR LEU
SEQRES 18 A 507 SER PRO ASP LEU TRP ASN ILE THR HIS LYS GLU ILE LEU
SEQRES 19 A 507 ARG GLN CYS ASP GLY ILE ASP GLY ALA GLU ASP GLY ILE
SEQRES 20 A 507 ILE GLU ASP PRO SER LEU CYS SER PRO VAL LEU GLU ALA
SEQRES 21 A 507 ILE ILE CYS LYS PRO GLY GLN ASN THR THR GLU CYS LEU
SEQRES 22 A 507 THR GLY LYS GLN ALA HIS THR VAL ARG GLU ILE PHE SER
SEQRES 23 A 507 PRO LEU TYR GLY VAL ASN GLY THR LEU LEU TYR PRO ARG
SEQRES 24 A 507 MET GLN PRO GLY SER GLU VAL MET ALA SER SER ILE MET
SEQRES 25 A 507 TYR ASN GLY GLN PRO PHE GLN TYR SER ALA ASP TRP TYR
SEQRES 26 A 507 ARG TYR VAL VAL TYR GLU ASN PRO ASN TRP ASP ALA THR
SEQRES 27 A 507 LYS PHE SER VAL ARG ASP ALA ALA VAL ALA LEU LYS GLN
SEQRES 28 A 507 ASN PRO PHE ASN LEU GLN THR TRP ASP ALA ASP ILE SER
SEQRES 29 A 507 SER PHE ARG LYS ALA GLY GLY LYS VAL LEU THR TYR HIS
SEQRES 30 A 507 GLY LEU MET ASP GLN LEU ILE SER SER GLU ASN SER LYS
SEQRES 31 A 507 LEU TYR TYR ALA ARG VAL ALA GLU THR MET ASN VAL PRO
SEQRES 32 A 507 PRO GLU GLU LEU ASP GLU PHE TYR ARG PHE PHE GLN ILE
SEQRES 33 A 507 SER GLY MET ALA HIS CYS SER GLY GLY ASP GLY ALA TYR
SEQRES 34 A 507 GLY ILE GLY ASN GLN LEU VAL THR TYR ASN ASP ALA ASN
SEQRES 35 A 507 PRO GLU ASN ASN VAL LEU MET ALA MET VAL GLN TRP VAL
SEQRES 36 A 507 GLU LYS GLY ILE ALA PRO GLU THR ILE ARG GLY ALA LYS
SEQRES 37 A 507 PHE THR ASN GLY THR GLY SER ALA VAL GLU TYR THR ARG
SEQRES 38 A 507 LYS HIS CYS ARG TYR PRO ARG ARG ASN VAL TYR LYS GLY
SEQRES 39 A 507 PRO GLY ASN TYR THR ASP GLU ASN ALA TRP GLN CYS VAL
SEQRES 1 B 507 SER GLN ASP THR PHE GLN GLY LYS CYS THR GLY PHE ALA
SEQRES 2 B 507 ASP LYS ILE ASN LEU PRO ASN VAL ARG VAL ASN PHE VAL
SEQRES 3 B 507 ASN TYR VAL PRO GLY GLY THR ASN LEU SER LEU PRO ASP
SEQRES 4 B 507 ASN PRO THR SER CYS GLY THR THR SER GLN VAL VAL SER
SEQRES 5 B 507 GLU ASP VAL CYS ARG ILE ALA MET ALA VAL ALA THR SER
SEQRES 6 B 507 ASN SER SER GLU ILE THR LEU GLU ALA TRP LEU PRO GLN
SEQRES 7 B 507 ASN TYR THR GLY ARG PHE LEU SER THR GLY ASN GLY GLY
SEQRES 8 B 507 LEU SER GLY CYS ILE GLN TYR TYR ASP LEU ALA TYR THR
SEQRES 9 B 507 SER GLY LEU GLY PHE ALA THR VAL GLY ALA ASN SER GLY
SEQRES 10 B 507 HIS ASN GLY THR SER GLY GLU PRO PHE TYR HIS HIS PRO
SEQRES 11 B 507 GLU VAL LEU GLU ASP PHE VAL HIS ARG SER VAL HIS THR
SEQRES 12 B 507 GLY VAL VAL VAL GLY LYS GLN LEU THR LYS LEU PHE TYR
SEQRES 13 B 507 GLU GLU GLY PHE LYS LYS SER TYR TYR LEU GLY CYS SER
