HEADER LYASE 13-APR-15 4ZAA
TITLE STRUCTURE OF A. NIGER FDC1 IN COMPLEX WITH 4-VINYL GUAIACOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FDC1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.1.1.61;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 GENE: AN03G06590;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS (DE)CARBOXYLASE, PRENYLATED FLAVIN BINDING, UBID-TYPE ENZYME, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.P.PAYNE,D.LEYS
REVDAT 3 08-JUN-16 4ZAA 1
REVDAT 2 01-JUL-15 4ZAA 1 JRNL
REVDAT 1 17-JUN-15 4ZAA 0
JRNL AUTH K.A.PAYNE,M.D.WHITE,K.FISHER,B.KHARA,S.S.BAILEY,D.PARKER,
JRNL AUTH 2 N.J.RATTRAY,D.K.TRIVEDI,R.GOODACRE,R.BEVERIDGE,P.BARRAN,
JRNL AUTH 3 S.E.RIGBY,N.S.SCRUTTON,S.HAY,D.LEYS
JRNL TITL NEW COFACTOR SUPPORTS ALPHA , BETA-UNSATURATED ACID
JRNL TITL 2 DECARBOXYLATION VIA 1,3-DIPOLAR CYCLOADDITION.
JRNL REF NATURE V. 522 502 2015
JRNL REFN ESSN 1476-4687
JRNL PMID 26083754
JRNL DOI 10.1038/NATURE14560
REMARK 2
REMARK 2 RESOLUTION. 1.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 94.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 146799
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.163
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7752
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) : 1.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10440
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 516
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3815
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 467
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.20000
REMARK 3 B22 (A**2) : -2.48000
REMARK 3 B33 (A**2) : 1.28000
REMARK 3 B12 (A**2) : 0.00000
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): 0.038
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.026
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.327
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4326 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2878 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5944 ; 2.304 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7061 ; 4.401 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 563 ; 6.464 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;33.954 ;24.104
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 698 ;12.154 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;20.558 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 642 ; 0.171 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4956 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 851 ; 0.022 ; 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): 2691 ; 2.374 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1071 ; 7.956 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4390 ; 3.164 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1635 ; 4.859 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1554 ; 6.487 ; 4.500
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): 7204 ; 5.277 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ZAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208926.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146799
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.242
REMARK 200 RESOLUTION RANGE LOW (A) : 94.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, BIS-TRIS
