HEADER OXIDOREDUCTASE 12-OCT-09 3K73
TITLE CRYSTAL STRUCTURE OF PHOSPHATE BOUND HOLO GLYCERALDEHYDE-3-PHOSPHATE
TITLE 2 DEHYDROGENASE 1 FROM MRSA252 AT 2.5 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 1;
COMPND 3 CHAIN: Q, O, P, R;
COMPND 4 SYNONYM: GAPDH 1;
COMPND 5 EC: 1.2.1.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 282458;
SOURCE 4 STRAIN: MRSA252;
SOURCE 5 GENE: GAP, GAP1, GAPA, GAPA1, SAR0828;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15(PREP4);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS ROSSMANN FOLD, GLYCOLYSIS, NAD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MUKHERJEE,D.DUTTA,B.SAHA,A.K.DAS
REVDAT 3 01-NOV-23 3K73 1 REMARK
REVDAT 2 04-DEC-13 3K73 1 JRNL VERSN
REVDAT 1 18-AUG-10 3K73 0
JRNL AUTH S.MUKHERJEE,D.DUTTA,B.SAHA,A.K.DAS
JRNL TITL CRYSTAL STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE
JRNL TITL 2 DEHYDROGENASE 1 FROM METHICILLIN-RESISTANT STAPHYLOCOCCUS
JRNL TITL 3 AUREUS MRSA252 PROVIDES NOVEL INSIGHTS INTO SUBSTRATE
JRNL TITL 4 BINDING AND CATALYTIC MECHANISM.
JRNL REF J.MOL.BIOL. V. 401 949 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20620151
JRNL DOI 10.1016/J.JMB.2010.07.002
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 41927
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2115
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2920
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10184
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 216
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.16000
REMARK 3 B22 (A**2) : -1.51000
REMARK 3 B33 (A**2) : 0.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.43000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.984
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10550 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14326 ; 1.553 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1342 ; 6.546 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 461 ;37.676 ;25.401
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1793 ;15.463 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;22.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1673 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7812 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 6639 ; 0.636 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10674 ; 1.394 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3911 ; 4.063 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3651 ; 6.930 ;10.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : Q P R O
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 Q 1 Q 336 2
REMARK 3 1 P 1 P 336 2
REMARK 3 1 R 1 R 336 2
REMARK 3 1 O 1 O 336 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 Q (A): 1343 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 O (A): 1343 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 P (A): 1343 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 R (A): 1343 ; 0.060 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 Q (A): 1198 ; 0.060 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 O (A): 1198 ; 0.060 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 P (A): 1198 ; 0.060 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 R (A): 1198 ; 0.060 ; 0.500
