HEADER ISOMERASE 15-JUL-04 1U1I
TITLE MYO-INOSITOL PHOSPHATE SYNTHASE MIPS FROM A. FULGIDUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYO-INOSITOL-1-PHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: INO1, MIPS;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 224325;
SOURCE 4 STRAIN: DSM 4304;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23+
KEYWDS NAD COFACTOR, METAL IONS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.STIEGLITZ,H.YANG,M.F.ROBERTS,B.STEC
REVDAT 6 23-AUG-23 1U1I 1 REMARK LINK
REVDAT 5 11-OCT-17 1U1I 1 REMARK
REVDAT 4 13-JUL-11 1U1I 1 VERSN
REVDAT 3 24-FEB-09 1U1I 1 VERSN
REVDAT 2 18-JAN-05 1U1I 1 JRNL
REVDAT 1 10-AUG-04 1U1I 0
JRNL AUTH K.A.STIEGLITZ,H.YANG,M.F.ROBERTS,B.STEC
JRNL TITL REACHING FOR MECHANISTIC CONSENSUS ACROSS LIFE KINGDOMS:
JRNL TITL 2 STRUCTURE AND INSIGHTS INTO CATALYSIS OF THE
JRNL TITL 3 MYO-INOSITOL-1-PHOSPHATE SYNTHASE (MIPS) FROM ARCHAEOGLOBUS
JRNL TITL 4 FULGIDUS
JRNL REF BIOCHEMISTRY V. 44 213 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15628862
JRNL DOI 10.1021/BI048267O
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.213
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3714
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 92870
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12336
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 1019
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 ANGLE DISTANCES (A) : 0.018
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.262
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.027
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.012
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U1I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023128.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 7.0
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92870
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.4
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 36.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1JKF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, POTASSIUM SULFATE, AMMONIUM
REMARK 280 SULFATE, MAGNESIUM CHLORIDE, POTASSIUM CHLORIDE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: FULL TETRAMER IN THE ASYMMETRIC UNIT
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: 21370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 CD1 LEU C 916 CG MET C 926 2.03
REMARK 500 CD1 LEU C 916 SD MET C 926 2.19
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 GLY A 223 C - N - CA ANGL. DEV. = 16.3 DEGREES
REMARK 500 LEU A 257 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ASN C1024 C - N - CA ANGL. DEV. = 18.3 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 HIS A 39 -39.31 -38.57
