HEADER TRANSFERASE, HYDROLASE 08-JUL-07 2QJO
TITLE CRYSTAL STRUCTURE OF A BIFUNCTIONAL NMN ADENYLYLTRANSFERASE/ADP RIBOSE
TITLE 2 PYROPHOSPHATASE (NADM) COMPLEXED WITH ADPRP AND NAD FROM
TITLE 3 SYNECHOCYSTIS SP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL NMN ADENYLYLTRANSFERASE/NUDIX HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: NICOTINAMIDE-NUCLEOTIDE ADENYLYLTRANSFERASE, NAD(+)
COMPND 5 PYROPHOSPHORYLASE, NAD(+) DIPHOSPHORYLASE, ADP COMPOUNDS HYDROLASE.;
COMPND 6 EC: 2.7.7.1, 3.6.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
SOURCE 5 GENE: SLR0787;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX
KEYWDS TWO INDIVIDUAL DOMAINS, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.HUANG,L.SORCI,X.ZHANG,C.BRAUTIGAN,N.RAFFAELLI,G.MAGNI,N.V.GRISHIN,
AUTHOR 2 A.OSTERMAN,H.ZHANG
REVDAT 5 21-FEB-24 2QJO 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2QJO 1 REMARK
REVDAT 3 13-JUL-11 2QJO 1 VERSN
REVDAT 2 24-FEB-09 2QJO 1 VERSN
REVDAT 1 11-MAR-08 2QJO 0
JRNL AUTH N.HUANG,L.SORCI,X.ZHANG,C.A.BRAUTIGAM,X.LI,N.RAFFAELLI,
JRNL AUTH 2 G.MAGNI,N.V.GRISHIN,A.L.OSTERMAN,H.ZHANG
JRNL TITL BIFUNCTIONAL NMN ADENYLYLTRANSFERASE/ADP-RIBOSE
JRNL TITL 2 PYROPHOSPHATASE: STRUCTURE AND FUNCTION IN BACTERIAL NAD
JRNL TITL 3 METABOLISM.
JRNL REF STRUCTURE V. 16 196 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18275811
JRNL DOI 10.1016/J.STR.2007.11.017
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 66426
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3549
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4935
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE SET COUNT : 248
REMARK 3 BIN FREE R VALUE : 0.3970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8022
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 287
REMARK 3 SOLVENT ATOMS : 313
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : -0.01000
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): 0.269
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8570 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11701 ; 1.571 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 996 ; 8.649 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 395 ;37.590 ;23.266
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1362 ;17.696 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;22.699 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1259 ; 0.162 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6456 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3801 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5753 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 459 ; 0.156 ; 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): 51 ; 0.156 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.331 ; 0.200
