HEADER HYDROLASE 17-FEB-16 5I78
TITLE CRYSTAL STRUCTURE OF A BETA-1,4-ENDOGLUCANASE FROM ASPERGILLUS NIGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-BETA-1, 4-GLUCANASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 31-331;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 GENE: EG1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: P. PASTORIS X33;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPICZAA
KEYWDS SUBSTRATE BINDING, ENDOGLUCANASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.D.LIU,J.J.YAN,Y.J.LI,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
REVDAT 3 08-NOV-23 5I78 1 HETSYN
REVDAT 2 29-JUL-20 5I78 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 21-DEC-16 5I78 0
JRNL AUTH J.YAN,W.LIU,Y.LI,H.L.LAI,Y.ZHENG,J.W.HUANG,C.C.CHEN,Y.CHEN,
JRNL AUTH 2 J.JIN,H.LI,R.T.GUO
JRNL TITL FUNCTIONAL AND STRUCTURAL ANALYSIS OF PICHIA
JRNL TITL 2 PASTORIS-EXPRESSED ASPERGILLUS NIGER 1,4-BETA-ENDOGLUCANASE
JRNL REF BIOCHEM. BIOPHYS. RES. V. 475 8 2016
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 27154222
JRNL DOI 10.1016/J.BBRC.2016.05.012
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 78792
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4044
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5687
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.1610
REMARK 3 BIN FREE R VALUE SET COUNT : 271
REMARK 3 BIN FREE R VALUE : 0.1960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4796
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 129
REMARK 3 SOLVENT ATOMS : 591
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 0.31000
REMARK 3 B33 (A**2) : -0.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.235
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
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): 5052 ; 0.024 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4425 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6854 ; 2.179 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10179 ; 1.079 ; 3.007
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 608 ; 6.662 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 252 ;38.654 ;25.476
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 738 ;13.456 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;22.307 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 716 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5798 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1190 ; 0.001 ; 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): 2438 ; 1.572 ; 1.168
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2437 ; 1.543 ; 1.166
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3044 ; 2.284 ; 1.751
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5I78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-14
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 : NSRRC
REMARK 200 BEAMLINE : BL13C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97622
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82837