REMARK 500 ALA A 47 64.92 -155.13
REMARK 500 ARG A 59 63.47 -111.21
REMARK 500 LEU A 60 110.10 -38.15
REMARK 500 ALA A 100 40.40 -146.85
REMARK 500 ASN A 102 70.20 55.25
REMARK 500 ILE A 107 46.97 -76.26
REMARK 500 GLU A 109 -74.57 170.91
REMARK 500 ASP A 112 73.28 -117.51
REMARK 500 THR A 115 -24.69 176.66
REMARK 500 LEU A 116 -110.95 -123.34
REMARK 500 GLU A 119 47.90 -90.32
REMARK 500 ASP A 139 -138.40 -120.81
REMARK 500 ALA A 206 46.95 -88.49
REMARK 500 ASN A 224 114.99 135.98
REMARK 500 ASP A 225 106.46 70.02
REMARK 500 LYS A 227 78.53 -112.22
REMARK 500 ASP A 259 -156.93 -115.08
REMARK 500 LEU A 265 30.18 -85.95
REMARK 500 ASP A 269 -79.84 -46.89
REMARK 500 PRO A 300 27.32 -78.05
REMARK 500 VAL A 303 -111.59 73.78
REMARK 500 PHE A 317 131.57 -34.42
REMARK 500 ALA A 333 -32.19 -31.71
REMARK 500 SER A 368 74.48 -119.09
REMARK 500 PRO B 429 -178.65 -53.26
REMARK 500 ARG B 459 51.21 -108.05
REMARK 500 LEU B 461 -148.85 -126.33
REMARK 500 ASP B 479 127.89 -32.71
REMARK 500 ALA B 495 174.23 -55.82
REMARK 500 THR B 499 140.38 176.63
REMARK 500 LEU B 501 99.69 -46.48
REMARK 500 ASN B 502 87.99 74.26
REMARK 500 SER B 505 39.35 161.59
REMARK 500 LYS B 508 64.28 -154.99
REMARK 500 GLU B 509 -30.69 178.95
REMARK 500 LYS B 514 75.26 -173.39
REMARK 500 LEU B 516 -112.57 -105.31
REMARK 500 ASP B 539 -127.24 -122.73
REMARK 500 SER B 563 143.98 -177.54
REMARK 500 PRO B 603 -75.67 -43.80
REMARK 500 ASN B 624 88.67 82.84
REMARK 500 ASP B 625 86.32 76.00
REMARK 500 THR B 628 -96.35 -110.86
REMARK 500 ASP B 659 -142.33 -121.22
REMARK 500 ALA B 667 -178.66 -60.41
REMARK 500 ASP B 679 -49.12 -143.45
REMARK 500 PHE B 699 83.99 -171.95
REMARK 500 VAL B 703 -128.96 45.78
REMARK 500 ASN B 705 70.33 -65.08
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 K B 797 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 704 OD2
REMARK 620 2 ASP B 732 OD2 92.2
REMARK 620 3 ALA B 733 N 82.3 101.5
REMARK 620 4 NAD B 796 O1N 101.6 119.8 138.1
REMARK 620 5 NAD B 796 O7N 156.7 83.4 76.1 100.4
REMARK 620 6 HOH B1602 O 68.0 52.4 137.5 79.4 124.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1197 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C1104 OD2
REMARK 620 2 NAD C1196 O1N 102.2
REMARK 620 3 NAD C1196 O7N 133.9 112.7
REMARK 620 4 HOH C1601 O 65.0 59.2 108.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 795
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1595
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 396
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 796
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 1596
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JKF RELATED DB: PDB
REMARK 900 MYO-INOSITOL SYNTHASE FROM S. CEREVISIAE
REMARK 900 RELATED ID: 1GR0 RELATED DB: PDB
REMARK 900 MYO-INOSITOL SYNTHASE FROM M. TUBERCULOSIS