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): 4975 ; 0.823 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8028 ; 1.551 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3595 ; 2.019 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3672 ; 3.256 ; 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): 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 : 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: NULL
REMARK 4
REMARK 4 2QJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97874, 0.97891, 0.984
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70016
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS, 1.5 M LI2SO4, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 65.79667
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 32.89833
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 32.89833
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 65.79667
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE
REMARK 300 TRIMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: X-Y,-Y,-Z+1/3
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 29290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 82890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -246.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 32.89833
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 B 705 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 GLY A 302
REMARK 465 GLY A 303
REMARK 465 ASP A 304
REMARK 465 ASP A 305
REMARK 465 ALA A 306
REMARK 465 GLN A 307
REMARK 465 SER A 337
REMARK 465 LYS A 338
REMARK 465 VAL A 339
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 ASP C -1
REMARK 465 PRO C 0
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 THR C 3
REMARK 465 LYS C 301
REMARK 465 GLY C 302
REMARK 465 GLY C 303
REMARK 465 ASP C 304
REMARK 465 ASP C 305
REMARK 465 ALA C 306
REMARK 465 GLN C 307
REMARK 465 LYS C 338
REMARK 465 VAL C 339
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 C 727 O HOH C 736 2.01
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 813 O HOH B 774 2564 1.95
REMARK 500 O HOH B 757 O HOH B 838 5555 2.13
REMARK 500 O HOH B 714 O HOH B 805 5555 2.14
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 72 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 GLY B 281 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 ARG C 280 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 280 NE - CZ - NH2 ANGL. DEV. = -3.3 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 PHE A 14 71.62 50.12
REMARK 500 PHE A 123 62.44 -115.67
REMARK 500 ALA A 191 -18.48 -47.07
REMARK 500 GLU A 321 -49.26 -27.80
REMARK 500 GLU A 326 -125.45 47.27