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: 1GZJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG600, CA(OAC)2, CACODYLATE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.63650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.41100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.63650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.41100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 O HOH A 562 O HOH A 748 1.37
REMARK 500 O HOH A 734 O HOH A 748 1.54
REMARK 500 O HOH A 752 O HOH A 769 1.74
REMARK 500 O HOH A 506 O HOH A 508 1.77
REMARK 500 OD1 ASP B 167 O HOH B 501 1.81
REMARK 500 O HOH B 752 O HOH B 776 1.84
REMARK 500 O HOH A 733 O HOH A 757 1.86
REMARK 500 O HOH B 540 O HOH B 611 1.89
REMARK 500 O4 NAG A 404 O HOH A 501 2.01
REMARK 500 O HOH B 745 O HOH B 759 2.01
REMARK 500 O HOH A 507 O HOH A 606 2.04
REMARK 500 O HOH A 654 O HOH A 751 2.05
REMARK 500 O HOH A 735 O HOH A 748 2.06
REMARK 500 O HOH A 672 O HOH A 751 2.08
REMARK 500 OH TYR B 331 O HOH B 502 2.10
REMARK 500 O1 PGE B 405 O1 PGE B 407 2.10
REMARK 500 OE1 GLU B 141 O HOH B 503 2.14
REMARK 500 O HOH B 764 O HOH B 774 2.18
REMARK 500 O HOH A 517 O HOH A 761 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 601 O HOH B 643 1554 1.71
REMARK 500 O HOH A 662 O HOH B 683 1554 1.81
REMARK 500 O HOH A 592 O HOH A 672 4555 1.87
REMARK 500 O HOH B 648 O HOH B 756 1565 2.15
REMARK 500 OE2 GLU A 237 OE2 GLU A 237 2655 2.16
REMARK 500 O HOH A 575 O HOH B 507 4546 2.17
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 39 CD GLU A 39 OE2 0.072
REMARK 500 GLU A 314 CD GLU A 314 OE1 0.067
REMARK 500 TYR B 147 CE1 TYR B 147 CZ 0.089
REMARK 500 SER B 298 CB SER B 298 OG -0.092
REMARK 500 TYR B 309 CZ TYR B 309 CE2 -0.083
REMARK 500 TYR B 331 CE1 TYR B 331 CZ -0.081
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 76 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 94 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 118 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 GLU B 29 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 ASP B 69 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 124 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 124 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 MET B 154 CG - SD - CE ANGL. DEV. = -10.1 DEGREES
REMARK 500 VAL B 206 CG1 - CB - CG2 ANGL. DEV. = -15.5 DEGREES
REMARK 500 ASP B 308 CB - CG - OD1 ANGL. DEV. = 6.9 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 158 144.83 -178.58
REMARK 500 ASN A 290 49.05 -141.06
REMARK 500 ASN B 158 147.34 -172.67
REMARK 500 ASN B 290 41.90 -141.98
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 GLU B 29 PHE B 30 125.92
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 B 804 DISTANCE = 8.14 ANGSTROMS
REMARK 525 HOH B 805 DISTANCE = 8.61 ANGSTROMS
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 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 29 OE1
REMARK 620 2 GLU A 29 OE2 50.3
REMARK 620 3 LEU A 332 O 89.9 86.3