DBREF 1U1I A 1 392 UNP O28480 O28480_ARCFU 1 392
DBREF 1U1I B 401 792 UNP O28480 O28480_ARCFU 1 392
DBREF 1U1I C 801 1192 UNP O28480 O28480_ARCFU 1 392
DBREF 1U1I D 1201 1592 UNP O28480 O28480_ARCFU 1 392
SEQRES 1 A 392 MET LYS VAL TRP LEU VAL GLY ALA TYR GLY ILE VAL SER
SEQRES 2 A 392 THR THR ALA MET VAL GLY ALA ARG ALA ILE GLU ARG GLY
SEQRES 3 A 392 ILE ALA PRO LYS ILE GLY LEU VAL SER GLU LEU PRO HIS
SEQRES 4 A 392 PHE GLU GLY ILE GLU LYS TYR ALA PRO PHE SER PHE GLU
SEQRES 5 A 392 PHE GLY GLY HIS GLU ILE ARG LEU LEU SER ASN ALA TYR
SEQRES 6 A 392 GLU ALA ALA LYS GLU HIS TRP GLU LEU ASN ARG HIS PHE
SEQRES 7 A 392 ASP ARG GLU ILE LEU GLU ALA VAL LYS SER ASP LEU GLU
SEQRES 8 A 392 GLY ILE VAL ALA ARG LYS GLY THR ALA LEU ASN CYS GLY
SEQRES 9 A 392 SER GLY ILE LYS GLU LEU GLY ASP ILE LYS THR LEU GLU
SEQRES 10 A 392 GLY GLU GLY LEU SER LEU ALA GLU MET VAL SER ARG ILE
SEQRES 11 A 392 GLU GLU ASP ILE LYS SER PHE ALA ASP ASP GLU THR VAL
SEQRES 12 A 392 VAL ILE ASN VAL ALA SER THR GLU PRO LEU PRO ASN TYR
SEQRES 13 A 392 SER GLU GLU TYR HIS GLY SER LEU GLU GLY PHE GLU ARG
SEQRES 14 A 392 MET ILE ASP GLU ASP ARG LYS GLU TYR ALA SER ALA SER
SEQRES 15 A 392 MET LEU TYR ALA TYR ALA ALA LEU LYS LEU GLY LEU PRO
SEQRES 16 A 392 TYR ALA ASN PHE THR PRO SER PRO GLY SER ALA ILE PRO
SEQRES 17 A 392 ALA LEU LYS GLU LEU ALA GLU LYS LYS GLY VAL PRO HIS
SEQRES 18 A 392 ALA GLY ASN ASP GLY LYS THR GLY GLU THR LEU VAL LYS
SEQRES 19 A 392 THR THR LEU ALA PRO MET PHE ALA TYR ARG ASN MET GLU
SEQRES 20 A 392 VAL VAL GLY TRP MET SER TYR ASN ILE LEU GLY ASP TYR
SEQRES 21 A 392 ASP GLY LYS VAL LEU SER ALA ARG ASP ASN LYS GLU SER
SEQRES 22 A 392 LYS VAL LEU SER LYS ASP LYS VAL LEU GLU LYS MET LEU
SEQRES 23 A 392 GLY TYR SER PRO TYR SER ILE THR GLU ILE GLN TYR PHE
SEQRES 24 A 392 PRO SER LEU VAL ASP ASN LYS THR ALA PHE ASP PHE VAL
SEQRES 25 A 392 HIS PHE LYS GLY PHE LEU GLY LYS LEU MET LYS PHE TYR
SEQRES 26 A 392 PHE ILE TRP ASP ALA ILE ASP ALA ILE VAL ALA ALA PRO
SEQRES 27 A 392 LEU ILE LEU ASP ILE ALA ARG PHE LEU LEU PHE ALA LYS
SEQRES 28 A 392 LYS LYS GLY VAL LYS GLY VAL VAL LYS GLU MET ALA PHE
SEQRES 29 A 392 PHE PHE LYS SER PRO MET ASP THR ASN VAL ILE ASN THR
SEQRES 30 A 392 HIS GLU GLN PHE VAL VAL LEU LYS GLU TRP TYR SER ASN
SEQRES 31 A 392 LEU LYS
SEQRES 1 B 392 MET LYS VAL TRP LEU VAL GLY ALA TYR GLY ILE VAL SER
SEQRES 2 B 392 THR THR ALA MET VAL GLY ALA ARG ALA ILE GLU ARG GLY
SEQRES 3 B 392 ILE ALA PRO LYS ILE GLY LEU VAL SER GLU LEU PRO HIS
SEQRES 4 B 392 PHE GLU GLY ILE GLU LYS TYR ALA PRO PHE SER PHE GLU
SEQRES 5 B 392 PHE GLY GLY HIS GLU ILE ARG LEU LEU SER ASN ALA TYR
SEQRES 6 B 392 GLU ALA ALA LYS GLU HIS TRP GLU LEU ASN ARG HIS PHE
SEQRES 7 B 392 ASP ARG GLU ILE LEU GLU ALA VAL LYS SER ASP LEU GLU