REMARK 280 PROPANE 6.5, 20 % W/V PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 48.29600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.23350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.29600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.23350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 946 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 ASN A 500
REMARK 465 LEU A 501
REMARK 465 GLU A 502
REMARK 465 HIS A 503
REMARK 465 HIS A 504
REMARK 465 HIS A 505
REMARK 465 HIS A 506
REMARK 465 HIS A 507
REMARK 465 HIS A 508
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 60 CG CD CE NZ
REMARK 470 LYS A 75 CD CE NZ
REMARK 470 ASP A 129 OD1 OD2
REMARK 470 LYS A 179 CE NZ
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 293 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 412 CE NZ
REMARK 470 ARG A 470 CZ NH1 NH2
REMARK 470 LYS A 495 CG CD CE NZ
REMARK 470 SER A 499 CB OG
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 715 O HOH A 856 1.47
REMARK 500 O HOH A 1000 O HOH A 1044 1.85
REMARK 500 O HOH A 969 O HOH A 1045 1.89
REMARK 500 O HOH A 859 O HOH A 1096 1.93
REMARK 500 O HOH A 1041 O HOH A 1046 2.00
REMARK 500 CE2 TYR A 394 O1 4M4 A 606 2.11
REMARK 500 O HOH A 832 O HOH A 1102 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 C5 4M4 A 607 O HOH A 1162 3545 0.25
REMARK 500 C6 4M4 A 607 O HOH A 1162 3545 1.15
REMARK 500 C4 4M4 A 607 O HOH A 1162 3545 1.55
REMARK 500 O HOH A 1067 O HOH A 1154 2555 1.94
REMARK 500 C9 4M4 A 607 O HOH A 1162 3545 2.10
REMARK 500 O HOH A 1016 O HOH A 1145 2655 2.15
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 15 CG GLU A 15 CD 0.099
REMARK 500 LYS A 18 CD LYS A 18 CE 0.175
REMARK 500 LYS A 18 CE LYS A 18 NZ 0.196
REMARK 500 ARG A 65 NE ARG A 65 CZ 0.092
REMARK 500 ARG A 65 CZ ARG A 65 NH1 -0.090
REMARK 500 ARG A 370 CZ ARG A 370 NH2 0.089
REMARK 500 TYR A 394 CG TYR A 394 CD1 -0.105
REMARK 500 TYR A 394 CD1 TYR A 394 CE1 0.121
REMARK 500 GLU A 410 CD GLU A 410 OE1 0.066
REMARK 500 GLU A 473 CD GLU A 473 OE1 0.095
REMARK 500 LYS A 486 CD LYS A 486 CE -0.180
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 65 NH1 - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 83 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 97 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 MET A 221 CG - SD - CE ANGL. DEV. = -17.7 DEGREES
REMARK 500 ASP A 291 C - N - CA ANGL. DEV. = -15.3 DEGREES
REMARK 500 ASP A 291 CB - CG - OD1 ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG A 302 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 336 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 363 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 370 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 380 CG - CD - NE ANGL. DEV. = 16.0 DEGREES
REMARK 500 ASP A 404 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 435 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 435 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 452 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 484 CB - CG - OD1 ANGL. DEV. = 7.0 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 LEU A 34 -35.21 71.96
REMARK 500 MET A 59 131.68 -39.35
REMARK 500 LYS A 60 -163.30 -167.88
REMARK 500 ASN A 61 22.87 13.37
REMARK 500 TYR A 154 20.03 -154.05
REMARK 500 MET A 443 -80.00 -93.04
REMARK 500 THR A 467 -82.90 -121.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASP A 291 0.12 SIDE CHAIN
