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HEADER HYDROLASE 19-AUG-03 1UKC
TITLE CRYSTAL STRUCTURE OF ASPERGILLUS NIGER ESTA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_COMMON: ASCOMYCETES;
SOURCE 4 GENE: ESTA;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: ASCOMYCETES;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NW128;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PIM4421-15
KEYWDS ESTERASE, FUNGI, A/B HYDROLASE FOLD, ACETYLCHOLINESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,A.A.HASPER,H.CHAHINIAN,M.JUIN,L.H.DE GRAAFF,
AUTHOR 2 P.MARCHOT
REVDAT 1 27-JUL-04 1UKC 0
JRNL AUTH Y.BOURNE,A.A.HASPER,H.CHAHINIAN,M.JUIN,
JRNL AUTH 2 L.H.DE GRAAFF,P.MARCHOT
JRNL TITL ASPERGILLUS NIGER PROTEIN ESTA DEFINES A NEW CLASS
JRNL TITL 2 OF FUNGAL ESTERASES WITHIN THE ALPHA/BETA
JRNL TITL 3 HYDROLASE FOLD SUPERFAMILY OF PROTEINS
JRNL REF STRUCTURE V. 12 677 2004
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 103714
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7588
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.1730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 9377
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.13000
REMARK 3 B22 (A**2) : -1.13000
REMARK 3 B33 (A**2) : 1.69000
REMARK 3 B12 (A**2) : -0.56000
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): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.018
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8438 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11506 ; 1.287 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1028 ; 5.759 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1268 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6548 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4193 ; 0.228 ; 0.200
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): 944 ; 0.169 ; 0.200
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): 40 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.281 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 5120 ; 0.582 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8230 ; 1.117 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3318 ; 1.952 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3276 ; 3.137 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 22 A 538
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7702 61.1643 -5.1135
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.1421
REMARK 3 T33: 0.1429 T12: -0.0013
REMARK 3 T13: -0.0914 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.4275 L22: 0.3721
REMARK 3 L33: 0.1894 L12: -0.0908
REMARK 3 L13: 0.1121 L23: 0.1130
REMARK 3 S TENSOR
REMARK 3 S11: 0.0161 S12: 0.0450 S13: -0.1085
REMARK 3 S21: 0.0583 S22: -0.0087 S23: 0.0703
REMARK 3 S31: -0.0455 S32: -0.0202 S33: -0.0074
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 26 B 538
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7241 44.4534 9.8958
REMARK 3 T TENSOR
REMARK 3 T11: 0.1389 T22: 0.1563
REMARK 3 T33: 0.1096 T12: 0.0466
REMARK 3 T13: -0.1058 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 0.5156 L22: 0.7125
REMARK 3 L33: 0.2180 L12: -0.1233
REMARK 3 L13: 0.2833 L23: -0.1144
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: 0.1046 S13: -0.0234
REMARK 3 S21: -0.0074 S22: -0.0263 S23: -0.0395
REMARK 3 S31: 0.0322 S32: 0.1190 S33: 0.0103
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UKC COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-2003.