SEQRES 8 B 392 GLY ILE VAL ALA ARG LYS GLY THR ALA LEU ASN CYS GLY
SEQRES 9 B 392 SER GLY ILE LYS GLU LEU GLY ASP ILE LYS THR LEU GLU
SEQRES 10 B 392 GLY GLU GLY LEU SER LEU ALA GLU MET VAL SER ARG ILE
SEQRES 11 B 392 GLU GLU ASP ILE LYS SER PHE ALA ASP ASP GLU THR VAL
SEQRES 12 B 392 VAL ILE ASN VAL ALA SER THR GLU PRO LEU PRO ASN TYR
SEQRES 13 B 392 SER GLU GLU TYR HIS GLY SER LEU GLU GLY PHE GLU ARG
SEQRES 14 B 392 MET ILE ASP GLU ASP ARG LYS GLU TYR ALA SER ALA SER
SEQRES 15 B 392 MET LEU TYR ALA TYR ALA ALA LEU LYS LEU GLY LEU PRO
SEQRES 16 B 392 TYR ALA ASN PHE THR PRO SER PRO GLY SER ALA ILE PRO
SEQRES 17 B 392 ALA LEU LYS GLU LEU ALA GLU LYS LYS GLY VAL PRO HIS
SEQRES 18 B 392 ALA GLY ASN ASP GLY LYS THR GLY GLU THR LEU VAL LYS
SEQRES 19 B 392 THR THR LEU ALA PRO MET PHE ALA TYR ARG ASN MET GLU
SEQRES 20 B 392 VAL VAL GLY TRP MET SER TYR ASN ILE LEU GLY ASP TYR
SEQRES 21 B 392 ASP GLY LYS VAL LEU SER ALA ARG ASP ASN LYS GLU SER
SEQRES 22 B 392 LYS VAL LEU SER LYS ASP LYS VAL LEU GLU LYS MET LEU
SEQRES 23 B 392 GLY TYR SER PRO TYR SER ILE THR GLU ILE GLN TYR PHE
SEQRES 24 B 392 PRO SER LEU VAL ASP ASN LYS THR ALA PHE ASP PHE VAL
SEQRES 25 B 392 HIS PHE LYS GLY PHE LEU GLY LYS LEU MET LYS PHE TYR
SEQRES 26 B 392 PHE ILE TRP ASP ALA ILE ASP ALA ILE VAL ALA ALA PRO
SEQRES 27 B 392 LEU ILE LEU ASP ILE ALA ARG PHE LEU LEU PHE ALA LYS
SEQRES 28 B 392 LYS LYS GLY VAL LYS GLY VAL VAL LYS GLU MET ALA PHE
SEQRES 29 B 392 PHE PHE LYS SER PRO MET ASP THR ASN VAL ILE ASN THR
SEQRES 30 B 392 HIS GLU GLN PHE VAL VAL LEU LYS GLU TRP TYR SER ASN
SEQRES 31 B 392 LEU LYS
SEQRES 1 C 392 MET LYS VAL TRP LEU VAL GLY ALA TYR GLY ILE VAL SER
SEQRES 2 C 392 THR THR ALA MET VAL GLY ALA ARG ALA ILE GLU ARG GLY
SEQRES 3 C 392 ILE ALA PRO LYS ILE GLY LEU VAL SER GLU LEU PRO HIS
SEQRES 4 C 392 PHE GLU GLY ILE GLU LYS TYR ALA PRO PHE SER PHE GLU
SEQRES 5 C 392 PHE GLY GLY HIS GLU ILE ARG LEU LEU SER ASN ALA TYR
SEQRES 6 C 392 GLU ALA ALA LYS GLU HIS TRP GLU LEU ASN ARG HIS PHE
SEQRES 7 C 392 ASP ARG GLU ILE LEU GLU ALA VAL LYS SER ASP LEU GLU
SEQRES 8 C 392 GLY ILE VAL ALA ARG LYS GLY THR ALA LEU ASN CYS GLY
SEQRES 9 C 392 SER GLY ILE LYS GLU LEU GLY ASP ILE LYS THR LEU GLU
SEQRES 10 C 392 GLY GLU GLY LEU SER LEU ALA GLU MET VAL SER ARG ILE
SEQRES 11 C 392 GLU GLU ASP ILE LYS SER PHE ALA ASP ASP GLU THR VAL
SEQRES 12 C 392 VAL ILE ASN VAL ALA SER THR GLU PRO LEU PRO ASN TYR
SEQRES 13 C 392 SER GLU GLU TYR HIS GLY SER LEU GLU GLY PHE GLU ARG
SEQRES 14 C 392 MET ILE ASP GLU ASP ARG LYS GLU TYR ALA SER ALA SER
SEQRES 15 C 392 MET LEU TYR ALA TYR ALA ALA LEU LYS LEU GLY LEU PRO
SEQRES 16 C 392 TYR ALA ASN PHE THR PRO SER PRO GLY SER ALA ILE PRO
SEQRES 17 C 392 ALA LEU LYS GLU LEU ALA GLU LYS LYS GLY VAL PRO HIS