REMARK 3 TIGHT THERMAL 1 Q (A**2): 1343 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 1 O (A**2): 1343 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 1 P (A**2): 1343 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 1 R (A**2): 1343 ; 0.130 ; 0.500
REMARK 3 MEDIUM THERMAL 1 Q (A**2): 1198 ; 0.150 ; 2.000
REMARK 3 MEDIUM THERMAL 1 O (A**2): 1198 ; 0.160 ; 2.000
REMARK 3 MEDIUM THERMAL 1 P (A**2): 1198 ; 0.150 ; 2.000
REMARK 3 MEDIUM THERMAL 1 R (A**2): 1198 ; 0.150 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 : Q 1 Q 336
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6654 -0.6649 7.8518
REMARK 3 T TENSOR
REMARK 3 T11: 0.0417 T22: 0.0953
REMARK 3 T33: 0.1011 T12: 0.0180
REMARK 3 T13: 0.0439 T23: 0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 0.7498 L22: 1.6819
REMARK 3 L33: 0.9548 L12: -0.0140
REMARK 3 L13: -0.1190 L23: 0.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.1219 S13: 0.1446
REMARK 3 S21: -0.2443 S22: -0.0580 S23: -0.2006
REMARK 3 S31: -0.0644 S32: 0.0507 S33: 0.0346
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 336
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4858 -21.6002 39.6276
REMARK 3 T TENSOR
REMARK 3 T11: 0.0399 T22: 0.0821
REMARK 3 T33: 0.1036 T12: -0.0109
REMARK 3 T13: -0.0400 T23: 0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 1.1812 L22: 1.0086
REMARK 3 L33: 1.2794 L12: -0.1763
REMARK 3 L13: -0.1781 L23: 0.0131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0393 S12: -0.1525 S13: -0.0233
REMARK 3 S21: 0.0565 S22: -0.0505 S23: -0.2064
REMARK 3 S31: 0.1088 S32: 0.1460 S33: 0.0899
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 336
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1720 -5.9621 34.3962
REMARK 3 T TENSOR
REMARK 3 T11: 0.0111 T22: 0.0987
REMARK 3 T33: 0.0598 T12: -0.0225
REMARK 3 T13: 0.0147 T23: -0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 0.9676 L22: 1.0133
REMARK 3 L33: 1.2608 L12: -0.2309
REMARK 3 L13: -0.0796 L23: -0.3428
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: -0.0811 S13: 0.0315
REMARK 3 S21: 0.0522 S22: 0.0220 S23: 0.1820
REMARK 3 S31: -0.0006 S32: -0.1873 S33: -0.0222
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 336
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1047 -33.6403 9.7408
REMARK 3 T TENSOR
REMARK 3 T11: 0.1782 T22: 0.0864
REMARK 3 T33: 0.0633 T12: -0.0390
REMARK 3 T13: -0.0387 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 0.7737 L22: 1.6125
REMARK 3 L33: 1.8355 L12: 0.1125
REMARK 3 L13: 0.4887 L23: 0.0204
REMARK 3 S TENSOR
REMARK 3 S11: 0.0953 S12: 0.0707 S13: -0.1487
REMARK 3 S21: -0.2234 S22: -0.0666 S23: 0.1027
REMARK 3 S31: 0.4668 S32: -0.1823 S33: -0.0286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: RESIDUAL ONLY
REMARK 4
REMARK 4 3K73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055628.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.8L
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41937