REMARK 100 THE RCSB ID CODE IS RCSB005924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104730
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: CHIMERA MODEL BUILT FROM 1THG AND 1MAA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 6K, 100MM AMSO4, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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,1/2+Z
REMARK 290 5555 Y,-X+Y,1/2+Z
REMARK 290 6555 X-Y,X,1/2+Z
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 56.41350
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 56.41350
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 56.41350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, C
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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 LEU A 17
REMARK 465 PRO A 18
REMARK 465 THR A 19
REMARK 465 GLN A 20
REMARK 465 ALA A 21
REMARK 465 LEU B 17
REMARK 465 PRO B 18
REMARK 465 THR B 19
REMARK 465 GLN B 20
REMARK 465 ALA B 21
REMARK 465 SER B 22
REMARK 465 HIS B 23
REMARK 465 ASN B 24
REMARK 465 ALA B 25
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 GLN B 26 CG CD OE1 NE2
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
REMARK 500 O HOH 12 O HOH 750 1.63
REMARK 500 NH1 ARG A 35 O HOH 1112 1.73
REMARK 500 ND2 ASN A 511 C1 NAG 1801 1.78
REMARK 500 ND2 ASN B 511 C1 NAG 1851 1.86
REMARK 500 O4 NAG 1659 C1 NAG 1658 1.89
REMARK 500 ND2 ASN B 138 C1 NAG 1659 1.90
REMARK 500 ND2 ASN A 72 C1 NAG 1501 1.91
REMARK 500 ND2 ASN B 345 C1 NAG 1751 1.93
REMARK 500 ND2 ASN A 345 C1 NAG 1701 1.97
REMARK 500 O4 NAG C 608 C1 MAN 1602 1.97
REMARK 500 O HOH 157 O HOH 859 2.04
REMARK 500 O HOH 271 O HOH 737 2.13
REMARK 500 O HOH 499 O HOH 554 2.13
REMARK 500 N HIS A 23 CL CL 2902 2.14
REMARK 500 O HOH 138 O HOH 367 2.14
REMARK 500 O HOH 756 O HOH 887 2.16
REMARK 500 O HOH 382 O HOH 750 2.19
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 NE2 HIS A 475 CL CL 2902 2665 2.12
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO B 416 CB PRO B 416 CG 0.079
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 1119 DISTANCE = 5.51 ANGSTROMS
DBREF 1UKC A 17 538 GB 42405320 AAS13488 17 538
DBREF 1UKC B 17 538 GB 42405320 AAS13488 17 538
SEQRES 1 A 522 LEU PRO THR GLN ALA SER HIS ASN ALA GLN PRO VAL ILE
SEQRES 2 A 522 ASN LEU GLY TYR ALA ARG TYR GLN GLY VAL ARG LEU GLU
SEQRES 3 A 522 ALA GLY VAL ASP GLU PHE LEU GLY MET ARG TYR ALA SER
SEQRES 4 A 522 PRO PRO ILE GLY ASP LEU ARG PHE ARG ALA PRO GLN ASP