REMARK 620 4 LEU A 332 OXT 78.9 114.6 51.2
REMARK 620 5 HOH A 717 O 128.9 79.2 79.1 124.8
REMARK 620 6 ASP B 69 O 94.6 82.4 161.0 147.9 83.7
REMARK 620 7 ASP B 69 OD1 75.8 119.9 122.0 70.9 150.1 77.0
REMARK 620 8 HOH B 738 O 154.6 155.0 90.0 81.2 75.9 93.8 82.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 95 OE2
REMARK 620 2 NAG A 405 O7 94.7
REMARK 620 3 HOH A 620 O 96.7 3.0
REMARK 620 4 HOH A 628 O 93.8 1.6 3.1
REMARK 620 5 HOH A 734 O 95.3 3.4 1.8 2.6
REMARK 620 6 HOH A 747 O 94.7 4.6 3.2 3.4 1.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 329 O
REMARK 620 2 LEU A 332 OXT 83.8
REMARK 620 3 HOH A 639 O 92.9 78.9
REMARK 620 4 HOH A 736 O 94.4 87.5 163.8
REMARK 620 5 ASP B 69 OD1 156.8 73.4 79.2 88.5
REMARK 620 6 ASP B 69 OD2 152.7 122.9 87.6 92.4 49.6
REMARK 620 7 HOH B 692 O 80.7 162.8 94.4 101.0 121.3 72.0
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I79 RELATED DB: PDB
REMARK 900 RELATED ID: 5I77 RELATED DB: PDB
DBREF1 5I78 A 31 331 UNP A0A023UH08_ASPNG
DBREF2 5I78 A A0A023UH08 31 331
DBREF1 5I78 B 31 331 UNP A0A023UH08_ASPNG
DBREF2 5I78 B A0A023UH08 31 331
SEQADV 5I78 ALA A 28 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 GLU A 29 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 PHE A 30 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 ALA A 267 UNP A0A023UH0 GLU 267 ENGINEERED MUTATION
SEQADV 5I78 LEU A 332 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 ALA B 28 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 GLU B 29 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 PHE B 30 UNP A0A023UH0 EXPRESSION TAG
SEQADV 5I78 ALA B 267 UNP A0A023UH0 GLU 267 ENGINEERED MUTATION
SEQADV 5I78 LEU B 332 UNP A0A023UH0 EXPRESSION TAG
SEQRES 1 A 305 ALA GLU PHE VAL PHE GLU TRP PHE GLY SER ASN GLU SER
SEQRES 2 A 305 GLY ALA GLU PHE GLY THR ASN ILE PRO GLY VAL TRP GLY
SEQRES 3 A 305 THR ASP TYR ILE PHE PRO ASP PRO SER ALA ILE SER THR
SEQRES 4 A 305 LEU ILE ASP LYS GLY MET ASN PHE PHE ARG VAL GLN PHE
SEQRES 5 A 305 MET MET GLU ARG LEU LEU PRO ASP SER MET THR GLY SER
SEQRES 6 A 305 TYR ASP GLU GLU TYR LEU ALA ASN LEU THR THR VAL ILE
SEQRES 7 A 305 LYS ALA VAL THR ASP GLY GLY ALA HIS ALA LEU VAL ASP
SEQRES 8 A 305 PRO HIS ASN TYR GLY ARG TYR ASN GLY GLU ILE ILE SER
SEQRES 9 A 305 SER THR SER ASP PHE GLN THR PHE TRP GLU ASN LEU ALA
SEQRES 10 A 305 GLY GLN TYR LYS ASP ASN ASP LEU VAL MET PHE ASP THR
SEQRES 11 A 305 ASN ASN GLU TYR HIS ASP MET ASP GLN ASP LEU VAL LEU
SEQRES 12 A 305 ASN LEU ASN GLN ALA ALA ILE ASN GLY ILE ARG ALA ALA
SEQRES 13 A 305 GLY ALA THR SER GLN TYR ILE PHE VAL GLU GLY ASN SER
SEQRES 14 A 305 TRP THR GLY ALA TRP THR TRP VAL ASP VAL ASN ASP ASN
SEQRES 15 A 305 MET LYS ASN LEU THR ASP PRO GLU ASP LYS ILE VAL TYR
SEQRES 16 A 305 GLU MET HIS GLN TYR LEU ASP SER ASP GLY SER GLY THR
SEQRES 17 A 305 SER GLU THR CYS VAL SER GLU THR ILE GLY LYS GLU ARG
SEQRES 18 A 305 VAL THR GLU ALA THR GLN TRP LEU LYS ASP ASN LYS LYS
SEQRES 19 A 305 VAL GLY PHE ILE GLY ALA TYR ALA GLY GLY SER ASN ASP