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 86.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.020
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.86
REMARK 200 R MERGE FOR SHELL (I) : 0.37600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3H48
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 25% PEG 4000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 52.42550
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -167.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, O, P, R
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 OD2 ASP Q 183 NH1 ARG Q 198 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 ASP Q 188 CB - CG - OD1 ANGL. DEV. = 6.3 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 ASP Q 34 -157.32 -150.67
REMARK 500 SER Q 120 37.82 -78.15
REMARK 500 ASN Q 135 18.51 -141.22
REMARK 500 ALA Q 149 -165.97 67.58
REMARK 500 ALA Q 213 -56.61 -27.69
REMARK 500 GLU Q 317 -77.92 -81.61
REMARK 500 ASP O 34 -154.64 -151.98
REMARK 500 ASP O 102 136.93 -170.67
REMARK 500 SER O 120 34.39 -79.37
REMARK 500 ASN O 135 16.52 -141.22
REMARK 500 ALA O 149 -160.79 64.11
REMARK 500 ALA O 213 -55.39 -25.22
REMARK 500 GLU O 317 -77.74 -80.08
REMARK 500 ASP P 34 -154.43 -149.14
REMARK 500 SER P 120 38.03 -82.80
REMARK 500 ASN P 135 21.92 -144.08
REMARK 500 ALA P 149 -165.54 67.16
REMARK 500 ALA P 213 -53.92 -29.02
REMARK 500 GLU P 317 -79.51 -84.18
REMARK 500 ASP R 34 -154.85 -150.01
REMARK 500 ASN R 89 36.66 72.04
REMARK 500 ASP R 102 137.88 -170.45
REMARK 500 SER R 120 36.69 -79.24
REMARK 500 ASN R 135 16.78 -142.23
REMARK 500 ALA R 149 -168.74 63.68
REMARK 500 ASP R 188 119.41 -39.76
REMARK 500 ALA R 201 110.55 -39.25
REMARK 500 ALA R 213 -57.61 -23.39
REMARK 500 SER R 290 122.94 -170.76
REMARK 500 GLU R 317 -76.19 -86.13
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 NAD Q 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 Q 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 Q 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD O 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 O 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 O 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD P 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD R 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 R 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 R 338
DBREF 3K73 Q 1 336 UNP Q6GIL8 G3P1_STAAR 1 336
DBREF 3K73 O 1 336 UNP Q6GIL8 G3P1_STAAR 1 336
DBREF 3K73 P 1 336 UNP Q6GIL8 G3P1_STAAR 1 336
DBREF 3K73 R 1 336 UNP Q6GIL8 G3P1_STAAR 1 336
SEQRES 1 Q 336 MET ALA VAL LYS VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 Q 336 GLY ARG LEU ALA PHE ARG ARG ILE GLN GLU VAL GLU GLY
SEQRES 3 Q 336 LEU GLU VAL VAL ALA VAL ASN ASP LEU THR ASP ASP ASP
SEQRES 4 Q 336 MET LEU ALA HIS LEU LEU LYS TYR ASP THR MET GLN GLY
SEQRES 5 Q 336 ARG PHE THR GLY GLU VAL GLU VAL VAL ASP GLY GLY PHE
SEQRES 6 Q 336 ARG VAL ASN GLY LYS GLU VAL LYS SER PHE SER GLU PRO
SEQRES 7 Q 336 ASP ALA SER LYS LEU PRO TRP LYS ASP LEU ASN ILE ASP
SEQRES 8 Q 336 VAL VAL LEU GLU CYS THR GLY PHE TYR THR ASP LYS ASP
