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HEADER HYDROLASE 18-MAY-15 4ZV7
TITLE CRYSTAL STRUCTURE OF HEXAGONAL FORM OF LIPASE B FROM CANDIDA
TITLE 2 ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 26-342;
COMPND 5 SYNONYM: CALB;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 34362;
SOURCE 5 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS CAL-B, HEXAGONAL FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.STRZELCZYK,J.BLASZCZYK,G.BUJACZ
REVDAT 1 13-JAN-16 4ZV7 0
JRNL AUTH P.STRZELCZYK,G.D.BUJACZ,P.KIEBASINSKI,J.BASZCZYK
JRNL TITL CRYSTAL AND MOLECULAR STRUCTURE OF HEXAGONAL FORM OF LIPASE
JRNL TITL 2 B FROM CANDIDA ANTARCTICA.
JRNL REF ACTA BIOCHIM.POL. 2015
JRNL REFN ISSN 0001-527X
JRNL PMID 26716135
JRNL DOI 10.18388/ABP.2015_1065
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 20971
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1032
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1418
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.1750
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 332
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -1.04000
REMARK 3 B12 (A**2) : 0.16000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.698
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2449 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2289 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3371 ; 1.964 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5296 ; 1.136 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 6.744 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 85 ;34.756 ;24.706
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 348 ;13.024 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.036 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 397 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2805 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 517 ; 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): 1281 ; 1.000 ; 1.743
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1280 ; 0.990 ; 1.741
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1604 ; 1.537 ; 2.607
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1605 ; 1.541 ; 2.608
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1168 ; 1.395 ; 1.910
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1169 ; 1.395 ; 1.913
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1766 ; 2.132 ; 2.817
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3035 ; 5.510 ;16.203
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3036 ; 5.509 ;16.217
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 : 1
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 1 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1757 11.8976 16.3273
REMARK 3 T TENSOR
REMARK 3 T11: 0.0489 T22: 0.0081
REMARK 3 T33: 0.0248 T12: 0.0084
REMARK 3 T13: 0.0203 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.5089 L22: 0.2068
REMARK 3 L33: 0.3678 L12: -0.0066
REMARK 3 L13: 0.2814 L23: -0.2130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: -0.0414 S13: 0.0386
REMARK 3 S21: -0.0734 S22: -0.0298 S23: -0.0256
REMARK 3 S31: 0.0683 S32: 0.0054 S33: 0.0419
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 : 1.20
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 4ZV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209973.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD TITAN CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22034
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 77.110
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.5800
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: PHASER
REMARK 200 STARTING MODEL: 3W9B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% POLYETHYLENE GLYCOL 3350, 0.1M
REMARK 280 CITRIC ACID, AND 0.1M SODIUM ACETATE, PH 5.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 294.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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
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 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-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 68.62850
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 68.62850
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 68.62850
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 0.00000
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 0.00000
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 68.62850
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 68.62850
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 68.62850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL
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 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 OG1 THR A 21 O HOH A 901 1.96
REMARK 500 O HOH A 1084 O HOH A 1148 1.96
REMARK 500 O HOH A 1200 O HOH A 1218 1.98
REMARK 500 OD2 ASP A 265 O HOH A 902 2.01
REMARK 500 O HOH A 901 O HOH A 1036 2.11
REMARK 500 ND2 ASN A 74 O5 NAG A 800 2.19
REMARK 500 O HOH A 1018 O HOH A 1080 2.19
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 1127 O HOH A 1213 7555 2.18
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 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 238 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH1 ANGL. DEV. = 3.2 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 51 -94.67 -151.24
REMARK 500 ASP A 75 118.57 -30.58
REMARK 500 SER A 105 -121.66 50.33
REMARK 500 ASP A 134 64.54 -114.71
REMARK 500 THR A 186 45.75 -96.13
REMARK 500 ASP A 223 -159.48 -93.60
REMARK 500 ALA A 305 34.39 -144.02
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 A1231 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A1232 DISTANCE = 6.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 800 through NAG A 801 bound to ASN A 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TCA RELATED DB: PDB
REMARK 900 RELATED ID: 1TCB RELATED DB: PDB
REMARK 900 RELATED ID: 1TCC RELATED DB: PDB
REMARK 900 RELATED ID: 3W9B RELATED DB: PDB
DBREF 4ZV7 A 1 317 UNP P41365 LIPB_CANAR 26 342
SEQRES 1 A 317 LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS
SEQRES 2 A 317 SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER
SEQRES 3 A 317 PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY
SEQRES 4 A 317 THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP
SEQRES 5 A 317 ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP
SEQRES 6 A 317 ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL
SEQRES 7 A 317 ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR
SEQRES 8 A 317 ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP
SEQRES 9 A 317 SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE
SEQRES 10 A 317 PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA
SEQRES 11 A 317 PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO
SEQRES 12 A 317 LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN
SEQRES 13 A 317 GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN
SEQRES 14 A 317 ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU
SEQRES 15 A 317 TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER
SEQRES 16 A 317 ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS
SEQRES 17 A 317 ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL
SEQRES 18 A 317 ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR
SEQRES 19 A 317 VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN
SEQRES 20 A 317 ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO
SEQRES 21 A 317 LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA
SEQRES 22 A 317 ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL
SEQRES 23 A 317 ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO
SEQRES 24 A 317 TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER
SEQRES 25 A 317 GLY ILE VAL THR PRO
HET NAG A 800 14
HET NAG A 801 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 HOH *332(H2 O)
HELIX 1 AA1 PRO A 12 GLY A 19 1 8
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 SER A 105 PHE A 118 1 14
HELIX 6 AA6 PRO A 119 ARG A 122 5 4
HELIX 7 AA7 THR A 138 LEU A 140 5 3
HELIX 8 AA8 ALA A 141 LEU A 147 1 7
HELIX 9 AA9 ALA A 151 GLN A 157 1 7
HELIX 10 AB1 SER A 161 ALA A 170 1 10
HELIX 11 AB2 ALA A 212 GLY A 217 1 6
HELIX 12 AB3 ALA A 225 SER A 230 1 6
HELIX 13 AB4 SER A 230 SER A 243 1 14
HELIX 14 AB5 ARG A 249 TYR A 253 5 5
HELIX 15 AB6 GLY A 254 CYS A 258 5 5
HELIX 16 AB7 THR A 267 ALA A 276 1 10
HELIX 17 AB8 LEU A 277 GLY A 288 1 12
HELIX 18 AB9 MET A 298 ALA A 305 5 8
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N ILE A 34 O CYS A 64
SHEET 4 AA1 7 LEU A 99 TRP A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O MET A 129 N THR A 103
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.10
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.04
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.04
LINK ND2 ASN A 74 C1 NAG A 800 1555 1555 1.43
LINK O4 NAG A 800 C1 NAG A 801 1555 1555 1.44
CISPEP 1 PRO A 69 PRO A 70 0 -11.53
CISPEP 2 GLN A 191 PRO A 192 0 5.84
SITE 1 AC1 5 PRO A 70 ASN A 74 HOH A 958 HOH A1015
SITE 2 AC1 5 HOH A1053
CRYST1 89.034 89.034 137.257 90.00 90.00 120.00 P 63 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 0.011232 0.006485 0.000000 0.00000
SCALE2 0.000000 0.012969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007286 0.00000
TER 2354 PRO A 317
MASTER 397 0 2 18 9 0 2 6 2684 1 35 25
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