REMARK 500 ASP B 114 -169.26 -162.18
REMARK 500 ASP B 136 6.72 85.24
REMARK 500 ASP B 304 -63.13 -141.70
REMARK 500 ASP B 305 -56.48 176.63
REMARK 500 GLU B 326 -125.36 40.04
REMARK 500 ARG C 53 155.75 -42.71
REMARK 500 LEU C 70 -19.19 -43.03
REMARK 500 ARG C 112 98.15 -64.73
REMARK 500 ASP C 114 -142.17 -146.23
REMARK 500 THR C 131 -142.83 -100.10
REMARK 500 ALA C 211 53.56 35.99
REMARK 500 ARG C 282 103.39 -56.36
REMARK 500 GLU C 326 -123.96 42.06
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 PRO A 135 ASP A 136 -43.13
REMARK 500 ARG B 280 GLY B 281 -101.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APR A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APR B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APR C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP C 703
DBREF 2QJO A 1 339 UNP Q55928 NADM_SYNY3 1 339
DBREF 2QJO B 1 339 UNP Q55928 NADM_SYNY3 1 339
DBREF 2QJO C 1 339 UNP Q55928 NADM_SYNY3 1 339
SEQADV 2QJO ASP A -1 UNP Q55928 CLONING ARTIFACT
SEQADV 2QJO PRO A 0 UNP Q55928 CLONING ARTIFACT
SEQADV 2QJO ASP B -1 UNP Q55928 CLONING ARTIFACT
SEQADV 2QJO PRO B 0 UNP Q55928 CLONING ARTIFACT
SEQADV 2QJO ASP C -1 UNP Q55928 CLONING ARTIFACT
SEQADV 2QJO PRO C 0 UNP Q55928 CLONING ARTIFACT
SEQRES 1 A 341 ASP PRO MET GLN THR LYS TYR GLN TYR GLY ILE TYR ILE
SEQRES 2 A 341 GLY ARG PHE GLN PRO PHE HIS LEU GLY HIS LEU ARG THR
SEQRES 3 A 341 LEU ASN LEU ALA LEU GLU LYS ALA GLU GLN VAL ILE ILE
SEQRES 4 A 341 ILE LEU GLY SER HIS ARG VAL ALA ALA ASP THR ARG ASN
SEQRES 5 A 341 PRO TRP ARG SER PRO GLU ARG MET ALA MET ILE GLU ALA
SEQRES 6 A 341 CYS LEU SER PRO GLN ILE LEU LYS ARG VAL HIS PHE LEU
SEQRES 7 A 341 THR VAL ARG ASP TRP LEU TYR SER ASP ASN LEU TRP LEU
SEQRES 8 A 341 ALA ALA VAL GLN GLN GLN VAL LEU LYS ILE THR GLY GLY
SEQRES 9 A 341 SER ASN SER VAL VAL VAL LEU GLY HIS ARG LYS ASP ALA
SEQRES 10 A 341 SER SER TYR TYR LEU ASN LEU PHE PRO GLN TRP ASP TYR
SEQRES 11 A 341 LEU GLU THR GLY HIS TYR PRO ASP PHE SER SER THR ALA
SEQRES 12 A 341 ILE ARG GLY ALA TYR PHE GLU GLY LYS GLU GLY ASP TYR
SEQRES 13 A 341 LEU ASP LYS VAL PRO PRO ALA ILE ALA ASP TYR LEU GLN
SEQRES 14 A 341 THR PHE GLN LYS SER GLU ARG TYR ILE ALA LEU CYS ASP
SEQRES 15 A 341 GLU TYR GLN PHE LEU GLN ALA TYR LYS GLN ALA TRP ALA
SEQRES 16 A 341 THR ALA PRO TYR ALA PRO THR PHE ILE THR THR ASP ALA
SEQRES 17 A 341 VAL VAL VAL GLN ALA GLY HIS VAL LEU MET VAL ARG ARG
SEQRES 18 A 341 GLN ALA LYS PRO GLY LEU GLY LEU ILE ALA LEU PRO GLY
SEQRES 19 A 341 GLY PHE ILE LYS GLN ASN GLU THR LEU VAL GLU GLY MET
SEQRES 20 A 341 LEU ARG GLU LEU LYS GLU GLU THR ARG LEU LYS VAL PRO
SEQRES 21 A 341 LEU PRO VAL LEU ARG GLY SER ILE VAL ASP SER HIS VAL
SEQRES 22 A 341 PHE ASP ALA PRO GLY ARG SER LEU ARG GLY ARG THR ILE