SEQRES 9 Q 336 LYS ALA GLN ALA HIS ILE GLU ALA GLY ALA LYS LYS VAL
SEQRES 10 Q 336 LEU ILE SER ALA PRO ALA THR GLY ASP LEU LYS THR ILE
SEQRES 11 Q 336 VAL PHE ASN THR ASN HIS GLN GLU LEU ASP GLY SER GLU
SEQRES 12 Q 336 THR VAL VAL SER GLY ALA SER CYS THR THR ASN SER LEU
SEQRES 13 Q 336 ALA PRO VAL ALA LYS VAL LEU ASN ASP ASP PHE GLY LEU
SEQRES 14 Q 336 VAL GLU GLY LEU MET THR THR ILE HIS ALA TYR THR GLY
SEQRES 15 Q 336 ASP GLN ASN THR GLN ASP ALA PRO HIS ARG LYS GLY ASP
SEQRES 16 Q 336 LYS ARG ARG ALA ARG ALA ALA ALA GLU ASN ILE ILE PRO
SEQRES 17 Q 336 ASN SER THR GLY ALA ALA LYS ALA ILE GLY LYS VAL ILE
SEQRES 18 Q 336 PRO GLU ILE ASP GLY LYS LEU ASP GLY GLY ALA GLN ARG
SEQRES 19 Q 336 VAL PRO VAL ALA THR GLY SER LEU THR GLU LEU THR VAL
SEQRES 20 Q 336 VAL LEU GLU LYS GLN ASP VAL THR VAL GLU GLN VAL ASN
SEQRES 21 Q 336 GLU ALA MET LYS ASN ALA SER ASN GLU SER PHE GLY TYR
SEQRES 22 Q 336 THR GLU ASP GLU ILE VAL SER SER ASP VAL VAL GLY MET
SEQRES 23 Q 336 THR TYR GLY SER LEU PHE ASP ALA THR GLN THR ARG VAL
SEQRES 24 Q 336 MET SER VAL GLY ASP ARG GLN LEU VAL LYS VAL ALA ALA
SEQRES 25 Q 336 TRP TYR ASP ASN GLU MET SER TYR THR ALA GLN LEU VAL
SEQRES 26 Q 336 ARG THR LEU ALA TYR LEU ALA GLU LEU SER LYS
SEQRES 1 O 336 MET ALA VAL LYS VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 O 336 GLY ARG LEU ALA PHE ARG ARG ILE GLN GLU VAL GLU GLY
SEQRES 3 O 336 LEU GLU VAL VAL ALA VAL ASN ASP LEU THR ASP ASP ASP
SEQRES 4 O 336 MET LEU ALA HIS LEU LEU LYS TYR ASP THR MET GLN GLY
SEQRES 5 O 336 ARG PHE THR GLY GLU VAL GLU VAL VAL ASP GLY GLY PHE
SEQRES 6 O 336 ARG VAL ASN GLY LYS GLU VAL LYS SER PHE SER GLU PRO
SEQRES 7 O 336 ASP ALA SER LYS LEU PRO TRP LYS ASP LEU ASN ILE ASP
SEQRES 8 O 336 VAL VAL LEU GLU CYS THR GLY PHE TYR THR ASP LYS ASP
SEQRES 9 O 336 LYS ALA GLN ALA HIS ILE GLU ALA GLY ALA LYS LYS VAL
SEQRES 10 O 336 LEU ILE SER ALA PRO ALA THR GLY ASP LEU LYS THR ILE
SEQRES 11 O 336 VAL PHE ASN THR ASN HIS GLN GLU LEU ASP GLY SER GLU
SEQRES 12 O 336 THR VAL VAL SER GLY ALA SER CYS THR THR ASN SER LEU
SEQRES 13 O 336 ALA PRO VAL ALA LYS VAL LEU ASN ASP ASP PHE GLY LEU
SEQRES 14 O 336 VAL GLU GLY LEU MET THR THR ILE HIS ALA TYR THR GLY
SEQRES 15 O 336 ASP GLN ASN THR GLN ASP ALA PRO HIS ARG LYS GLY ASP
SEQRES 16 O 336 LYS ARG ARG ALA ARG ALA ALA ALA GLU ASN ILE ILE PRO
SEQRES 17 O 336 ASN SER THR GLY ALA ALA LYS ALA ILE GLY LYS VAL ILE
SEQRES 18 O 336 PRO GLU ILE ASP GLY LYS LEU ASP GLY GLY ALA GLN ARG
SEQRES 19 O 336 VAL PRO VAL ALA THR GLY SER LEU THR GLU LEU THR VAL
SEQRES 20 O 336 VAL LEU GLU LYS GLN ASP VAL THR VAL GLU GLN VAL ASN
SEQRES 21 O 336 GLU ALA MET LYS ASN ALA SER ASN GLU SER PHE GLY TYR
SEQRES 22 O 336 THR GLU ASP GLU ILE VAL SER SER ASP VAL VAL GLY MET
SEQRES 23 O 336 THR TYR GLY SER LEU PHE ASP ALA THR GLN THR ARG VAL
SEQRES 24 O 336 MET SER VAL GLY ASP ARG GLN LEU VAL LYS VAL ALA ALA
SEQRES 25 O 336 TRP TYR ASP ASN GLU MET SER TYR THR ALA GLN LEU VAL
SEQRES 26 O 336 ARG THR LEU ALA TYR LEU ALA GLU LEU SER LYS
SEQRES 1 P 336 MET ALA VAL LYS VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 P 336 GLY ARG LEU ALA PHE ARG ARG ILE GLN GLU VAL GLU GLY