SEQRES 20 A 305 VAL CYS ARG SER ALA VAL SER GLY MET LEU GLU TYR MET
SEQRES 21 A 305 ALA ASN ASN THR ASP VAL TRP LYS GLY ALA SER TRP TRP
SEQRES 22 A 305 ALA ALA GLY PRO TRP TRP GLY ASP TYR ILE PHE SER LEU
SEQRES 23 A 305 GLU PRO PRO ASP GLY THR ALA TYR THR GLY MET LEU ASP
SEQRES 24 A 305 ILE LEU GLU ALA TYR LEU
SEQRES 1 B 305 ALA GLU PHE VAL PHE GLU TRP PHE GLY SER ASN GLU SER
SEQRES 2 B 305 GLY ALA GLU PHE GLY THR ASN ILE PRO GLY VAL TRP GLY
SEQRES 3 B 305 THR ASP TYR ILE PHE PRO ASP PRO SER ALA ILE SER THR
SEQRES 4 B 305 LEU ILE ASP LYS GLY MET ASN PHE PHE ARG VAL GLN PHE
SEQRES 5 B 305 MET MET GLU ARG LEU LEU PRO ASP SER MET THR GLY SER
SEQRES 6 B 305 TYR ASP GLU GLU TYR LEU ALA ASN LEU THR THR VAL ILE
SEQRES 7 B 305 LYS ALA VAL THR ASP GLY GLY ALA HIS ALA LEU VAL ASP
SEQRES 8 B 305 PRO HIS ASN TYR GLY ARG TYR ASN GLY GLU ILE ILE SER
SEQRES 9 B 305 SER THR SER ASP PHE GLN THR PHE TRP GLU ASN LEU ALA
SEQRES 10 B 305 GLY GLN TYR LYS ASP ASN ASP LEU VAL MET PHE ASP THR
SEQRES 11 B 305 ASN ASN GLU TYR HIS ASP MET ASP GLN ASP LEU VAL LEU
SEQRES 12 B 305 ASN LEU ASN GLN ALA ALA ILE ASN GLY ILE ARG ALA ALA
SEQRES 13 B 305 GLY ALA THR SER GLN TYR ILE PHE VAL GLU GLY ASN SER
SEQRES 14 B 305 TRP THR GLY ALA TRP THR TRP VAL ASP VAL ASN ASP ASN
SEQRES 15 B 305 MET LYS ASN LEU THR ASP PRO GLU ASP LYS ILE VAL TYR
SEQRES 16 B 305 GLU MET HIS GLN TYR LEU ASP SER ASP GLY SER GLY THR
SEQRES 17 B 305 SER GLU THR CYS VAL SER GLU THR ILE GLY LYS GLU ARG
SEQRES 18 B 305 VAL THR GLU ALA THR GLN TRP LEU LYS ASP ASN LYS LYS
SEQRES 19 B 305 VAL GLY PHE ILE GLY ALA TYR ALA GLY GLY SER ASN ASP
SEQRES 20 B 305 VAL CYS ARG SER ALA VAL SER GLY MET LEU GLU TYR MET
SEQRES 21 B 305 ALA ASN ASN THR ASP VAL TRP LYS GLY ALA SER TRP TRP
SEQRES 22 B 305 ALA ALA GLY PRO TRP TRP GLY ASP TYR ILE PHE SER LEU
SEQRES 23 B 305 GLU PRO PRO ASP GLY THR ALA TYR THR GLY MET LEU ASP
SEQRES 24 B 305 ILE LEU GLU ALA TYR LEU
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET NAG A 404 14
HET NAG A 405 14
HET PGE A 406 10
HET PGE B 401 10
HET PGE B 402 10
HET NAG B 403 14
HET PGE B 404 10
HET PGE B 405 10
HET PGE B 406 10
HET PGE B 407 10
HET NAG B 408 14
HETNAM CA CALCIUM ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PGE TRIETHYLENE GLYCOL
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
FORMUL 3 CA 3(CA 2+)
FORMUL 6 NAG 4(C8 H15 N O6)
FORMUL 8 PGE 7(C6 H14 O4)
FORMUL 17 HOH *591(H2 O)
HELIX 1 AA1 ASP A 60 LYS A 70 1 11
HELIX 2 AA2 MET A 80 LEU A 85 1 6
HELIX 3 AA3 ASP A 94 GLY A 111 1 18
HELIX 4 AA4 SER A 132 LYS A 148 1 17
HELIX 5 AA5 ASP A 165 ALA A 183 1 19
HELIX 6 AA6 THR A 202 ASN A 207 1 6
HELIX 7 AA7 ASP A 208 LEU A 213 5 6
HELIX 8 AA8 THR A 243 LYS A 260 1 18
HELIX 9 AA9 ASN A 273 ASN A 289 1 17
HELIX 10 AB1 GLY A 318 GLU A 329 1 12
HELIX 11 AB2 ALA A 330 LEU A 332 5 3
HELIX 12 AB3 ASP B 60 GLY B 71 1 12
HELIX 13 AB4 MET B 80 LEU B 85 1 6
HELIX 14 AB5 ASP B 94 GLY B 111 1 18
HELIX 15 AB6 SER B 132 LYS B 148 1 17
HELIX 16 AB7 ASP B 165 ALA B 183 1 19
HELIX 17 AB8 THR B 202 ASN B 207 1 6
HELIX 18 AB9 ASP B 208 LEU B 213 5 6