SEQRES 23 A 341 THR HIS ALA TYR PHE ILE GLN LEU PRO GLY GLY GLU LEU
SEQRES 24 A 341 PRO ALA VAL LYS GLY GLY ASP ASP ALA GLN LYS ALA TRP
SEQRES 25 A 341 TRP MET SER LEU ALA ASP LEU TYR ALA GLN GLU GLU GLN
SEQRES 26 A 341 ILE TYR GLU ASP HIS PHE GLN ILE ILE GLN HIS PHE VAL
SEQRES 27 A 341 SER LYS VAL
SEQRES 1 B 341 ASP PRO MET GLN THR LYS TYR GLN TYR GLY ILE TYR ILE
SEQRES 2 B 341 GLY ARG PHE GLN PRO PHE HIS LEU GLY HIS LEU ARG THR
SEQRES 3 B 341 LEU ASN LEU ALA LEU GLU LYS ALA GLU GLN VAL ILE ILE
SEQRES 4 B 341 ILE LEU GLY SER HIS ARG VAL ALA ALA ASP THR ARG ASN
SEQRES 5 B 341 PRO TRP ARG SER PRO GLU ARG MET ALA MET ILE GLU ALA
SEQRES 6 B 341 CYS LEU SER PRO GLN ILE LEU LYS ARG VAL HIS PHE LEU
SEQRES 7 B 341 THR VAL ARG ASP TRP LEU TYR SER ASP ASN LEU TRP LEU
SEQRES 8 B 341 ALA ALA VAL GLN GLN GLN VAL LEU LYS ILE THR GLY GLY
SEQRES 9 B 341 SER ASN SER VAL VAL VAL LEU GLY HIS ARG LYS ASP ALA
SEQRES 10 B 341 SER SER TYR TYR LEU ASN LEU PHE PRO GLN TRP ASP TYR
SEQRES 11 B 341 LEU GLU THR GLY HIS TYR PRO ASP PHE SER SER THR ALA
SEQRES 12 B 341 ILE ARG GLY ALA TYR PHE GLU GLY LYS GLU GLY ASP TYR
SEQRES 13 B 341 LEU ASP LYS VAL PRO PRO ALA ILE ALA ASP TYR LEU GLN
SEQRES 14 B 341 THR PHE GLN LYS SER GLU ARG TYR ILE ALA LEU CYS ASP
SEQRES 15 B 341 GLU TYR GLN PHE LEU GLN ALA TYR LYS GLN ALA TRP ALA
SEQRES 16 B 341 THR ALA PRO TYR ALA PRO THR PHE ILE THR THR ASP ALA
SEQRES 17 B 341 VAL VAL VAL GLN ALA GLY HIS VAL LEU MET VAL ARG ARG
SEQRES 18 B 341 GLN ALA LYS PRO GLY LEU GLY LEU ILE ALA LEU PRO GLY
SEQRES 19 B 341 GLY PHE ILE LYS GLN ASN GLU THR LEU VAL GLU GLY MET
SEQRES 20 B 341 LEU ARG GLU LEU LYS GLU GLU THR ARG LEU LYS VAL PRO
SEQRES 21 B 341 LEU PRO VAL LEU ARG GLY SER ILE VAL ASP SER HIS VAL
SEQRES 22 B 341 PHE ASP ALA PRO GLY ARG SER LEU ARG GLY ARG THR ILE
SEQRES 23 B 341 THR HIS ALA TYR PHE ILE GLN LEU PRO GLY GLY GLU LEU
SEQRES 24 B 341 PRO ALA VAL LYS GLY GLY ASP ASP ALA GLN LYS ALA TRP
SEQRES 25 B 341 TRP MET SER LEU ALA ASP LEU TYR ALA GLN GLU GLU GLN
SEQRES 26 B 341 ILE TYR GLU ASP HIS PHE GLN ILE ILE GLN HIS PHE VAL
SEQRES 27 B 341 SER LYS VAL
SEQRES 1 C 341 ASP PRO MET GLN THR LYS TYR GLN TYR GLY ILE TYR ILE
SEQRES 2 C 341 GLY ARG PHE GLN PRO PHE HIS LEU GLY HIS LEU ARG THR
SEQRES 3 C 341 LEU ASN LEU ALA LEU GLU LYS ALA GLU GLN VAL ILE ILE
SEQRES 4 C 341 ILE LEU GLY SER HIS ARG VAL ALA ALA ASP THR ARG ASN
SEQRES 5 C 341 PRO TRP ARG SER PRO GLU ARG MET ALA MET ILE GLU ALA
SEQRES 6 C 341 CYS LEU SER PRO GLN ILE LEU LYS ARG VAL HIS PHE LEU
SEQRES 7 C 341 THR VAL ARG ASP TRP LEU TYR SER ASP ASN LEU TRP LEU
SEQRES 8 C 341 ALA ALA VAL GLN GLN GLN VAL LEU LYS ILE THR GLY GLY
SEQRES 9 C 341 SER ASN SER VAL VAL VAL LEU GLY HIS ARG LYS ASP ALA