SEQRES 18 C 392 ALA GLY ASN ASP GLY LYS THR GLY GLU THR LEU VAL LYS
SEQRES 19 C 392 THR THR LEU ALA PRO MET PHE ALA TYR ARG ASN MET GLU
SEQRES 20 C 392 VAL VAL GLY TRP MET SER TYR ASN ILE LEU GLY ASP TYR
SEQRES 21 C 392 ASP GLY LYS VAL LEU SER ALA ARG ASP ASN LYS GLU SER
SEQRES 22 C 392 LYS VAL LEU SER LYS ASP LYS VAL LEU GLU LYS MET LEU
SEQRES 23 C 392 GLY TYR SER PRO TYR SER ILE THR GLU ILE GLN TYR PHE
SEQRES 24 C 392 PRO SER LEU VAL ASP ASN LYS THR ALA PHE ASP PHE VAL
SEQRES 25 C 392 HIS PHE LYS GLY PHE LEU GLY LYS LEU MET LYS PHE TYR
SEQRES 26 C 392 PHE ILE TRP ASP ALA ILE ASP ALA ILE VAL ALA ALA PRO
SEQRES 27 C 392 LEU ILE LEU ASP ILE ALA ARG PHE LEU LEU PHE ALA LYS
SEQRES 28 C 392 LYS LYS GLY VAL LYS GLY VAL VAL LYS GLU MET ALA PHE
SEQRES 29 C 392 PHE PHE LYS SER PRO MET ASP THR ASN VAL ILE ASN THR
SEQRES 30 C 392 HIS GLU GLN PHE VAL VAL LEU LYS GLU TRP TYR SER ASN
SEQRES 31 C 392 LEU LYS
SEQRES 1 D 392 MET LYS VAL TRP LEU VAL GLY ALA TYR GLY ILE VAL SER
SEQRES 2 D 392 THR THR ALA MET VAL GLY ALA ARG ALA ILE GLU ARG GLY
SEQRES 3 D 392 ILE ALA PRO LYS ILE GLY LEU VAL SER GLU LEU PRO HIS
SEQRES 4 D 392 PHE GLU GLY ILE GLU LYS TYR ALA PRO PHE SER PHE GLU
SEQRES 5 D 392 PHE GLY GLY HIS GLU ILE ARG LEU LEU SER ASN ALA TYR
SEQRES 6 D 392 GLU ALA ALA LYS GLU HIS TRP GLU LEU ASN ARG HIS PHE
SEQRES 7 D 392 ASP ARG GLU ILE LEU GLU ALA VAL LYS SER ASP LEU GLU
SEQRES 8 D 392 GLY ILE VAL ALA ARG LYS GLY THR ALA LEU ASN CYS GLY
SEQRES 9 D 392 SER GLY ILE LYS GLU LEU GLY ASP ILE LYS THR LEU GLU
SEQRES 10 D 392 GLY GLU GLY LEU SER LEU ALA GLU MET VAL SER ARG ILE
SEQRES 11 D 392 GLU GLU ASP ILE LYS SER PHE ALA ASP ASP GLU THR VAL
SEQRES 12 D 392 VAL ILE ASN VAL ALA SER THR GLU PRO LEU PRO ASN TYR
SEQRES 13 D 392 SER GLU GLU TYR HIS GLY SER LEU GLU GLY PHE GLU ARG
SEQRES 14 D 392 MET ILE ASP GLU ASP ARG LYS GLU TYR ALA SER ALA SER
SEQRES 15 D 392 MET LEU TYR ALA TYR ALA ALA LEU LYS LEU GLY LEU PRO
SEQRES 16 D 392 TYR ALA ASN PHE THR PRO SER PRO GLY SER ALA ILE PRO
SEQRES 17 D 392 ALA LEU LYS GLU LEU ALA GLU LYS LYS GLY VAL PRO HIS
SEQRES 18 D 392 ALA GLY ASN ASP GLY LYS THR GLY GLU THR LEU VAL LYS
SEQRES 19 D 392 THR THR LEU ALA PRO MET PHE ALA TYR ARG ASN MET GLU
SEQRES 20 D 392 VAL VAL GLY TRP MET SER TYR ASN ILE LEU GLY ASP TYR
SEQRES 21 D 392 ASP GLY LYS VAL LEU SER ALA ARG ASP ASN LYS GLU SER
SEQRES 22 D 392 LYS VAL LEU SER LYS ASP LYS VAL LEU GLU LYS MET LEU
SEQRES 23 D 392 GLY TYR SER PRO TYR SER ILE THR GLU ILE GLN TYR PHE
SEQRES 24 D 392 PRO SER LEU VAL ASP ASN LYS THR ALA PHE ASP PHE VAL
SEQRES 25 D 392 HIS PHE LYS GLY PHE LEU GLY LYS LEU MET LYS PHE TYR
SEQRES 26 D 392 PHE ILE TRP ASP ALA ILE ASP ALA ILE VAL ALA ALA PRO
SEQRES 27 D 392 LEU ILE LEU ASP ILE ALA ARG PHE LEU LEU PHE ALA LYS
SEQRES 28 D 392 LYS LYS GLY VAL LYS GLY VAL VAL LYS GLU MET ALA PHE