SEQRES 14 B 507 THR GLY GLY ARG GLN GLY PHE LYS SER VAL GLN LYS TYR
SEQRES 15 B 507 PRO ASN ASP PHE ASP GLY VAL VAL ALA GLY ALA PRO ALA
SEQRES 16 B 507 PHE ASN MET ILE ASN LEU MET SER TRP SER ALA HIS PHE
SEQRES 17 B 507 TYR SER ILE THR GLY PRO VAL GLY SER ASP THR TYR LEU
SEQRES 18 B 507 SER PRO ASP LEU TRP ASN ILE THR HIS LYS GLU ILE LEU
SEQRES 19 B 507 ARG GLN CYS ASP GLY ILE ASP GLY ALA GLU ASP GLY ILE
SEQRES 20 B 507 ILE GLU ASP PRO SER LEU CYS SER PRO VAL LEU GLU ALA
SEQRES 21 B 507 ILE ILE CYS LYS PRO GLY GLN ASN THR THR GLU CYS LEU
SEQRES 22 B 507 THR GLY LYS GLN ALA HIS THR VAL ARG GLU ILE PHE SER
SEQRES 23 B 507 PRO LEU TYR GLY VAL ASN GLY THR LEU LEU TYR PRO ARG
SEQRES 24 B 507 MET GLN PRO GLY SER GLU VAL MET ALA SER SER ILE MET
SEQRES 25 B 507 TYR ASN GLY GLN PRO PHE GLN TYR SER ALA ASP TRP TYR
SEQRES 26 B 507 ARG TYR VAL VAL TYR GLU ASN PRO ASN TRP ASP ALA THR
SEQRES 27 B 507 LYS PHE SER VAL ARG ASP ALA ALA VAL ALA LEU LYS GLN
SEQRES 28 B 507 ASN PRO PHE ASN LEU GLN THR TRP ASP ALA ASP ILE SER
SEQRES 29 B 507 SER PHE ARG LYS ALA GLY GLY LYS VAL LEU THR TYR HIS
SEQRES 30 B 507 GLY LEU MET ASP GLN LEU ILE SER SER GLU ASN SER LYS
SEQRES 31 B 507 LEU TYR TYR ALA ARG VAL ALA GLU THR MET ASN VAL PRO
SEQRES 32 B 507 PRO GLU GLU LEU ASP GLU PHE TYR ARG PHE PHE GLN ILE
SEQRES 33 B 507 SER GLY MET ALA HIS CYS SER GLY GLY ASP GLY ALA TYR
SEQRES 34 B 507 GLY ILE GLY ASN GLN LEU VAL THR TYR ASN ASP ALA ASN
SEQRES 35 B 507 PRO GLU ASN ASN VAL LEU MET ALA MET VAL GLN TRP VAL
SEQRES 36 B 507 GLU LYS GLY ILE ALA PRO GLU THR ILE ARG GLY ALA LYS
SEQRES 37 B 507 PHE THR ASN GLY THR GLY SER ALA VAL GLU TYR THR ARG
SEQRES 38 B 507 LYS HIS CYS ARG TYR PRO ARG ARG ASN VAL TYR LYS GLY
SEQRES 39 B 507 PRO GLY ASN TYR THR ASP GLU ASN ALA TRP GLN CYS VAL
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET FER A 608 14
HET SO4 A 609 5
HET SO4 A 610 5
HET CA A 611 1
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET FER B 606 14
HET SO4 B 607 5
HET CA B 608 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
HETSYN FER FERULIC ACID
FORMUL 3 NAG 12(C8 H15 N O6)
FORMUL 9 FER 2(C10 H10 O4)
FORMUL 10 SO4 3(O4 S 2-)
FORMUL 12 CA 2(CA 2+)
FORMUL 21 HOH *436(H2 O)
HELIX 1 AA1 THR A 4 GLY A 11 1 8
HELIX 2 AA2 PHE A 12 ILE A 16 5 5
HELIX 3 AA3 PRO A 41 GLY A 45 5 5
HELIX 4 AA4 GLN A 97 LEU A 107 1 11