SEQRES 10 C 341 SER SER TYR TYR LEU ASN LEU PHE PRO GLN TRP ASP TYR
SEQRES 11 C 341 LEU GLU THR GLY HIS TYR PRO ASP PHE SER SER THR ALA
SEQRES 12 C 341 ILE ARG GLY ALA TYR PHE GLU GLY LYS GLU GLY ASP TYR
SEQRES 13 C 341 LEU ASP LYS VAL PRO PRO ALA ILE ALA ASP TYR LEU GLN
SEQRES 14 C 341 THR PHE GLN LYS SER GLU ARG TYR ILE ALA LEU CYS ASP
SEQRES 15 C 341 GLU TYR GLN PHE LEU GLN ALA TYR LYS GLN ALA TRP ALA
SEQRES 16 C 341 THR ALA PRO TYR ALA PRO THR PHE ILE THR THR ASP ALA
SEQRES 17 C 341 VAL VAL VAL GLN ALA GLY HIS VAL LEU MET VAL ARG ARG
SEQRES 18 C 341 GLN ALA LYS PRO GLY LEU GLY LEU ILE ALA LEU PRO GLY
SEQRES 19 C 341 GLY PHE ILE LYS GLN ASN GLU THR LEU VAL GLU GLY MET
SEQRES 20 C 341 LEU ARG GLU LEU LYS GLU GLU THR ARG LEU LYS VAL PRO
SEQRES 21 C 341 LEU PRO VAL LEU ARG GLY SER ILE VAL ASP SER HIS VAL
SEQRES 22 C 341 PHE ASP ALA PRO GLY ARG SER LEU ARG GLY ARG THR ILE
SEQRES 23 C 341 THR HIS ALA TYR PHE ILE GLN LEU PRO GLY GLY GLU LEU
SEQRES 24 C 341 PRO ALA VAL LYS GLY GLY ASP ASP ALA GLN LYS ALA TRP
SEQRES 25 C 341 TRP MET SER LEU ALA ASP LEU TYR ALA GLN GLU GLU GLN
SEQRES 26 C 341 ILE TYR GLU ASP HIS PHE GLN ILE ILE GLN HIS PHE VAL
SEQRES 27 C 341 SER LYS VAL
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET APR A 501 36
HET NAD A 601 44
HET POP A 701 9
HET SO4 B 401 5
HET APR B 502 36
HET NAD B 602 44
HET POP B 702 9
HET APR C 503 36
HET NAD C 603 44
HET POP C 703 9
HETNAM SO4 SULFATE ION
HETNAM APR ADENOSINE-5-DIPHOSPHORIBOSE
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM POP PYROPHOSPHATE 2-
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 7 APR 3(C15 H23 N5 O14 P2)
FORMUL 8 NAD 3(C21 H27 N7 O14 P2)
FORMUL 9 POP 3(H2 O7 P2 2-)
FORMUL 17 HOH *313(H2 O)
HELIX 1 1 HIS A 18 LYS A 31 1 14
HELIX 2 2 ARG A 53 ALA A 63 1 11
HELIX 3 3 SER A 66 LYS A 71 1 6
HELIX 4 4 SER A 84 GLY A 101 1 18
HELIX 5 5 ASP A 114 LEU A 122 5 9
HELIX 6 6 SER A 138 GLY A 149 1 12
HELIX 7 7 LYS A 150 TYR A 154 5 5
HELIX 8 8 PRO A 159 GLN A 170 1 12
HELIX 9 9 SER A 172 ALA A 191 1 20
HELIX 10 10 THR A 240 ARG A 254 1 15
HELIX 11 11 PRO A 258 SER A 265 1 8
HELIX 12 12 LEU A 314 GLN A 320 1 7
HELIX 13 13 GLU A 321 ILE A 324 5 4
HELIX 14 14 ASP A 327 VAL A 336 1 10
HELIX 15 15 HIS B 18 ALA B 32 1 15
HELIX 16 16 ARG B 53 ALA B 63 1 11
HELIX 17 17 SER B 66 LYS B 71 1 6
HELIX 18 18 SER B 84 GLY B 101 1 18
HELIX 19 19 ASP B 114 LEU B 122 5 9
HELIX 20 20 SER B 138 GLU B 148 1 11
HELIX 21 21 LYS B 150 VAL B 158 5 9
HELIX 22 22 PRO B 159 GLN B 170 1 12
HELIX 23 23 SER B 172 ALA B 191 1 20
HELIX 24 24 THR B 240 ARG B 254 1 15
HELIX 25 25 PRO B 258 GLY B 264 1 7
HELIX 26 26 LEU B 314 GLN B 320 1 7
HELIX 27 27 GLU B 321 ILE B 324 5 4
HELIX 28 28 ASP B 327 VAL B 339 1 13
HELIX 29 29 HIS C 18 ALA C 32 1 15