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 A1166 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A1167 DISTANCE = 7.13 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 MN A 603 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 168 OD1
REMARK 620 2 HIS A 191 ND1 91.2
REMARK 620 3 GLU A 233 OE2 96.0 172.3
REMARK 620 4 4LU A 601 O2P 95.1 88.5 93.5
REMARK 620 5 HOH A 724 O 176.3 85.7 87.2 82.8
REMARK 620 6 HOH A 816 O 91.6 85.2 91.9 170.9 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 604 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 169 O
REMARK 620 2 ALA A 222 O 96.9
REMARK 620 3 SER A 223 O 74.4 75.0
REMARK 620 4 MET A 225 O 170.4 73.7 100.9
REMARK 620 5 GLU A 233 OE2 69.7 106.4 144.0 114.2
REMARK 620 6 4LU A 601 O5' 94.5 136.2 67.7 91.3 117.2
REMARK 620 7 4LU A 601 O2P 80.0 174.3 108.5 109.5 68.1 49.2
REMARK 620 8 HOH A 724 O 121.4 122.5 150.6 66.6 59.2 85.4 56.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 605 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 421 O
REMARK 620 2 ASP A 427 OD2 85.5
REMARK 620 3 ASP A 459 O 86.7 98.0
REMARK 620 4 LEU A 461 O 103.9 160.8 99.2
REMARK 620 5 HOH A1077 O 73.8 78.3 160.3 88.2
REMARK 620 6 HOH A 999 O 144.7 110.2 120.3 53.1 78.7
REMARK 620 7 HOH A1014 O 164.9 81.8 86.9 90.7 111.4 49.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4LU A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FZZ A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4M4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4M4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO2 A 608
DBREF 4ZAA A 1 500 UNP A2QHE5 A2QHE5_ASPNC 1 500
SEQADV 4ZAA LEU A 501 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA GLU A 502 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA HIS A 503 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA HIS A 504 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA HIS A 505 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA HIS A 506 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA HIS A 507 UNP A2QHE5 EXPRESSION TAG
SEQADV 4ZAA HIS A 508 UNP A2QHE5 EXPRESSION TAG
SEQRES 1 A 508 MET SER ALA GLN PRO ALA HIS LEU CYS PHE ARG SER PHE
SEQRES 2 A 508 VAL GLU ALA LEU LYS VAL ASP ASN ASP LEU VAL GLU ILE
SEQRES 3 A 508 ASN THR PRO ILE ASP PRO ASN LEU GLU ALA ALA ALA ILE
SEQRES 4 A 508 THR ARG ARG VAL CYS GLU THR ASN ASP LYS ALA PRO LEU
SEQRES 5 A 508 PHE ASN ASN LEU ILE GLY MET LYS ASN GLY LEU PHE ARG
SEQRES 6 A 508 ILE LEU GLY ALA PRO GLY SER LEU ARG LYS SER SER ALA
SEQRES 7 A 508 ASP ARG TYR GLY ARG LEU ALA ARG HIS LEU ALA LEU PRO
SEQRES 8 A 508 PRO THR ALA SER MET ARG GLU ILE LEU ASP LYS MET LEU
SEQRES 9 A 508 SER ALA SER ASP MET PRO PRO ILE PRO PRO THR ILE VAL
SEQRES 10 A 508 PRO THR GLY PRO CYS LYS GLU ASN SER LEU ASP ASP SER
SEQRES 11 A 508 GLU PHE ASP LEU THR GLU LEU PRO VAL PRO LEU ILE HIS
SEQRES 12 A 508 LYS SER ASP GLY GLY LYS TYR ILE GLN THR TYR GLY MET
SEQRES 13 A 508 HIS ILE VAL GLN SER PRO ASP GLY THR TRP THR ASN TRP
SEQRES 14 A 508 SER ILE ALA ARG ALA MET VAL HIS ASP LYS ASN HIS LEU
SEQRES 15 A 508 THR GLY LEU VAL ILE PRO PRO GLN HIS ILE TRP GLN ILE
SEQRES 16 A 508 HIS GLN MET TRP LYS LYS GLU GLY ARG SER ASP VAL PRO
SEQRES 17 A 508 TRP ALA LEU ALA PHE GLY VAL PRO PRO ALA ALA ILE MET
SEQRES 18 A 508 ALA SER SER MET PRO ILE PRO ASP GLY VAL THR GLU ALA
SEQRES 19 A 508 GLY TYR VAL GLY ALA MET THR GLY SER SER LEU GLU LEU
SEQRES 20 A 508 VAL LYS CYS ASP THR ASN ASP LEU TYR VAL PRO ALA THR