SEQRES 29 D 392 PHE PHE LYS SER PRO MET ASP THR ASN VAL ILE ASN THR
SEQRES 30 D 392 HIS GLU GLN PHE VAL VAL LEU LYS GLU TRP TYR SER ASN
SEQRES 31 D 392 LEU LYS
HET PO4 A 395 5
HET NAD A 396 44
HET PO4 B 795 5
HET K B 797 1
HET NAD B 796 44
HET PO4 C1195 5
HET K C1197 1
HET NAD C1196 44
HET PO4 D1595 5
HET NAD D1596 44
HETNAM PO4 PHOSPHATE ION
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM K POTASSIUM ION
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 6 NAD 4(C21 H27 N7 O14 P2)
FORMUL 8 K 2(K 1+)
FORMUL 15 HOH *1019(H2 O)
HELIX 1 1 GLY A 10 GLY A 26 1 17
HELIX 2 2 LEU A 33 GLU A 41 5 9
HELIX 3 3 ASN A 63 ARG A 76 1 14
HELIX 4 4 ASP A 79 GLU A 91 1 13
HELIX 5 5 LEU A 123 ILE A 130 1 8
HELIX 6 6 ASP A 133 ALA A 138 1 6
HELIX 7 7 SER A 157 GLY A 162 1 6
HELIX 8 8 SER A 163 GLU A 173 1 11
HELIX 9 9 SER A 180 LEU A 192 1 13
HELIX 10 10 ILE A 207 LYS A 216 1 10
HELIX 11 11 GLY A 229 TYR A 243 1 15
HELIX 12 12 ASP A 259 LEU A 265 1 7
HELIX 13 13 ALA A 267 GLY A 287 1 21
HELIX 14 14 PHE A 317 GLY A 319 5 3
HELIX 15 15 ILE A 331 LYS A 352 1 22
HELIX 16 16 MET A 362 PHE A 366 5 5
HELIX 17 17 ASN A 376 LYS A 392 1 17
HELIX 18 18 GLY B 410 ARG B 425 1 16
HELIX 19 19 LEU B 433 GLU B 441 5 9
HELIX 20 20 GLY B 442 TYR B 446 5 5
HELIX 21 21 ASN B 463 ARG B 476 1 14
HELIX 22 22 ASP B 479 GLY B 492 1 14
HELIX 23 23 LEU B 516 GLY B 520 5 5
HELIX 24 24 SER B 522 SER B 536 1 15
HELIX 25 25 SER B 563 ASP B 572 1 10
HELIX 26 26 SER B 580 LYS B 591 1 12
HELIX 27 27 ILE B 607 GLY B 618 1 12
HELIX 28 28 THR B 628 ARG B 644 1 17
HELIX 29 29 ASP B 659 LEU B 665 1 7
HELIX 30 30 ARG B 668 LYS B 678 1 11
HELIX 31 31 LEU B 682 GLY B 687 1 6
HELIX 32 32 PRO B 700 VAL B 703 5 4
HELIX 33 33 ILE B 731 LYS B 753 1 23
HELIX 34 34 LYS B 760 PHE B 766 5 7
HELIX 35 35 ASN B 776 LYS B 792 1 17
HELIX 36 36 GLY C 810 ARG C 825 1 16
HELIX 37 37 LEU C 833 GLU C 841 5 9
HELIX 38 38 GLY C 842 TYR C 846 5 5
HELIX 39 39 ALA C 864 ARG C 876 1 13
HELIX 40 40 ASP C 879 VAL C 886 1 8
HELIX 41 41 VAL C 886 GLY C 892 1 7
HELIX 42 42 LEU C 916 GLY C 920 5 5
HELIX 43 43 SER C 922 SER C 936 1 15
HELIX 44 44 SER C 957 GLY C 962 1 6
HELIX 45 45 SER C 963 ILE C 971 1 9
HELIX 46 46 SER C 980 LEU C 992 1 13
HELIX 47 47 PRO C 1008 LYS C 1017 1 10
HELIX 48 48 GLY C 1029 ALA C 1038 1 10
HELIX 49 49 ALA C 1038 ARG C 1044 1 7
HELIX 50 50 ASP C 1059 LEU C 1065 1 7
HELIX 51 51 ASP C 1069 VAL C 1081 1 13
HELIX 52 52 LEU C 1082 GLY C 1087 1 6
HELIX 53 53 ILE C 1131 LYS C 1153 1 23
HELIX 54 54 MET C 1162 PHE C 1166 5 5
HELIX 55 55 ASN C 1176 ASN C 1190 1 15
HELIX 56 56 GLY D 1210 ARG D 1225 1 16
HELIX 57 57 LEU D 1233 GLU D 1241 5 9
HELIX 58 58 GLY D 1242 TYR D 1246 5 5
HELIX 59 59 ASN D 1263 GLU D 1273 1 11
HELIX 60 60 ASP D 1279 VAL D 1286 1 8