SEQRES 3 P 336 LEU GLU VAL VAL ALA VAL ASN ASP LEU THR ASP ASP ASP
SEQRES 4 P 336 MET LEU ALA HIS LEU LEU LYS TYR ASP THR MET GLN GLY
SEQRES 5 P 336 ARG PHE THR GLY GLU VAL GLU VAL VAL ASP GLY GLY PHE
SEQRES 6 P 336 ARG VAL ASN GLY LYS GLU VAL LYS SER PHE SER GLU PRO
SEQRES 7 P 336 ASP ALA SER LYS LEU PRO TRP LYS ASP LEU ASN ILE ASP
SEQRES 8 P 336 VAL VAL LEU GLU CYS THR GLY PHE TYR THR ASP LYS ASP
SEQRES 9 P 336 LYS ALA GLN ALA HIS ILE GLU ALA GLY ALA LYS LYS VAL
SEQRES 10 P 336 LEU ILE SER ALA PRO ALA THR GLY ASP LEU LYS THR ILE
SEQRES 11 P 336 VAL PHE ASN THR ASN HIS GLN GLU LEU ASP GLY SER GLU
SEQRES 12 P 336 THR VAL VAL SER GLY ALA SER CYS THR THR ASN SER LEU
SEQRES 13 P 336 ALA PRO VAL ALA LYS VAL LEU ASN ASP ASP PHE GLY LEU
SEQRES 14 P 336 VAL GLU GLY LEU MET THR THR ILE HIS ALA TYR THR GLY
SEQRES 15 P 336 ASP GLN ASN THR GLN ASP ALA PRO HIS ARG LYS GLY ASP
SEQRES 16 P 336 LYS ARG ARG ALA ARG ALA ALA ALA GLU ASN ILE ILE PRO
SEQRES 17 P 336 ASN SER THR GLY ALA ALA LYS ALA ILE GLY LYS VAL ILE
SEQRES 18 P 336 PRO GLU ILE ASP GLY LYS LEU ASP GLY GLY ALA GLN ARG
SEQRES 19 P 336 VAL PRO VAL ALA THR GLY SER LEU THR GLU LEU THR VAL
SEQRES 20 P 336 VAL LEU GLU LYS GLN ASP VAL THR VAL GLU GLN VAL ASN
SEQRES 21 P 336 GLU ALA MET LYS ASN ALA SER ASN GLU SER PHE GLY TYR
SEQRES 22 P 336 THR GLU ASP GLU ILE VAL SER SER ASP VAL VAL GLY MET
SEQRES 23 P 336 THR TYR GLY SER LEU PHE ASP ALA THR GLN THR ARG VAL
SEQRES 24 P 336 MET SER VAL GLY ASP ARG GLN LEU VAL LYS VAL ALA ALA
SEQRES 25 P 336 TRP TYR ASP ASN GLU MET SER TYR THR ALA GLN LEU VAL
SEQRES 26 P 336 ARG THR LEU ALA TYR LEU ALA GLU LEU SER LYS
SEQRES 1 R 336 MET ALA VAL LYS VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 R 336 GLY ARG LEU ALA PHE ARG ARG ILE GLN GLU VAL GLU GLY
SEQRES 3 R 336 LEU GLU VAL VAL ALA VAL ASN ASP LEU THR ASP ASP ASP
SEQRES 4 R 336 MET LEU ALA HIS LEU LEU LYS TYR ASP THR MET GLN GLY
SEQRES 5 R 336 ARG PHE THR GLY GLU VAL GLU VAL VAL ASP GLY GLY PHE
SEQRES 6 R 336 ARG VAL ASN GLY LYS GLU VAL LYS SER PHE SER GLU PRO
SEQRES 7 R 336 ASP ALA SER LYS LEU PRO TRP LYS ASP LEU ASN ILE ASP
SEQRES 8 R 336 VAL VAL LEU GLU CYS THR GLY PHE TYR THR ASP LYS ASP
SEQRES 9 R 336 LYS ALA GLN ALA HIS ILE GLU ALA GLY ALA LYS LYS VAL
SEQRES 10 R 336 LEU ILE SER ALA PRO ALA THR GLY ASP LEU LYS THR ILE
SEQRES 11 R 336 VAL PHE ASN THR ASN HIS GLN GLU LEU ASP GLY SER GLU
SEQRES 12 R 336 THR VAL VAL SER GLY ALA SER CYS THR THR ASN SER LEU
SEQRES 13 R 336 ALA PRO VAL ALA LYS VAL LEU ASN ASP ASP PHE GLY LEU
SEQRES 14 R 336 VAL GLU GLY LEU MET THR THR ILE HIS ALA TYR THR GLY
SEQRES 15 R 336 ASP GLN ASN THR GLN ASP ALA PRO HIS ARG LYS GLY ASP
SEQRES 16 R 336 LYS ARG ARG ALA ARG ALA ALA ALA GLU ASN ILE ILE PRO
SEQRES 17 R 336 ASN SER THR GLY ALA ALA LYS ALA ILE GLY LYS VAL ILE
SEQRES 18 R 336 PRO GLU ILE ASP GLY LYS LEU ASP GLY GLY ALA GLN ARG
SEQRES 19 R 336 VAL PRO VAL ALA THR GLY SER LEU THR GLU LEU THR VAL
SEQRES 20 R 336 VAL LEU GLU LYS GLN ASP VAL THR VAL GLU GLN VAL ASN
SEQRES 21 R 336 GLU ALA MET LYS ASN ALA SER ASN GLU SER PHE GLY TYR
SEQRES 22 R 336 THR GLU ASP GLU ILE VAL SER SER ASP VAL VAL GLY MET