SEQRES 21 A 508 SER GLU ILE VAL LEU GLU GLY THR LEU SER ILE SER GLU
SEQRES 22 A 508 THR GLY PRO GLU GLY PRO PHE GLY GLU MET HIS GLY TYR
SEQRES 23 A 508 ILE PHE PRO GLY ASP THR HIS LEU GLY ALA LYS TYR LYS
SEQRES 24 A 508 VAL ASN ARG ILE THR TYR ARG ASN ASN ALA ILE MET PRO
SEQRES 25 A 508 MET SER SER CYS GLY ARG LEU THR ASP GLU THR HIS THR
SEQRES 26 A 508 MET ILE GLY SER LEU ALA ALA ALA GLU ILE ARG LYS LEU
SEQRES 27 A 508 CYS GLN GLN ASN ASP LEU PRO ILE THR ASP ALA PHE ALA
SEQRES 28 A 508 PRO PHE GLU SER GLN VAL THR TRP VAL ALA LEU ARG VAL
SEQRES 29 A 508 ASP THR GLU LYS LEU ARG ALA MET LYS THR THR SER GLU
SEQRES 30 A 508 GLY PHE ARG LYS ARG VAL GLY ASP VAL VAL PHE ASN HIS
SEQRES 31 A 508 LYS ALA GLY TYR THR ILE HIS ARG LEU VAL LEU VAL GLY
SEQRES 32 A 508 ASP ASP ILE ASP VAL TYR GLU GLY LYS ASP VAL LEU TRP
SEQRES 33 A 508 ALA PHE SER THR ARG CYS ARG PRO GLY MET ASP GLU THR
SEQRES 34 A 508 LEU PHE GLU ASP VAL ARG GLY PHE PRO LEU ILE PRO TYR
SEQRES 35 A 508 MET GLY HIS GLY ASN GLY PRO ALA HIS ARG GLY GLY LYS
SEQRES 36 A 508 VAL VAL SER ASP ALA LEU MET PRO THR GLU TYR THR THR
SEQRES 37 A 508 GLY ARG ASN TRP GLU ALA ALA ASP PHE ASN GLN SER TYR
SEQRES 38 A 508 PRO GLU ASP LEU LYS GLN LYS VAL LEU ASP ASN TRP THR
SEQRES 39 A 508 LYS MET GLY PHE SER ASN LEU GLU HIS HIS HIS HIS HIS
SEQRES 40 A 508 HIS
HET 4LU A 601 36
HET FZZ A 602 36
HET MN A 603 1
HET K A 604 1
HET K A 605 1
HET 4M4 A 606 11
HET 4M4 A 607 11
HET CO2 A 608 3
HETNAM 4LU 1-DEOXY-5-O-PHOSPHONO-1-(3,3,4,5-TETRAMETHYL-9,11-
HETNAM 2 4LU DIOXO-2,3,8,9,10,11-HEXAHYDRO-7H-QUINOLINO[1,8-
HETNAM 3 4LU FG]PTERIDIN-12-IUM-7-YL)-D-RIBITOL
HETNAM FZZ 1-DEOXY-5-O-PHOSPHONO-1-[(10AR)-2,2,3,4-TETRAMETHYL-8,
HETNAM 2 FZZ 10-DIOXO-1,2,8,9,10,10A-HEXAHYDRO-6H-INDENO[1,7-
HETNAM 3 FZZ EF]PYRIMIDO[4,5-B][1,4]DIAZEPIN-6-YL]-D-RIBITOL
HETNAM MN MANGANESE (II) ION
HETNAM K POTASSIUM ION
HETNAM 4M4 2-METHOXY-4-VINYLPHENOL
HETNAM CO2 CARBON DIOXIDE
HETSYN 4LU PRENYLATED-FMN IMINIUM FORM
HETSYN 4M4 4-VINYL GUAIACOL
FORMUL 2 4LU C22 H30 N4 O9 P 1+
FORMUL 3 FZZ C22 H29 N4 O9 P
FORMUL 4 MN MN 2+
FORMUL 5 K 2(K 1+)
FORMUL 7 4M4 2(C9 H10 O2)
FORMUL 9 CO2 C O2
FORMUL 10 HOH *467(H2 O)
HELIX 1 AA1 PRO A 5 LEU A 8 5 4
HELIX 2 AA2 CYS A 9 ASP A 20 1 12
HELIX 3 AA3 LEU A 34 ASN A 47 1 14
HELIX 4 AA4 TYR A 81 ARG A 86 1 6
HELIX 5 AA5 SER A 95 ALA A 106 1 12
HELIX 6 AA6 SER A 107 MET A 109 5 3
HELIX 7 AA7 GLY A 120 GLU A 124 5 5
HELIX 8 AA8 GLN A 190 GLY A 203 1 14
HELIX 9 AA9 PRO A 216 SER A 224 1 9
HELIX 10 AB1 THR A 232 GLY A 242 1 11
HELIX 11 AB2 ASP A 321 MET A 326 1 6
HELIX 12 AB3 MET A 326 ASN A 342 1 17
HELIX 13 AB4 PRO A 352 GLN A 356 5 5
HELIX 14 AB5 ASP A 365 LYS A 373 1 9
HELIX 15 AB6 THR A 375 ASN A 389 1 15
HELIX 16 AB7 HIS A 390 TYR A 394 5 5
HELIX 17 AB8 GLU A 410 CYS A 422 1 13
HELIX 18 AB9 ILE A 440 HIS A 445 1 6
HELIX 19 AC1 MET A 462 THR A 467 5 6
HELIX 20 AC2 ASP A 476 TYR A 481 1 6
HELIX 21 AC3 PRO A 482 GLY A 497 1 16
SHEET 1 AA1 4 LEU A 23 ILE A 26 0
SHEET 2 AA1 4 ALA A 50 PHE A 53 1 O LEU A 52 N ILE A 26
SHEET 3 AA1 4 ARG A 65 GLY A 68 -1 O ILE A 66 N PHE A 53
SHEET 4 AA1 4 ILE A 310 MET A 313 1 O MET A 311 N ARG A 65
SHEET 1 AA2 3 THR A 115 ILE A 116 0
SHEET 2 AA2 3 GLU A 246 LYS A 249 1 O LEU A 247 N THR A 115
SHEET 3 AA2 3 TYR A 256 PRO A 258 -1 O VAL A 257 N VAL A 248
SHEET 1 AA3 6 ASN A 125 ASP A 128 0
SHEET 2 AA3 6 HIS A 293 TYR A 305 -1 O ILE A 303 N LEU A 127
SHEET 3 AA3 6 ILE A 263 GLU A 277 -1 N GLY A 275 O GLY A 295