HELIX 30 30 ARG C 53 CYS C 64 1 12
HELIX 31 31 SER C 66 LYS C 71 1 6
HELIX 32 32 SER C 84 GLY C 101 1 18
HELIX 33 33 SER C 117 ASN C 121 5 5
HELIX 34 34 SER C 138 GLY C 149 1 12
HELIX 35 35 LYS C 150 TYR C 154 5 5
HELIX 36 36 PRO C 159 GLN C 170 1 12
HELIX 37 37 SER C 172 ALA C 191 1 20
HELIX 38 38 THR C 240 ARG C 254 1 15
HELIX 39 39 PRO C 258 SER C 265 1 8
HELIX 40 40 LEU C 314 GLN C 320 1 7
HELIX 41 41 GLU C 321 ILE C 324 5 4
HELIX 42 42 ASP C 327 VAL C 336 1 10
SHEET 1 A 5 VAL A 73 ARG A 79 0
SHEET 2 A 5 ALA A 32 HIS A 42 1 N LEU A 39 O LEU A 76
SHEET 3 A 5 TYR A 5 GLY A 12 1 N GLY A 8 O ILE A 36
SHEET 4 A 5 VAL A 106 GLY A 110 1 O VAL A 107 N ILE A 9
SHEET 5 A 5 ASP A 127 GLU A 130 1 O LEU A 129 N VAL A 108
SHEET 1 B 5 ILE A 228 ALA A 229 0
SHEET 2 B 5 HIS A 213 ARG A 218 -1 N VAL A 217 O ALA A 229
SHEET 3 B 5 PHE A 201 GLN A 210 -1 N VAL A 208 O LEU A 215
SHEET 4 B 5 THR A 283 GLN A 291 1 O ILE A 290 N VAL A 207
SHEET 5 B 5 ILE A 266 PHE A 272 -1 N ASP A 268 O PHE A 289
SHEET 1 C 4 GLY A 232 PHE A 234 0
SHEET 2 C 4 PHE A 201 GLN A 210 -1 N THR A 204 O GLY A 233
SHEET 3 C 4 HIS A 213 ARG A 218 -1 O LEU A 215 N VAL A 208
SHEET 4 C 4 ALA A 309 SER A 313 -1 O TRP A 310 N MET A 216
SHEET 1 D 5 VAL B 73 ARG B 79 0
SHEET 2 D 5 GLN B 34 HIS B 42 1 N VAL B 35 O HIS B 74
SHEET 3 D 5 TYR B 7 GLY B 12 1 N GLY B 8 O ILE B 36
SHEET 4 D 5 VAL B 106 GLY B 110 1 O VAL B 107 N ILE B 9
SHEET 5 D 5 ASP B 127 GLU B 130 1 O LEU B 129 N VAL B 108
SHEET 1 E 5 ILE B 228 ALA B 229 0
SHEET 2 E 5 HIS B 213 ARG B 218 -1 N VAL B 217 O ALA B 229
SHEET 3 E 5 THR B 200 GLN B 210 -1 N VAL B 208 O LEU B 215
SHEET 4 E 5 ARG B 282 GLN B 291 1 O ARG B 282 N PHE B 201
SHEET 5 E 5 ILE B 266 PHE B 272 -1 N ASP B 268 O PHE B 289
SHEET 1 F 4 GLY B 232 PHE B 234 0
SHEET 2 F 4 THR B 200 GLN B 210 -1 N THR B 204 O GLY B 233
SHEET 3 F 4 HIS B 213 ARG B 218 -1 O LEU B 215 N VAL B 208
SHEET 4 F 4 ALA B 309 SER B 313 -1 O TRP B 310 N MET B 216
SHEET 1 G 5 VAL C 73 ARG C 79 0
SHEET 2 G 5 GLN C 34 HIS C 42 1 N LEU C 39 O LEU C 76
SHEET 3 G 5 TYR C 7 GLY C 12 1 N GLY C 8 O ILE C 36
SHEET 4 G 5 VAL C 106 GLY C 110 1 O VAL C 107 N ILE C 9
SHEET 5 G 5 ASP C 127 GLU C 130 1 O ASP C 127 N VAL C 108
SHEET 1 H 5 ILE C 228 ALA C 229 0
SHEET 2 H 5 HIS C 213 ARG C 218 -1 N VAL C 217 O ALA C 229
SHEET 3 H 5 PHE C 201 GLN C 210 -1 N GLN C 210 O HIS C 213
SHEET 4 H 5 THR C 283 GLN C 291 1 O TYR C 288 N VAL C 207
SHEET 5 H 5 ILE C 266 PHE C 272 -1 N HIS C 270 O ALA C 287
SHEET 1 I 4 GLY C 232 PHE C 234 0
SHEET 2 I 4 PHE C 201 GLN C 210 -1 N THR C 204 O GLY C 233
SHEET 3 I 4 HIS C 213 ARG C 218 -1 O HIS C 213 N GLN C 210
SHEET 4 I 4 ALA C 309 SER C 313 -1 O MET C 312 N VAL C 214
CISPEP 1 GLN A 15 PRO A 16 0 1.67
CISPEP 2 LYS A 222 PRO A 223 0 -5.55