SEQRES 23 R 336 THR TYR GLY SER LEU PHE ASP ALA THR GLN THR ARG VAL
SEQRES 24 R 336 MET SER VAL GLY ASP ARG GLN LEU VAL LYS VAL ALA ALA
SEQRES 25 R 336 TRP TYR ASP ASN GLU MET SER TYR THR ALA GLN LEU VAL
SEQRES 26 R 336 ARG THR LEU ALA TYR LEU ALA GLU LEU SER LYS
HET NAD Q 0 44
HET PO4 Q 337 5
HET PO4 Q 338 5
HET NAD O 0 44
HET PO4 O 337 5
HET PO4 O 338 5
HET NAD P 0 44
HET PO4 P 337 5
HET PO4 P 338 5
HET NAD R 0 44
HET PO4 R 337 5
HET PO4 R 338 5
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM PO4 PHOSPHATE ION
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 6 PO4 8(O4 P 3-)
FORMUL 17 HOH *174(H2 O)
HELIX 1 1 GLY Q 11 GLN Q 22 1 12
HELIX 2 2 ASP Q 37 TYR Q 47 1 11
HELIX 3 3 ASP Q 79 LEU Q 83 5 5
HELIX 4 4 PRO Q 84 ASN Q 89 1 6
HELIX 5 5 ASP Q 102 ALA Q 112 1 11
HELIX 6 6 ASN Q 135 LEU Q 139 5 5
HELIX 7 7 SER Q 150 GLY Q 168 1 19
HELIX 8 8 ALA Q 201 ASN Q 205 5 5
HELIX 9 9 ILE Q 221 ASP Q 225 5 5
HELIX 10 10 THR Q 255 ALA Q 266 1 12
HELIX 11 11 VAL Q 279 VAL Q 284 5 6
HELIX 12 12 THR Q 295 THR Q 297 5 3
HELIX 13 13 GLU Q 317 LYS Q 336 1 20
HELIX 14 14 GLY O 11 GLN O 22 1 12
HELIX 15 15 ASP O 37 TYR O 47 1 11
HELIX 16 16 ASP O 79 LEU O 83 5 5
HELIX 17 17 PRO O 84 ASN O 89 1 6
HELIX 18 18 ASP O 102 ALA O 112 1 11
HELIX 19 19 ASN O 135 LEU O 139 5 5
HELIX 20 20 SER O 150 GLY O 168 1 19
HELIX 21 21 ALA O 201 ASN O 205 5 5
HELIX 22 22 ALA O 216 VAL O 220 5 5
HELIX 23 23 ILE O 221 ASP O 225 5 5
HELIX 24 24 THR O 255 ALA O 266 1 12
HELIX 25 25 VAL O 279 VAL O 284 5 6
HELIX 26 26 THR O 295 THR O 297 5 3
HELIX 27 27 GLU O 317 LYS O 336 1 20
HELIX 28 28 GLY P 11 GLU P 23 1 13
HELIX 29 29 ASP P 37 TYR P 47 1 11
HELIX 30 30 ASP P 79 LEU P 83 5 5
HELIX 31 31 PRO P 84 ASN P 89 1 6
HELIX 32 32 ASP P 102 GLY P 113 1 12
HELIX 33 33 ASN P 135 LEU P 139 5 5
HELIX 34 34 SER P 150 GLY P 168 1 19
HELIX 35 35 ALA P 201 ASN P 205 5 5
HELIX 36 36 ILE P 221 ASP P 225 5 5
HELIX 37 37 THR P 255 ALA P 266 1 12
HELIX 38 38 VAL P 279 VAL P 284 5 6
HELIX 39 39 THR P 295 THR P 297 5 3
HELIX 40 40 GLU P 317 LYS P 336 1 20
HELIX 41 41 GLY R 11 GLN R 22 1 12
HELIX 42 42 ASP R 37 TYR R 47 1 11
HELIX 43 43 ASP R 79 LEU R 83 5 5
HELIX 44 44 PRO R 84 ASN R 89 1 6
HELIX 45 45 ASP R 102 GLY R 113 1 12
HELIX 46 46 ASN R 135 LEU R 139 5 5
HELIX 47 47 SER R 150 GLY R 168 1 19
HELIX 48 48 ALA R 201 ASN R 205 5 5
HELIX 49 49 ILE R 221 ASP R 225 5 5
HELIX 50 50 THR R 255 ALA R 266 1 12
HELIX 51 51 VAL R 279 VAL R 284 5 6
HELIX 52 52 THR R 295 THR R 297 5 3
HELIX 53 53 GLU R 317 LYS R 336 1 20
SHEET 1 A 9 VAL Q 58 VAL Q 61 0
SHEET 2 A 9 GLY Q 64 VAL Q 67 -1 O ARG Q 66 N GLU Q 59
SHEET 3 A 9 LYS Q 70 PHE Q 75 -1 O LYS Q 70 N VAL Q 67
SHEET 4 A 9 LEU Q 27 ASN Q 33 1 N VAL Q 30 O LYS Q 73
SHEET 5 A 9 VAL Q 3 ASN Q 8 1 N VAL Q 5 O GLU Q 28
SHEET 6 A 9 VAL Q 92 GLU Q 95 1 O LEU Q 94 N ASN Q 8
SHEET 7 A 9 LYS Q 116 ILE Q 119 1 O LEU Q 118 N VAL Q 93
SHEET 8 A 9 VAL Q 145 SER Q 147 1 O VAL Q 146 N ILE Q 119
SHEET 9 A 9 LYS Q 128 THR Q 129 1 N LYS Q 128 O SER Q 147
SHEET 1 B 7 ILE Q 207 ASN Q 209 0
SHEET 2 B 7 LEU Q 228 VAL Q 235 -1 O ARG Q 234 N ILE Q 207
SHEET 3 B 7 LEU Q 169 ALA Q 179 1 N HIS Q 178 O VAL Q 235