SEQRES 5 A 522 PRO PRO ALA ASN GLN THR LEU GLN SER ALA THR GLU TYR
SEQRES 6 A 522 GLY PRO ILE CYS ILE GLY LEU ASP GLU GLU GLU SER PRO
SEQRES 7 A 522 GLY ASP ILE SER GLU ASP CYS LEU PHE ILE ASN VAL PHE
SEQRES 8 A 522 LYS PRO SER THR ALA THR SER GLN SER LYS LEU PRO VAL
SEQRES 9 A 522 TRP LEU PHE ILE GLN GLY GLY GLY TYR ALA GLU ASN SER
SEQRES 10 A 522 ASN ALA ASN TYR ASN GLY THR GLN VAL ILE GLN ALA SER
SEQRES 11 A 522 ASP ASP VAL ILE VAL PHE VAL THR PHE ASN TYR ARG VAL
SEQRES 12 A 522 GLY ALA LEU GLY PHE LEU ALA SER GLU LYS VAL ARG GLN
SEQRES 13 A 522 ASN GLY ASP LEU ASN ALA GLY LEU LEU ASP GLN ARG LYS
SEQRES 14 A 522 ALA LEU ARG TRP VAL LYS GLN TYR ILE GLU GLN PHE GLY
SEQRES 15 A 522 GLY ASP PRO ASP HIS ILE VAL ILE HIS GLY VAL SER ALA
SEQRES 16 A 522 GLY ALA GLY SER VAL ALA TYR HIS LEU SER ALA TYR GLY
SEQRES 17 A 522 GLY LYS ASP GLU GLY LEU PHE ILE GLY ALA ILE VAL GLU
SEQRES 18 A 522 SER SER PHE TRP PRO THR GLN ARG THR VAL SER GLU MET
SEQRES 19 A 522 GLU PHE GLN PHE GLU ARG PHE VAL ASN ASP THR GLY CYS
SEQRES 20 A 522 SER SER ALA ARG ASP SER LEU GLU CYS LEU ARG GLU GLN
SEQRES 21 A 522 ASP ILE ALA THR ILE GLN LYS GLY ASN THR GLY SER PRO
SEQRES 22 A 522 PHE PRO GLY GLY SER SER SER PRO LEU PRO ASP TRP TYR
SEQRES 23 A 522 PHE LEU PRO VAL THR ASP GLY SER LEU VAL PRO ASP GLU
SEQRES 24 A 522 LEU TYR ASN ALA PHE ASP ALA GLY ASN PHE ILE LYS VAL
SEQRES 25 A 522 PRO VAL LEU VAL GLY ASP ASP THR ASP GLU GLY SER ASN
SEQRES 26 A 522 PHE ALA TYR ASN ALA SER SER SER ALA ASP VAL SER ARG
SEQRES 27 A 522 PHE PHE LYS ASN ASN TYR PRO ASN LEU THR SER GLN GLN
SEQRES 28 A 522 LEU ASN GLU ILE ASN GLN VAL TYR PRO ARG GLY LYS LEU
SEQRES 29 A 522 LEU PRO ARG HIS ALA ALA TYR PHE GLY ALA SER SER ALA
SEQRES 30 A 522 ALA TYR GLY ASP ALA THR PHE THR CYS PRO GLY ASN HIS
SEQRES 31 A 522 VAL ALA SER SER ALA ALA ARG TYR LEU PRO ASN SER VAL
SEQRES 32 A 522 TRP ASN TYR ARG VAL ASN ILE ILE ASP GLU SER ASN ILE
SEQRES 33 A 522 ALA GLY GLY ILE GLY VAL PRO HIS THR PHE GLU LEU PRO
SEQRES 34 A 522 ALA ILE PHE GLY ALA GLY SER THR GLY THR LEU SER SER
SEQRES 35 A 522 ASP SER SER TYR LEU THR TYR ASN ALA ALA ILE ILE PRO
SEQRES 36 A 522 VAL THR MET HIS TYR PHE ILE SER PHE VAL GLN THR LEU
SEQRES 37 A 522 ASN PRO ASN THR TYR ARG TYR ALA THR ALA PRO GLU TRP
SEQRES 38 A 522 ASN THR TRP GLY ASN GLY GLN ARG LEU ARG LEU GLN THR
SEQRES 39 A 522 ASN ASP THR ALA MET GLU ALA VAL PRO GLU SER SER LEU
SEQRES 40 A 522 GLN ASP CYS ALA PHE TRP LYS SER LEU THR VAL PRO MET
SEQRES 41 A 522 GLU VAL