HELIX 19 AC1 THR B 243 LYS B 260 1 18
HELIX 20 AC2 ASN B 273 ASN B 289 1 17
HELIX 21 AC3 GLY B 318 MET B 324 1 7
HELIX 22 AC4 MET B 324 ALA B 330 1 7
SHEET 1 AA1 9 TRP A 34 GLU A 39 0
SHEET 2 AA1 9 PHE A 74 PHE A 79 1 O ARG A 76 N GLU A 39
SHEET 3 AA1 9 HIS A 114 PRO A 119 1 O LEU A 116 N PHE A 75
SHEET 4 AA1 9 VAL A 153 ASP A 156 1 O MET A 154 N VAL A 117
SHEET 5 AA1 9 ILE A 190 GLU A 193 1 O PHE A 191 N PHE A 155
SHEET 6 AA1 9 ILE A 220 TYR A 227 1 O GLU A 223 N VAL A 192
SHEET 7 AA1 9 GLY A 263 ALA A 269 1 O ALA A 267 N GLN A 226
SHEET 8 AA1 9 TRP A 294 ALA A 302 1 O TRP A 300 N TYR A 268
SHEET 9 AA1 9 TRP A 34 GLU A 39 1 N ASN A 38 O TRP A 299
SHEET 1 AA2 2 ARG A 124 TYR A 125 0
SHEET 2 AA2 2 GLU A 128 ILE A 129 -1 O GLU A 128 N TYR A 125
SHEET 1 AA3 9 TRP B 34 GLU B 39 0
SHEET 2 AA3 9 PHE B 74 PHE B 79 1 O ARG B 76 N GLU B 39
SHEET 3 AA3 9 HIS B 114 PRO B 119 1 O LEU B 116 N PHE B 75
SHEET 4 AA3 9 VAL B 153 ASP B 156 1 O MET B 154 N ALA B 115
SHEET 5 AA3 9 ILE B 190 GLU B 193 1 O PHE B 191 N PHE B 155
SHEET 6 AA3 9 ILE B 220 TYR B 227 1 O GLU B 223 N VAL B 192
SHEET 7 AA3 9 GLY B 263 ALA B 269 1 O PHE B 264 N MET B 224
SHEET 8 AA3 9 TRP B 294 ALA B 302 1 O TRP B 300 N TYR B 268
SHEET 9 AA3 9 TRP B 34 GLU B 39 1 N ASN B 38 O TRP B 299
SHEET 1 AA4 2 ARG B 124 TYR B 125 0
SHEET 2 AA4 2 GLU B 128 ILE B 129 -1 O GLU B 128 N TYR B 125
SSBOND 1 CYS A 239 CYS A 276 1555 1555 2.09
SSBOND 2 CYS B 239 CYS B 276 1555 1555 2.12
LINK ND2 ASN A 100 C1 NAG A 404 1555 1555 1.53
LINK ND2 ASN A 289 C1 NAG A 405 1555 1555 1.47
LINK ND2 ASN B 100 C1 NAG B 403 1555 1555 1.51
LINK ND2 ASN B 289 C1 NAG B 408 1555 1555 1.48
LINK OE1 GLU A 29 CA CA A 401 1555 1555 2.45
LINK OE2 GLU A 29 CA CA A 401 1555 1555 2.62
LINK OE2 GLU A 95 CA CA A 403 1555 1545 2.47
LINK O GLU A 329 CA CA A 402 1555 1555 2.40
LINK O LEU A 332 CA CA A 401 1555 1555 2.38
LINK OXT LEU A 332 CA CA A 401 1555 1555 2.56
LINK OXT LEU A 332 CA CA A 402 1555 1555 2.42
LINK CA CA A 401 O HOH A 717 1555 1555 2.35
LINK CA CA A 401 O ASP B 69 1555 1555 2.35
LINK CA CA A 401 OD1 ASP B 69 1555 1555 2.41
LINK CA CA A 401 O HOH B 738 1555 1555 2.38
LINK CA CA A 402 O HOH A 639 1555 1555 2.45
LINK CA CA A 402 O HOH A 736 1555 1555 2.32
LINK CA CA A 402 OD1 ASP B 69 1555 1555 2.41
LINK CA CA A 402 OD2 ASP B 69 1555 1555 2.63
LINK CA CA A 402 O HOH B 692 1555 1555 2.29
LINK CA CA A 403 O7 NAG A 405 1555 1555 2.31
LINK CA CA A 403 O HOH A 620 1555 1555 2.22
LINK CA CA A 403 O HOH A 628 1555 1565 2.21
LINK CA CA A 403 O HOH A 734 1555 1555 2.44
LINK CA CA A 403 O HOH A 747 1555 1565 2.21
CISPEP 1 ILE A 48 PRO A 49 0 3.08
CISPEP 2 TRP A 300 ALA A 301 0 3.67
CISPEP 3 PRO A 315 PRO A 316 0 3.15
CISPEP 4 ILE B 48 PRO B 49 0 -1.56
CISPEP 5 TRP B 300 ALA B 301 0 0.94
CISPEP 6 PRO B 315 PRO B 316 0 5.72
CRYST1 161.273 50.822 75.310 90.00 95.08 90.00 C 1 2 1 8
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 0.006201 0.000000 0.000552 0.00000
SCALE2 0.000000 0.019677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