HELIX 61 61 VAL D 1286 ILE D 1293 1 8
HELIX 62 62 SER D 1322 ALA D 1338 1 17
HELIX 63 63 SER D 1363 ASP D 1374 1 12
HELIX 64 64 ARG D 1375 ALA D 1379 5 5
HELIX 65 65 SER D 1380 LEU D 1392 1 13
HELIX 66 66 ILE D 1407 LYS D 1416 1 10
HELIX 67 67 GLY D 1429 ARG D 1444 1 16
HELIX 68 68 TYR D 1460 LEU D 1465 1 6
HELIX 69 69 ARG D 1468 LYS D 1480 1 13
HELIX 70 70 LEU D 1482 GLY D 1487 1 6
HELIX 71 71 PRO D 1500 VAL D 1503 5 4
HELIX 72 72 PHE D 1517 GLY D 1519 5 3
HELIX 73 73 ASP D 1532 ALA D 1537 1 6
HELIX 74 74 ALA D 1537 LYS D 1552 1 16
HELIX 75 75 VAL D 1559 PHE D 1566 5 8
HELIX 76 76 ASN D 1576 LYS D 1592 1 17
SHEET 1 A 7 ARG A 96 LYS A 97 0
SHEET 2 A 7 GLU A 52 GLU A 57 1 N GLY A 55 O ARG A 96
SHEET 3 A 7 LYS A 2 VAL A 6 1 N LEU A 5 O GLY A 54
SHEET 4 A 7 VAL A 144 ASN A 146 1 O ILE A 145 N VAL A 6
SHEET 5 A 7 TYR A 196 ASN A 198 1 O ALA A 197 N VAL A 144
SHEET 6 A 7 PRO A 220 GLY A 223 1 O ALA A 222 N TYR A 196
SHEET 7 A 7 GLY A 357 VAL A 358 1 O GLY A 357 N HIS A 221
SHEET 1 B 8 TYR A 291 TYR A 298 0
SHEET 2 B 8 GLU A 247 LEU A 257 1 N TRP A 251 O ILE A 293
SHEET 3 B 8 THR A 307 LYS A 315 -1 O PHE A 311 N MET A 252
SHEET 4 B 8 LEU A 321 ASP A 329 -1 O PHE A 326 N ASP A 310
SHEET 5 B 8 LEU B 721 ASP B 729 -1 O LYS B 723 N ASP A 329
SHEET 6 B 8 THR B 707 LYS B 715 -1 N ALA B 708 O TRP B 728
SHEET 7 B 8 GLU B 647 LEU B 657 -1 N MET B 652 O PHE B 711
SHEET 8 B 8 TYR B 691 TYR B 698 1 O GLN B 697 N ASN B 655
SHEET 1 C 7 ARG B 496 LYS B 497 0
SHEET 2 C 7 GLU B 452 GLU B 457 1 N GLU B 457 O ARG B 496
SHEET 3 C 7 LYS B 402 VAL B 406 1 N VAL B 403 O GLU B 452
SHEET 4 C 7 VAL B 543 ASN B 546 1 O VAL B 543 N TRP B 404
SHEET 5 C 7 TYR B 596 ASN B 598 1 O ALA B 597 N ASN B 546
SHEET 6 C 7 PRO B 620 GLY B 623 1 O ALA B 622 N ASN B 598
SHEET 7 C 7 GLY B 757 VAL B 758 1 O GLY B 757 N HIS B 621
SHEET 1 D 6 ARG C 896 LYS C 897 0
SHEET 2 D 6 GLU C 852 GLU C 857 1 N GLY C 855 O ARG C 896
SHEET 3 D 6 LYS C 802 VAL C 806 1 N VAL C 803 O GLU C 852
SHEET 4 D 6 THR C 942 ASN C 946 1 O VAL C 943 N TRP C 804
SHEET 5 D 6 TYR C 996 ASN C 998 1 O ALA C 997 N ASN C 946
SHEET 6 D 6 ALA C1022 GLY C1023 1 O ALA C1022 N TYR C 996
SHEET 1 E 8 TYR C1091 TYR C1098 0
SHEET 2 E 8 GLU C1047 LEU C1057 1 N SER C1053 O ILE C1093
SHEET 3 E 8 THR C1107 LYS C1115 -1 O HIS C1113 N VAL C1049
SHEET 4 E 8 LEU C1121 ASP C1129 -1 O TRP C1128 N ALA C1108
SHEET 5 E 8 LEU D1521 ILE D1531 -1 O LYS D1523 N ASP C1129
SHEET 6 E 8 ASN D1505 LYS D1515 -1 N ASP D1510 O PHE D1526
SHEET 7 E 8 GLU D1447 LEU D1457 -1 N MET D1452 O PHE D1511
SHEET 8 E 8 TYR D1491 TYR D1498 1 O GLU D1495 N ASN D1455
SHEET 1 F 4 GLU D1252 GLY D1254 0
SHEET 2 F 4 LYS D1202 VAL D1206 1 N LEU D1205 O GLY D1254
SHEET 3 F 4 THR D1342 ASN D1346 1 O ILE D1345 N TRP D1204