SEQRES 1 B 522 LEU PRO THR GLN ALA SER HIS ASN ALA GLN PRO VAL ILE
SEQRES 2 B 522 ASN LEU GLY TYR ALA ARG TYR GLN GLY VAL ARG LEU GLU
SEQRES 3 B 522 ALA GLY VAL ASP GLU PHE LEU GLY MET ARG TYR ALA SER
SEQRES 4 B 522 PRO PRO ILE GLY ASP LEU ARG PHE ARG ALA PRO GLN ASP
SEQRES 5 B 522 PRO PRO ALA ASN GLN THR LEU GLN SER ALA THR GLU TYR
SEQRES 6 B 522 GLY PRO ILE CYS ILE GLY LEU ASP GLU GLU GLU SER PRO
SEQRES 7 B 522 GLY ASP ILE SER GLU ASP CYS LEU PHE ILE ASN VAL PHE
SEQRES 8 B 522 LYS PRO SER THR ALA THR SER GLN SER LYS LEU PRO VAL
SEQRES 9 B 522 TRP LEU PHE ILE GLN GLY GLY GLY TYR ALA GLU ASN SER
SEQRES 10 B 522 ASN ALA ASN TYR ASN GLY THR GLN VAL ILE GLN ALA SER
SEQRES 11 B 522 ASP ASP VAL ILE VAL PHE VAL THR PHE ASN TYR ARG VAL
SEQRES 12 B 522 GLY ALA LEU GLY PHE LEU ALA SER GLU LYS VAL ARG GLN
SEQRES 13 B 522 ASN GLY ASP LEU ASN ALA GLY LEU LEU ASP GLN ARG LYS
SEQRES 14 B 522 ALA LEU ARG TRP VAL LYS GLN TYR ILE GLU GLN PHE GLY
SEQRES 15 B 522 GLY ASP PRO ASP HIS ILE VAL ILE HIS GLY VAL SER ALA
SEQRES 16 B 522 GLY ALA GLY SER VAL ALA TYR HIS LEU SER ALA TYR GLY
SEQRES 17 B 522 GLY LYS ASP GLU GLY LEU PHE ILE GLY ALA ILE VAL GLU
SEQRES 18 B 522 SER SER PHE TRP PRO THR GLN ARG THR VAL SER GLU MET
SEQRES 19 B 522 GLU PHE GLN PHE GLU ARG PHE VAL ASN ASP THR GLY CYS
SEQRES 20 B 522 SER SER ALA ARG ASP SER LEU GLU CYS LEU ARG GLU GLN
SEQRES 21 B 522 ASP ILE ALA THR ILE GLN LYS GLY ASN THR GLY SER PRO
SEQRES 22 B 522 PHE PRO GLY GLY SER SER SER PRO LEU PRO ASP TRP TYR
SEQRES 23 B 522 PHE LEU PRO VAL THR ASP GLY SER LEU VAL PRO ASP GLU
SEQRES 24 B 522 LEU TYR ASN ALA PHE ASP ALA GLY ASN PHE ILE LYS VAL
SEQRES 25 B 522 PRO VAL LEU VAL GLY ASP ASP THR ASP GLU GLY SER ASN
SEQRES 26 B 522 PHE ALA TYR ASN ALA SER SER SER ALA ASP VAL SER ARG
SEQRES 27 B 522 PHE PHE LYS ASN ASN TYR PRO ASN LEU THR SER GLN GLN
SEQRES 28 B 522 LEU ASN GLU ILE ASN GLN VAL TYR PRO ARG GLY LYS LEU
SEQRES 29 B 522 LEU PRO ARG HIS ALA ALA TYR PHE GLY ALA SER SER ALA
SEQRES 30 B 522 ALA TYR GLY ASP ALA THR PHE THR CYS PRO GLY ASN HIS
SEQRES 31 B 522 VAL ALA SER SER ALA ALA ARG TYR LEU PRO ASN SER VAL
SEQRES 32 B 522 TRP ASN TYR ARG VAL ASN ILE ILE ASP GLU SER ASN ILE
SEQRES 33 B 522 ALA GLY GLY ILE GLY VAL PRO HIS THR PHE GLU LEU PRO
SEQRES 34 B 522 ALA ILE PHE GLY ALA GLY SER THR GLY THR LEU SER SER
SEQRES 35 B 522 ASP SER SER TYR LEU THR TYR ASN ALA ALA ILE ILE PRO
SEQRES 36 B 522 VAL THR MET HIS TYR PHE ILE SER PHE VAL GLN THR LEU