SHEET 4 B 7 SER Q 241 LEU Q 249 -1 O THR Q 246 N LEU Q 173
SHEET 5 B 7 ARG Q 305 TYR Q 314 -1 O VAL Q 308 N VAL Q 247
SHEET 6 B 7 SER Q 290 ASP Q 293 -1 N LEU Q 291 O TRP Q 313
SHEET 7 B 7 PHE Q 271 THR Q 274 1 N GLY Q 272 O SER Q 290
SHEET 1 C 6 ILE Q 207 ASN Q 209 0
SHEET 2 C 6 LEU Q 228 VAL Q 235 -1 O ARG Q 234 N ILE Q 207
SHEET 3 C 6 LEU Q 169 ALA Q 179 1 N HIS Q 178 O VAL Q 235
SHEET 4 C 6 SER Q 241 LEU Q 249 -1 O THR Q 246 N LEU Q 173
SHEET 5 C 6 ARG Q 305 TYR Q 314 -1 O VAL Q 308 N VAL Q 247
SHEET 6 C 6 ARG Q 298 VAL Q 302 -1 N ARG Q 298 O LYS Q 309
SHEET 1 D 9 VAL O 58 VAL O 61 0
SHEET 2 D 9 GLY O 64 VAL O 67 -1 O ARG O 66 N GLU O 59
SHEET 3 D 9 LYS O 70 PHE O 75 -1 O VAL O 72 N PHE O 65
SHEET 4 D 9 LEU O 27 ASN O 33 1 N VAL O 30 O LYS O 73
SHEET 5 D 9 VAL O 3 ASN O 8 1 N VAL O 5 O GLU O 28
SHEET 6 D 9 VAL O 92 GLU O 95 1 O LEU O 94 N ALA O 6
SHEET 7 D 9 LYS O 116 ILE O 119 1 O LEU O 118 N VAL O 93
SHEET 8 D 9 VAL O 145 SER O 147 1 O VAL O 146 N ILE O 119
SHEET 9 D 9 LYS O 128 THR O 129 1 N LYS O 128 O SER O 147
SHEET 1 E 7 ILE O 207 SER O 210 0
SHEET 2 E 7 LEU O 228 VAL O 235 -1 O ARG O 234 N ILE O 207
SHEET 3 E 7 LEU O 169 ALA O 179 1 N HIS O 178 O GLN O 233
SHEET 4 E 7 SER O 241 LEU O 249 -1 O GLU O 244 N THR O 175
SHEET 5 E 7 ARG O 305 TYR O 314 -1 O VAL O 308 N VAL O 247
SHEET 6 E 7 SER O 290 ASP O 293 -1 N LEU O 291 O TRP O 313
SHEET 7 E 7 PHE O 271 THR O 274 1 N GLY O 272 O PHE O 292
SHEET 1 F 6 ILE O 207 SER O 210 0
SHEET 2 F 6 LEU O 228 VAL O 235 -1 O ARG O 234 N ILE O 207
SHEET 3 F 6 LEU O 169 ALA O 179 1 N HIS O 178 O GLN O 233
SHEET 4 F 6 SER O 241 LEU O 249 -1 O GLU O 244 N THR O 175
SHEET 5 F 6 ARG O 305 TYR O 314 -1 O VAL O 308 N VAL O 247
SHEET 6 F 6 ARG O 298 VAL O 302 -1 N MET O 300 O LEU O 307
SHEET 1 G 9 VAL P 58 VAL P 61 0
SHEET 2 G 9 GLY P 64 VAL P 67 -1 O ARG P 66 N GLU P 59
SHEET 3 G 9 LYS P 70 PHE P 75 -1 O LYS P 70 N VAL P 67
SHEET 4 G 9 LEU P 27 ASN P 33 1 N VAL P 30 O LYS P 73
SHEET 5 G 9 VAL P 3 ASN P 8 1 N VAL P 5 O GLU P 28
SHEET 6 G 9 VAL P 92 GLU P 95 1 O LEU P 94 N ALA P 6
SHEET 7 G 9 LYS P 116 ILE P 119 1 O LEU P 118 N VAL P 93
SHEET 8 G 9 VAL P 145 SER P 147 1 O VAL P 146 N ILE P 119
SHEET 9 G 9 LYS P 128 THR P 129 1 N LYS P 128 O SER P 147
SHEET 1 H 7 ILE P 207 ASN P 209 0
SHEET 2 H 7 LEU P 228 VAL P 235 -1 O ARG P 234 N ILE P 207
SHEET 3 H 7 LEU P 169 ALA P 179 1 N THR P 176 O GLN P 233
SHEET 4 H 7 SER P 241 LEU P 249 -1 O THR P 246 N LEU P 173
SHEET 5 H 7 ARG P 305 TYR P 314 -1 O VAL P 308 N VAL P 247
SHEET 6 H 7 SER P 290 ASP P 293 -1 N LEU P 291 O TRP P 313
SHEET 7 H 7 PHE P 271 THR P 274 1 N GLY P 272 O PHE P 292
SHEET 1 I 6 ILE P 207 ASN P 209 0
SHEET 2 I 6 LEU P 228 VAL P 235 -1 O ARG P 234 N ILE P 207
SHEET 3 I 6 LEU P 169 ALA P 179 1 N THR P 176 O GLN P 233
SHEET 4 I 6 SER P 241 LEU P 249 -1 O THR P 246 N LEU P 173
SHEET 5 I 6 ARG P 305 TYR P 314 -1 O VAL P 308 N VAL P 247
SHEET 6 I 6 ARG P 298 VAL P 302 -1 N MET P 300 O LEU P 307
SHEET 1 J 9 VAL R 58 VAL R 61 0
SHEET 2 J 9 GLY R 64 VAL R 67 -1 O ARG R 66 N GLU R 59
SHEET 3 J 9 LYS R 70 PHE R 75 -1 O VAL R 72 N PHE R 65