SHEET 4 F 4 TYR D1396 ASN D1398 1 O ALA D1397 N ASN D1346
SHEET 1 G 2 HIS D1256 GLU D1257 0
SHEET 2 G 2 ARG D1296 LYS D1297 1 O ARG D1296 N GLU D1257
LINK OD2 ASP B 704 K K B 797 1555 1555 2.78
LINK OD2 ASP B 732 K K B 797 1555 1555 3.42
LINK N ALA B 733 K K B 797 1555 1555 3.37
LINK O1N NAD B 796 K K B 797 1555 1555 2.76
LINK O7N NAD B 796 K K B 797 1555 1555 2.91
LINK K K B 797 O HOH B1602 1555 1555 2.86
LINK OD2 ASP C1104 K K C1197 1555 1555 2.88
LINK O1N NAD C1196 K K C1197 1555 1555 2.45
LINK O7N NAD C1196 K K C1197 1555 1555 3.01
LINK K K C1197 O HOH C1601 1555 1555 2.73
SITE 1 AC1 7 GLY A 226 GLY A 229 GLU A 230 THR A 231
SITE 2 AC1 7 LYS A 278 LYS A 306 LYS A 367
SITE 1 AC2 7 THR B 628 GLY B 629 GLU B 630 THR B 631
SITE 2 AC2 7 LYS B 678 LYS B 706 LYS B 767
SITE 1 AC3 7 THR C1028 GLY C1029 GLU C1030 THR C1031
SITE 2 AC3 7 LYS C1106 LYS C1167 HOH C1689
SITE 1 AC4 8 THR D1428 GLY D1429 GLU D1430 THR D1431
SITE 2 AC4 8 LYS D1474 LYS D1478 LYS D1506 LYS D1567
SITE 1 AC5 5 ASP B 704 ASP B 732 ALA B 733 NAD B 796
SITE 2 AC5 5 HOH B1602
SITE 1 AC6 5 ILE C 811 ASP C1104 ASP C1132 NAD C1196
SITE 2 AC6 5 HOH C1601
SITE 1 AC7 25 GLY A 7 TYR A 9 GLY A 10 ILE A 11
SITE 2 AC7 25 VAL A 12 HIS A 56 GLU A 57 ARG A 59
SITE 3 AC7 25 THR A 99 VAL A 147 ALA A 148 SER A 149
SITE 4 AC7 25 THR A 150 ALA A 181 TYR A 185 PHE A 199
SITE 5 AC7 25 GLY A 226 THR A 228 TYR A 260 ASP A 261
SITE 6 AC7 25 LEU A 265 LYS A 274 ASP A 304 ASP A 332
SITE 7 AC7 25 HOH A1604
SITE 1 AC8 25 GLY B 407 TYR B 409 GLY B 410 ILE B 411
SITE 2 AC8 25 VAL B 412 GLU B 457 ILE B 458 ARG B 459
SITE 3 AC8 25 HIS B 471 THR B 499 ALA B 500 VAL B 547
SITE 4 AC8 25 ALA B 548 SER B 549 THR B 550 TYR B 585
SITE 5 AC8 25 PHE B 599 GLY B 626 THR B 628 TYR B 660
SITE 6 AC8 25 ASP B 661 LYS B 674 ASP B 732 ALA B 736
SITE 7 AC8 25 K B 797
SITE 1 AC9 27 GLY C 807 TYR C 809 GLY C 810 ILE C 811
SITE 2 AC9 27 VAL C 812 GLU C 857 ILE C 858 ARG C 859
SITE 3 AC9 27 THR C 899 VAL C 947 ALA C 948 SER C 949
SITE 4 AC9 27 THR C 950 TYR C 985 THR C1000 PRO C1001
SITE 5 AC9 27 ASP C1025 GLY C1026 THR C1028 TYR C1060
SITE 6 AC9 27 ASP C1061 LYS C1074 ASP C1132 ALA C1136
SITE 7 AC9 27 LYS C1167 K C1197 HOH C1601
SITE 1 BC1 23 GLY D1207 TYR D1209 GLY D1210 ILE D1211
SITE 2 BC1 23 VAL D1212 GLU D1257 ILE D1258 ARG D1259
SITE 3 BC1 23 THR D1299 ALA D1300 VAL D1347 ALA D1348
SITE 4 BC1 23 SER D1349 THR D1350 TYR D1385 PHE D1399
SITE 5 BC1 23 ASP D1425 GLY D1426 THR D1428 TYR D1460
SITE 6 BC1 23 ASP D1461 LYS D1474 ASP D1532
CRYST1 62.770 83.940 91.790 65.79 72.43 74.98 P 1 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 0.015931 -0.004275 -0.003756 0.00000
SCALE2 0.000000 0.012335 -0.004766 0.00000
SCALE3 0.000000 0.000000 0.012251 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