SEQRES 37 B 522 ASN PRO ASN THR TYR ARG TYR ALA THR ALA PRO GLU TRP
SEQRES 38 B 522 ASN THR TRP GLY ASN GLY GLN ARG LEU ARG LEU GLN THR
SEQRES 39 B 522 ASN ASP THR ALA MET GLU ALA VAL PRO GLU SER SER LEU
SEQRES 40 B 522 GLN ASP CYS ALA PHE TRP LYS SER LEU THR VAL PRO MET
SEQRES 41 B 522 GLU VAL
MODRES 1UKC ASN A 138 ASN GLYCOSYLATION SITE
HET NAG 1501 14
HET NAG 1502 14
HET NAG C 609 14
HET NAG C 608 14
HET MAN 1602 11
HET MAN 1601 11
HET MAN 1603 11
HET NAG 1701 14
HET NAG 1801 14
HET NAG 1802 14
HET NAG 1951 14
HET NAG 1551 14
HET NAG 1659 14
HET NAG 1658 14
HET MAN 1652 11
HET MAN 1651 11
HET MAN 1653 11
HET NAG 1751 14
HET NAG 1851 14
HET NAG 1852 14
HET SO4 2901 5
HET SO4 2951 5
HET CL 2902 1
HET EDO 1902 4
HET EDO 1912 4
HET EDO 1922 4
HET EDO 1932 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG NAG
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 14(C8 H15 N1 O6)
FORMUL 6 MAN 6(C6 H12 O6)
FORMUL 22 SO4 2(O4 S1 2-)
FORMUL 24 CL CL1 1-
FORMUL 25 EDO 4(C2 H6 O2)
FORMUL 29 HOH *1149(H2 O1)
HELIX 1 1 ILE A 58 ARG A 62 5 5
HELIX 2 2 GLY A 139 SER A 146 1 8
HELIX 3 3 VAL A 159 LEU A 165 1 7
HELIX 4 4 SER A 167 ASN A 173 1 7
HELIX 5 5 ASN A 177 ILE A 194 1 18
HELIX 6 6 GLU A 195 PHE A 197 5 3
HELIX 7 7 SER A 210 SER A 221 1 12
HELIX 8 8 ALA A 222 GLY A 225 5 4
HELIX 9 9 VAL A 247 GLU A 249 5 3
HELIX 10 10 MET A 250 THR A 261 1 12
HELIX 11 11 ASP A 268 GLN A 276 1 9
HELIX 12 12 ASP A 277 ASN A 285 1 9
HELIX 13 13 GLU A 315 GLY A 323 1 9
HELIX 14 14 ASP A 337 PHE A 342 5 6
HELIX 15 15 SER A 348 TYR A 360 1 13
HELIX 16 16 THR A 364 TYR A 375 1 12
HELIX 17 17 TYR A 387 PHE A 400 1 14
HELIX 18 18 PHE A 400 LEU A 415 1 16
HELIX 19 19 ASP A 428 GLY A 434 1 7
HELIX 20 20 GLU A 443 GLY A 449 1 7
HELIX 21 21 SER A 460 THR A 464 5 5
HELIX 22 22 ALA A 468 LEU A 484 1 17
HELIX 23 23 PRO A 519 SER A 531 1 13
HELIX 24 24 LEU A 532 GLU A 537 1 6
HELIX 25 25 ILE B 58 ARG B 62 5 5
HELIX 26 26 GLY B 139 SER B 146 1 8
HELIX 27 27 VAL B 159 LEU B 165 1 7
HELIX 28 28 SER B 167 ASN B 173 1 7
HELIX 29 29 ASN B 177 ILE B 194 1 18
HELIX 30 30 GLU B 195 PHE B 197 5 3
HELIX 31 31 SER B 210 SER B 221 1 12
HELIX 32 32 ALA B 222 GLY B 225 5 4
HELIX 33 33 VAL B 247 GLU B 249 5 3
HELIX 34 34 MET B 250 THR B 261 1 12
HELIX 35 35 ASP B 268 GLN B 276 1 9
HELIX 36 36 ASP B 277 ASN B 285 1 9
HELIX 37 37 GLU B 315 GLY B 323 1 9
HELIX 38 38 ASP B 337 PHE B 342 5 6
HELIX 39 39 SER B 348 TYR B 360 1 13
HELIX 40 40 THR B 364 TYR B 375 1 12
HELIX 41 41 TYR B 387 PHE B 400 1 14