HELIX 5 AA5 GLY A 123 TYR A 127 5 5
HELIX 6 AA6 HIS A 129 HIS A 138 1 10
HELIX 7 AA7 HIS A 138 TYR A 156 1 19
HELIX 8 AA8 SER A 169 TYR A 182 1 14
HELIX 9 AA9 ASN A 197 GLY A 213 1 17
HELIX 10 AB1 SER A 222 ASP A 238 1 17
HELIX 11 AB2 GLY A 239 GLY A 242 5 4
HELIX 12 AB3 ASP A 250 CYS A 254 5 5
HELIX 13 AB4 VAL A 257 ILE A 262 5 6
HELIX 14 AB5 ASN A 268 CYS A 272 5 5
HELIX 15 AB6 THR A 274 PHE A 285 1 12
HELIX 16 AB7 VAL A 291 GLY A 293 5 3
HELIX 17 AB8 SER A 304 MET A 312 1 9
HELIX 18 AB9 PHE A 318 VAL A 328 1 11
HELIX 19 AC1 ASP A 336 PHE A 340 5 5
HELIX 20 AC2 SER A 341 ASN A 352 1 12
HELIX 21 AC3 PRO A 353 LEU A 356 5 4
HELIX 22 AC4 ILE A 363 GLY A 370 1 8
HELIX 23 AC5 SER A 385 ASN A 401 1 17
HELIX 24 AC6 PRO A 403 ASP A 408 1 6
HELIX 25 AC7 GLN A 434 TYR A 438 5 5
HELIX 26 AC8 ASN A 446 GLY A 458 1 13
HELIX 27 AC9 ASP A 500 ASN A 502 5 3
HELIX 28 AD1 PHE B 5 ALA B 13 1 9
HELIX 29 AD2 ASP B 14 ILE B 16 5 3
HELIX 30 AD3 PRO B 41 GLY B 45 5 5
HELIX 31 AD4 GLN B 97 LEU B 107 1 11
HELIX 32 AD5 GLY B 123 TYR B 127 5 5
HELIX 33 AD6 HIS B 129 HIS B 138 1 10
HELIX 34 AD7 HIS B 138 TYR B 156 1 19
HELIX 35 AD8 SER B 169 TYR B 182 1 14
HELIX 36 AD9 ASN B 197 GLY B 213 1 17
HELIX 37 AE1 SER B 222 ASP B 238 1 17
HELIX 38 AE2 GLY B 239 GLY B 242 5 4
HELIX 39 AE3 ASP B 250 CYS B 254 5 5
HELIX 40 AE4 VAL B 257 ILE B 262 5 6
HELIX 41 AE5 ASN B 268 CYS B 272 5 5
HELIX 42 AE6 THR B 274 PHE B 285 1 12
HELIX 43 AE7 SER B 304 ILE B 311 1 8
HELIX 44 AE8 PHE B 318 VAL B 328 1 11
HELIX 45 AE9 ASP B 336 PHE B 340 5 5
HELIX 46 AF1 SER B 341 ASN B 352 1 12
HELIX 47 AF2 PRO B 353 LEU B 356 5 4
HELIX 48 AF3 ILE B 363 ALA B 369 1 7
HELIX 49 AF4 SER B 385 ASN B 401 1 17
HELIX 50 AF5 PRO B 403 ASP B 408 1 6
HELIX 51 AF6 GLN B 434 TYR B 438 5 5
HELIX 52 AF7 ASN B 446 GLY B 458 1 13
HELIX 53 AF8 ASP B 500 ASN B 502 5 3
SHEET 1 AA1 9 VAL A 21 VAL A 29 0
SHEET 2 AA1 9 VAL A 55 SER A 65 -1 O ALA A 59 N ASN A 24
SHEET 3 AA1 9 SER A 68 PRO A 77 -1 O ALA A 74 N ILE A 58
SHEET 4 AA1 9 ALA A 110 ALA A 114 -1 O THR A 111 N TRP A 75
SHEET 5 AA1 9 ARG A 83 SER A 86 1 N LEU A 85 O ALA A 110
SHEET 6 AA1 9 LYS A 162 CYS A 168 1 O TYR A 164 N PHE A 84
SHEET 7 AA1 9 GLY A 188 GLY A 192 1 O GLY A 192 N GLY A 167
SHEET 8 AA1 9 LYS A 372 GLY A 378 1 O LEU A 374 N VAL A 189
SHEET 9 AA1 9 TYR A 411 ILE A 416 1 O PHE A 414 N THR A 375