CISPEP 3 GLN B 15 PRO B 16 0 0.55
CISPEP 4 LYS B 222 PRO B 223 0 -3.76
CISPEP 5 GLN C 15 PRO C 16 0 -3.48
CISPEP 6 LEU C 122 PHE C 123 0 26.07
CISPEP 7 GLY C 132 HIS C 133 0 -8.28
CISPEP 8 PRO C 135 ASP C 136 0 -15.06
CISPEP 9 LYS C 222 PRO C 223 0 -1.96
SITE 1 AC1 3 ARG A 43 ARG A 53 HOH A 805
SITE 1 AC2 5 LYS A 4 LYS A 31 ASN A 104 HOH A 731
SITE 2 AC2 5 HOH A 794
SITE 1 AC3 5 HIS A 42 ARG A 43 ARG A 79 HOH A 825
SITE 2 AC3 5 HOH B 788
SITE 1 AC4 4 ASP A 316 HIS B 42 ARG B 43 ARG B 79
SITE 1 AC5 21 TYR A 188 PHE A 201 THR A 203 ASP A 205
SITE 2 AC5 21 ARG A 219 GLY A 232 GLY A 233 PHE A 234
SITE 3 AC5 21 GLU A 248 GLU A 252 ARG A 277 ARG A 280
SITE 4 AC5 21 THR A 283 GLU A 326 HIS A 328 HOH A 767
SITE 5 AC5 21 HOH A 769 HOH A 799 HOH A 818 HOH A 819
SITE 6 AC5 21 TYR C 197
SITE 1 AC6 23 TYR A 10 ILE A 11 GLY A 12 ARG A 13
SITE 2 AC6 23 PHE A 14 HIS A 21 GLY A 40 SER A 41
SITE 3 AC6 23 ASP A 80 TRP A 81 ASP A 85 TRP A 88
SITE 4 AC6 23 HIS A 111 TYR A 118 TYR A 119 GLY A 132
SITE 5 AC6 23 HIS A 133 TYR A 134 PHE A 137 HOH A 710
SITE 6 AC6 23 HOH A 717 HOH A 774 HOH A 810
SITE 1 AC7 6 ARG A 13 LYS A 113 SER A 138 SER A 139
SITE 2 AC7 6 THR A 140 ARG A 143
SITE 1 AC8 20 TYR B 188 TYR B 197 PHE B 201 THR B 203
SITE 2 AC8 20 ASP B 205 ARG B 219 GLY B 232 GLY B 233
SITE 3 AC8 20 PHE B 234 GLU B 248 GLU B 252 ARG B 277
SITE 4 AC8 20 ARG B 280 GLU B 326 HIS B 328 HOH B 730
SITE 5 AC8 20 HOH B 775 HOH B 791 HOH B 799 HOH B 834
SITE 1 AC9 24 TYR B 10 ILE B 11 GLY B 12 ARG B 13
SITE 2 AC9 24 PHE B 14 HIS B 18 HIS B 21 GLY B 40
SITE 3 AC9 24 SER B 41 ASP B 80 TRP B 81 ASP B 85
SITE 4 AC9 24 TRP B 88 HIS B 111 LYS B 113 TYR B 118
SITE 5 AC9 24 TYR B 119 GLY B 132 HIS B 133 TYR B 134
SITE 6 AC9 24 PHE B 137 HOH B 734 HOH B 741 HOH B 745
SITE 1 BC1 7 ARG B 13 ARG B 49 LYS B 113 SER B 138
SITE 2 BC1 7 SER B 139 THR B 140 ARG B 143
SITE 1 BC2 17 TYR A 197 TYR C 188 PHE C 201 THR C 203
SITE 2 BC2 17 ASP C 205 ARG C 219 GLY C 232 GLY C 233
SITE 3 BC2 17 PHE C 234 GLU C 248 GLU C 252 ARG C 277
SITE 4 BC2 17 ARG C 280 GLU C 326 HIS C 328 HOH C 731
SITE 5 BC2 17 HOH C 748
SITE 1 BC3 20 TYR C 10 ILE C 11 GLY C 12 ARG C 13
SITE 2 BC3 20 PHE C 14 HIS C 18 GLY C 40 SER C 41
SITE 3 BC3 20 ASP C 80 TRP C 81 SER C 84 ASP C 85
SITE 4 BC3 20 TRP C 88 GLY C 110 HIS C 111 TYR C 118
SITE 5 BC3 20 TYR C 119 HIS C 133 TYR C 134 PHE C 137
SITE 1 BC4 6 ARG C 13 LYS C 113 SER C 138 SER C 139
SITE 2 BC4 6 THR C 140 ARG C 143
CRYST1 201.540 201.540 98.695 90.00 90.00 120.00 P 32 2 1 18
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 0.004962 0.002865 0.000000 0.00000
SCALE2 0.000000 0.005729 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010132 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