HELIX 42 42 PHE B 400 LEU B 415 1 16
HELIX 43 43 ASP B 428 GLY B 434 1 7
HELIX 44 44 GLU B 443 GLY B 449 1 7
HELIX 45 45 SER B 460 THR B 464 5 5
HELIX 46 46 ALA B 468 LEU B 484 1 17
HELIX 47 47 PRO B 519 SER B 531 1 13
HELIX 48 48 LEU B 532 GLU B 537 1 6
SHEET 1 A 3 VAL A 28 ASN A 30 0
SHEET 2 A 3 ARG A 35 GLN A 37 -1 O TYR A 36 N ILE A 29
SHEET 3 A 3 GLN A 76 SER A 77 1 O GLN A 76 N ARG A 35
SHEET 1 B11 VAL A 39 ARG A 40 0
SHEET 2 B11 VAL A 45 ARG A 52 -1 O GLU A 47 N VAL A 39
SHEET 3 B11 PHE A 103 PRO A 109 -1 O LYS A 108 N ASP A 46
SHEET 4 B11 VAL A 151 PHE A 155 -1 O PHE A 152 N PHE A 107
SHEET 5 B11 LEU A 118 ILE A 124 1 N PHE A 123 O VAL A 153
SHEET 6 B11 GLY A 199 VAL A 209 1 O HIS A 207 N ILE A 124
SHEET 7 B11 GLY A 233 GLU A 237 1 O ILE A 235 N ILE A 206
SHEET 8 B11 VAL A 330 ASP A 335 1 O LEU A 331 N VAL A 236
SHEET 9 B11 VAL A 419 VAL A 424 1 O VAL A 424 N ASP A 334
SHEET 10 B11 GLN A 504 LEU A 508 1 O LEU A 508 N ARG A 423
SHEET 11 B11 ALA A 514 ALA A 517 -1 O ALA A 514 N ARG A 507
SHEET 1 C 2 ILE A 84 CYS A 85 0
SHEET 2 C 2 ILE A 97 SER A 98 1 O SER A 98 N ILE A 84
SHEET 1 D 3 VAL B 28 ASN B 30 0
SHEET 2 D 3 ARG B 35 GLN B 37 -1 O TYR B 36 N ILE B 29
SHEET 3 D 3 LEU B 75 SER B 77 1 O GLN B 76 N ARG B 35
SHEET 1 E11 VAL B 39 ARG B 40 0
SHEET 2 E11 VAL B 45 ARG B 52 -1 O GLU B 47 N VAL B 39
SHEET 3 E11 PHE B 103 PRO B 109 -1 O LYS B 108 N ASP B 46
SHEET 4 E11 VAL B 151 PHE B 155 -1 O THR B 154 N ASN B 105
SHEET 5 E11 LEU B 118 ILE B 124 1 N PHE B 123 O VAL B 153
SHEET 6 E11 GLY B 199 VAL B 209 1 O HIS B 207 N ILE B 124
SHEET 7 E11 GLY B 233 GLU B 237 1 O GLU B 237 N GLY B 208
SHEET 8 E11 VAL B 330 ASP B 335 1 O LEU B 331 N VAL B 236
SHEET 9 E11 VAL B 419 VAL B 424 1 O TRP B 420 N VAL B 332
SHEET 10 E11 GLN B 504 LEU B 508 1 O LEU B 508 N ARG B 423
SHEET 11 E11 ALA B 514 ALA B 517 -1 O ALA B 514 N ARG B 507
SHEET 1 F 2 ILE B 84 CYS B 85 0
SHEET 2 F 2 ILE B 97 SER B 98 1 O SER B 98 N ILE B 84
SSBOND 1 CYS A 85 CYS A 101
SSBOND 2 CYS A 263 CYS A 272
SSBOND 3 CYS A 402 CYS A 526
SSBOND 4 CYS B 85 CYS B 101
SSBOND 5 CYS B 263 CYS B 272
SSBOND 6 CYS B 402 CYS B 526
LINK ND2 ASN A 138 C1 NAG C 609
LINK O4 NAG C 609 C1 NAG C 608
CISPEP 1 SER A 296 PRO A 297 0 -1.88
CISPEP 2 SER B 296 PRO B 297 0 -4.44
CRYST1 167.489 167.489 112.827 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 0.005971 0.003447 0.000000 0.00000
SCALE2 0.000000 0.006894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008863 0.00000
END |