SHEET 1 AA2 2 THR A 33 SER A 36 0
SHEET 2 AA2 2 SER A 48 VAL A 51 -1 O VAL A 51 N THR A 33
SHEET 1 AA3 2 LEU A 288 TYR A 289 0
SHEET 2 AA3 2 LEU A 295 TYR A 297 -1 O TYR A 297 N LEU A 288
SHEET 1 AA4 2 ILE A 464 PHE A 469 0
SHEET 2 AA4 2 VAL A 477 HIS A 483 -1 O TYR A 479 N LYS A 468
SHEET 1 AA5 2 ASN A 490 TYR A 492 0
SHEET 2 AA5 2 TRP A 504 CYS A 506 -1 O GLN A 505 N VAL A 491
SHEET 1 AA6 9 VAL B 21 VAL B 29 0
SHEET 2 AA6 9 VAL B 55 SER B 65 -1 O ALA B 59 N ASN B 24
SHEET 3 AA6 9 SER B 68 PRO B 77 -1 O LEU B 72 N MET B 60
SHEET 4 AA6 9 ALA B 110 ALA B 114 -1 O THR B 111 N TRP B 75
SHEET 5 AA6 9 ARG B 83 SER B 86 1 N LEU B 85 O ALA B 110
SHEET 6 AA6 9 LYS B 162 CYS B 168 1 O TYR B 164 N PHE B 84
SHEET 7 AA6 9 GLY B 188 GLY B 192 1 O GLY B 192 N GLY B 167
SHEET 8 AA6 9 LYS B 372 GLY B 378 1 O LEU B 374 N VAL B 189
SHEET 9 AA6 9 TYR B 411 ILE B 416 1 O PHE B 414 N THR B 375
SHEET 1 AA7 2 THR B 33 SER B 36 0
SHEET 2 AA7 2 SER B 48 VAL B 51 -1 O VAL B 51 N THR B 33
SHEET 1 AA8 2 LEU B 288 TYR B 289 0
SHEET 2 AA8 2 LEU B 295 TYR B 297 -1 O TYR B 297 N LEU B 288
SHEET 1 AA9 2 ILE B 464 PHE B 469 0
SHEET 2 AA9 2 VAL B 477 HIS B 483 -1 O TYR B 479 N LYS B 468
SHEET 1 AB1 2 ASN B 490 TYR B 492 0
SHEET 2 AB1 2 TRP B 504 CYS B 506 -1 O GLN B 505 N VAL B 491
SSBOND 1 CYS A 9 CYS A 56 1555 1555 2.09
SSBOND 2 CYS A 44 CYS A 95 1555 1555 2.03
SSBOND 3 CYS A 168 CYS A 422 1555 1555 2.08
SSBOND 4 CYS A 237 CYS A 254 1555 1555 2.07
SSBOND 5 CYS A 263 CYS A 272 1555 1555 2.04
SSBOND 6 CYS A 484 CYS A 506 1555 1555 2.03
SSBOND 7 CYS B 9 CYS B 56 1555 1555 2.08
SSBOND 8 CYS B 44 CYS B 95 1555 1555 2.03
SSBOND 9 CYS B 168 CYS B 422 1555 1555 2.09
SSBOND 10 CYS B 237 CYS B 254 1555 1555 2.07
SSBOND 11 CYS B 263 CYS B 272 1555 1555 2.05
SSBOND 12 CYS B 484 CYS B 506 1555 1555 2.06
LINK ND2 ASN A 34 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 66 C1 NAG A 602 1555 1555 1.42
LINK ND2 ASN A 119 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 227 C1 NAG A 605 1555 1555 1.45
LINK O ASP A 238 CA CA A 611 1555 1555 2.46
LINK OD1 ASP A 238 CA CA A 611 1555 1555 2.40
LINK OD1 ASP A 241 CA CA A 611 1555 1555 2.50
LINK OD2 ASP A 241 CA CA A 611 1555 1555 2.47
LINK O ALA A 243 CA CA A 611 1555 1555 2.43
LINK OD1 ASP A 245 CA CA A 611 1555 1555 2.47
LINK O ILE A 247 CA CA A 611 1555 1555 2.40
LINK ND2 ASN A 268 C1 NAG A 606 1555 1555 1.45