SHEET 4 J 9 LEU R 27 ASN R 33 1 N VAL R 32 O LYS R 73
SHEET 5 J 9 VAL R 3 ASN R 8 1 N VAL R 5 O GLU R 28
SHEET 6 J 9 VAL R 92 GLU R 95 1 O LEU R 94 N ALA R 6
SHEET 7 J 9 LYS R 116 ILE R 119 1 O LEU R 118 N VAL R 93
SHEET 8 J 9 VAL R 145 SER R 147 1 O VAL R 146 N ILE R 119
SHEET 9 J 9 LYS R 128 THR R 129 1 N LYS R 128 O SER R 147
SHEET 1 K 7 ILE R 207 ASN R 209 0
SHEET 2 K 7 LEU R 228 VAL R 235 -1 O ARG R 234 N ILE R 207
SHEET 3 K 7 LEU R 169 ALA R 179 1 N THR R 176 O GLN R 233
SHEET 4 K 7 SER R 241 LEU R 249 -1 O GLU R 244 N THR R 175
SHEET 5 K 7 ARG R 305 TYR R 314 -1 O VAL R 310 N LEU R 245
SHEET 6 K 7 SER R 290 ASP R 293 -1 N LEU R 291 O TRP R 313
SHEET 7 K 7 PHE R 271 THR R 274 1 N GLY R 272 O SER R 290
SHEET 1 L 6 ILE R 207 ASN R 209 0
SHEET 2 L 6 LEU R 228 VAL R 235 -1 O ARG R 234 N ILE R 207
SHEET 3 L 6 LEU R 169 ALA R 179 1 N THR R 176 O GLN R 233
SHEET 4 L 6 SER R 241 LEU R 249 -1 O GLU R 244 N THR R 175
SHEET 5 L 6 ARG R 305 TYR R 314 -1 O VAL R 310 N LEU R 245
SHEET 6 L 6 ARG R 298 VAL R 302 -1 N MET R 300 O LEU R 307
SITE 1 AC1 23 PRO P 190 GLY Q 9 GLY Q 11 ARG Q 12
SITE 2 AC1 23 ILE Q 13 ASN Q 33 ASP Q 34 LEU Q 35
SITE 3 AC1 23 PRO Q 78 CYS Q 96 THR Q 97 GLY Q 98
SITE 4 AC1 23 PHE Q 99 SER Q 120 ALA Q 121 CYS Q 151
SITE 5 AC1 23 ASN Q 316 TYR Q 320 PO4 Q 338 HOH Q 340
SITE 6 AC1 23 HOH Q 344 HOH Q 361 HOH Q 375
SITE 1 AC2 7 SER Q 150 CYS Q 151 THR Q 152 HIS Q 178
SITE 2 AC2 7 THR Q 211 ARG Q 234 HOH Q 364
SITE 1 AC3 4 NAD Q 0 THR Q 181 ASP Q 183 ARG Q 234
SITE 1 AC4 23 GLY O 9 GLY O 11 ARG O 12 ILE O 13
SITE 2 AC4 23 ASP O 34 LEU O 35 PRO O 78 CYS O 96
SITE 3 AC4 23 THR O 97 GLY O 98 PHE O 99 SER O 120
SITE 4 AC4 23 ALA O 121 CYS O 151 ASN O 316 TYR O 320
SITE 5 AC4 23 PO4 O 337 HOH O 341 HOH O 362 HOH O 367
SITE 6 AC4 23 HOH O 383 PRO R 190 HOH R 376
SITE 1 AC5 4 NAD O 0 THR O 181 ASP O 183 ARG O 234
SITE 1 AC6 7 SER O 150 CYS O 151 THR O 152 HIS O 178
SITE 2 AC6 7 THR O 211 ARG O 234 HOH O 364
SITE 1 AC7 25 GLY P 9 GLY P 11 ARG P 12 ILE P 13
SITE 2 AC7 25 ASN P 33 ASP P 34 LEU P 35 GLU P 77
SITE 3 AC7 25 PRO P 78 CYS P 96 THR P 97 GLY P 98
SITE 4 AC7 25 SER P 120 ALA P 121 THR P 181 ASN P 316
SITE 5 AC7 25 TYR P 320 PO4 P 337 HOH P 342 HOH P 349
SITE 6 AC7 25 HOH P 357 HOH P 366 HOH P 367 PRO Q 190
SITE 7 AC7 25 HOH Q 379
SITE 1 AC8 5 NAD P 0 THR P 181 ASP P 183 ARG P 234
SITE 2 AC8 5 PO4 P 338
SITE 1 AC9 5 CYS P 151 THR P 152 THR P 211 ARG P 234
SITE 2 AC9 5 PO4 P 337
SITE 1 BC1 21 PRO O 190 GLY R 9 GLY R 11 ARG R 12
SITE 2 BC1 21 ILE R 13 ASP R 34 PRO R 78 CYS R 96
SITE 3 BC1 21 THR R 97 GLY R 98 PHE R 99 SER R 120
SITE 4 BC1 21 ALA R 121 THR R 181 ASN R 316 TYR R 320
SITE 5 BC1 21 PO4 R 338 HOH R 351 HOH R 368 HOH R 369
SITE 6 BC1 21 HOH R 383
SITE 1 BC2 6 SER R 150 CYS R 151 THR R 152 HIS R 178
SITE 2 BC2 6 THR R 211 HOH R 358
SITE 1 BC3 4 NAD R 0 THR R 181 ASP R 183 ARG R 234
CRYST1 68.200 104.851 90.604 90.00 107.57 90.00 P 1 21 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 0.014663 0.000000 0.004642 0.00000
SCALE2 0.000000 0.009537 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011577 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