SHEET 4 AA3 6 VAL A 207 PHE A 213 -1 N PHE A 213 O ILE A 263
SHEET 5 AA3 6 MET A 156 GLN A 160 -1 N MET A 156 O ALA A 212
SHEET 6 AA3 6 THR A 167 SER A 170 -1 O SER A 170 N HIS A 157
SHEET 1 AA4 4 ASN A 125 ASP A 128 0
SHEET 2 AA4 4 HIS A 293 TYR A 305 -1 O ILE A 303 N LEU A 127
SHEET 3 AA4 4 HIS A 181 GLY A 184 -1 N LEU A 182 O TYR A 298
SHEET 4 AA4 4 ALA A 174 ASP A 178 -1 N MET A 175 O THR A 183
SHEET 1 AA5 5 ILE A 346 PHE A 350 0
SHEET 2 AA5 5 TRP A 359 VAL A 364 -1 O ALA A 361 N PHE A 350
SHEET 3 AA5 5 ARG A 398 VAL A 402 1 O VAL A 400 N LEU A 362
SHEET 4 AA5 5 LYS A 455 ASP A 459 1 O SER A 458 N LEU A 399
SHEET 5 AA5 5 GLU A 428 PHE A 431 -1 N PHE A 431 O LYS A 455
LINK OD1 ASN A 168 MN MN A 603 1555 1555 2.17
LINK O TRP A 169 K K A 604 1555 1555 3.13
LINK ND1 HIS A 191 MN MN A 603 1555 1555 2.29
LINK O ALA A 222 K K A 604 1555 1555 2.84
LINK O SER A 223 K K A 604 1555 1555 3.13
LINK O MET A 225 K K A 604 1555 1555 2.79
LINK OE2 GLU A 233 MN MN A 603 1555 1555 2.14
LINK OE2 GLU A 233 K K A 604 1555 1555 2.78
LINK O ARG A 421 K K A 605 1555 1555 2.65
LINK OD2 ASP A 427 K K A 605 1555 1555 2.81
LINK O ASP A 459 K K A 605 1555 1555 2.69
LINK O LEU A 461 K K A 605 1555 1555 2.66
LINK O5'A4LU A 601 K K A 604 1555 1555 2.98
LINK O2PA4LU A 601 MN MN A 603 1555 1555 2.20
LINK O2PA4LU A 601 K K A 604 1555 1555 2.87
LINK MN MN A 603 O HOH A 724 1555 1555 2.22
LINK MN MN A 603 O HOH A 816 1555 1555 2.24
LINK K K A 604 O HOH A 724 1555 1555 3.26
LINK K K A 605 O HOH A1077 1555 2555 2.80
LINK K K A 605 O HOH A 999 1555 2555 3.44
LINK K K A 605 O HOH A1014 1555 2555 2.74
CISPEP 1 LEU A 63 PHE A 64 0 -3.73
CISPEP 2 PRO A 188 PRO A 189 0 2.85
CISPEP 3 GLY A 278 PRO A 279 0 2.52
CISPEP 4 LEU A 319 THR A 320 0 0.86
SITE 1 AC1 26 THR A 153 ASN A 168 SER A 170 ILE A 171
SITE 2 AC1 26 ALA A 172 ARG A 173 LEU A 185 GLN A 190
SITE 3 AC1 26 HIS A 191 SER A 223 SER A 224 MET A 225
SITE 4 AC1 26 PRO A 226 GLU A 233 ILE A 327 LYS A 391
SITE 5 AC1 26 FZZ A 602 MN A 603 K A 604 4M4 A 606
SITE 6 AC1 26 CO2 A 608 HOH A 724 HOH A 726 HOH A 742
SITE 7 AC1 26 HOH A 746 HOH A 747
SITE 1 AC2 27 THR A 153 ASN A 168 SER A 170 ILE A 171
SITE 2 AC2 27 ALA A 172 ARG A 173 LEU A 185 GLN A 190
SITE 3 AC2 27 HIS A 191 SER A 223 SER A 224 MET A 225
SITE 4 AC2 27 PRO A 226 GLU A 233 THR A 323 ILE A 327
SITE 5 AC2 27 LYS A 391 4LU A 601 MN A 603 K A 604
SITE 6 AC2 27 4M4 A 606 CO2 A 608 HOH A 724 HOH A 726
SITE 7 AC2 27 HOH A 740 HOH A 742 HOH A 746
SITE 1 AC3 8 ASN A 168 HIS A 191 GLU A 233 4LU A 601
SITE 2 AC3 8 FZZ A 602 K A 604 HOH A 724 HOH A 816
SITE 1 AC4 8 TRP A 169 ALA A 222 SER A 223 MET A 225
SITE 2 AC4 8 GLU A 233 4LU A 601 FZZ A 602 MN A 603
SITE 1 AC5 6 ARG A 421 ASP A 427 ASP A 459 LEU A 461
SITE 2 AC5 6 HOH A1014 HOH A1077
SITE 1 AC6 10 LEU A 185 ILE A 187 GLN A 190 TYR A 394
SITE 2 AC6 10 THR A 395 PHE A 437 LEU A 439 4LU A 601
SITE 3 AC6 10 FZZ A 602 HOH A1055
SITE 1 AC7 10 ALA A 6 GLU A 15 ALA A 16 VAL A 19
SITE 2 AC7 10 ASP A 20 PRO A 29 ARG A 86 HOH A 820
SITE 3 AC7 10 HOH A1027 HOH A1162
SITE 1 AC8 5 ARG A 173 MET A 283 LEU A 439 4LU A 601
SITE 2 AC8 5 FZZ A 602
CRYST1 96.592 64.467 87.885 90.00 90.00 90.00 P 21 21 2 4
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 0.010353 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015512 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011379 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