LINK ND2 ASN A 497 C1 NAG A 607 1555 1555 1.43
LINK ND2 ASN B 34 C1 NAG B 601 1555 1555 1.44
LINK ND2 ASN B 66 C1 NAG B 602 1555 1555 1.47
LINK ND2 ASN B 119 C1 NAG B 603 1555 1555 1.47
LINK ND2 ASN B 227 C1 NAG B 604 1555 1555 1.44
LINK O ASP B 238 CA CA B 608 1555 1555 2.47
LINK OD1 ASP B 238 CA CA B 608 1555 1555 2.32
LINK OD1 ASP B 241 CA CA B 608 1555 1555 2.55
LINK OD2 ASP B 241 CA CA B 608 1555 1555 2.52
LINK O ALA B 243 CA CA B 608 1555 1555 2.37
LINK OD1 ASP B 245 CA CA B 608 1555 1555 2.50
LINK O ILE B 247 CA CA B 608 1555 1555 2.33
LINK ND2 ASN B 292 C1 NAG B 605 1555 1555 1.45
LINK O4 NAG A 603 C1 NAG A 604 1555 1555 1.47
LINK CA CA A 611 O HOH A 746 1555 1555 2.49
LINK CA CA B 608 O HOH B 810 1555 1555 2.44
CISPEP 1 TYR A 486 PRO A 487 0 7.39
CISPEP 2 GLY A 494 PRO A 495 0 -0.47
CISPEP 3 TYR B 486 PRO B 487 0 9.60
CISPEP 4 GLY B 494 PRO B 495 0 2.21
SITE 1 AC1 2 ARG A 395 ARG B 282
SITE 1 AC2 3 THR A 4 PHE A 5 GLN A 78
SITE 1 AC3 5 LYS A 177 LYS A 181 ASN A 355 HOH A 738
SITE 2 AC3 5 HOH A 739
SITE 1 AC4 6 ASP A 238 ASP A 241 ALA A 243 ASP A 245
SITE 2 AC4 6 ILE A 247 HOH A 746
SITE 1 AC5 4 ARG A 282 ARG B 395 HOH B 708 HOH B 792
SITE 1 AC6 5 LYS B 177 LYS B 181 ASN B 355 HOH B 739
SITE 2 AC6 5 HOH B 782
SITE 1 AC7 6 ASP B 238 ASP B 241 ALA B 243 ASP B 245
SITE 2 AC7 6 ILE B 247 HOH B 810
SITE 1 AC8 7 ASN A 34 SER A 48 SER B 122 GLU B 124
SITE 2 AC8 7 TYR B 327 PRO B 333 HOH B 737
SITE 1 AC9 7 ASN A 20 ALA A 63 SER A 65 ASN A 66
SITE 2 AC9 7 GLU A 131 HOH A 781 HOH A 783
SITE 1 AD1 9 ASN A 24 PHE A 25 ASP A 39 ALA A 59
SITE 2 AD1 9 THR A 71 GLU A 73 ASN A 119 HOH A 707
SITE 3 AD1 9 HOH A 869
SITE 1 AD2 4 ASP A 224 ASN A 227 VAL A 306 ASN B 27
SITE 1 AD3 7 ASN A 268 THR A 270 ASP A 440 ALA A 441
SITE 2 AD3 7 ASN A 442 HOH A 753 SER B 36
SITE 1 AD4 2 ASN A 497 TYR A 498
SITE 1 AD5 2 ASN B 34 HOH B 716
SITE 1 AD6 5 ASN B 20 ALA B 63 SER B 65 ASN B 66
SITE 2 AD6 5 HOH B 831
SITE 1 AD7 2 THR B 71 ASN B 119
SITE 1 AD8 3 THR A 4 ASN B 227 LYS B 231
SITE 1 AD9 1 ASN B 292
CRYST1 119.472 119.472 142.850 90.00 90.00 120.00 P 63 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 0.008370 0.004833 0.000000 0.00000
SCALE2 0.000000 0.009665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007000 0.00000
TER 3888 VAL A 507
TER 7797 VAL B 507
MASTER 481 0 19 53 34 0 28 6 8426 2 266 78
END |