HEADER TRANSFERASE 26-MAR-07 2P9T
TITLE CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE KINASE-2 BOUND TO 3-
TITLE 2 PHOSPHOGLYCERATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOGLYCERATE KINASE, TESTIS SPECIFIC;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.2.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: C3H/HE;
SOURCE 6 GENE: PGK2, PGK-2;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGK-2-PGEX4T3
KEYWDS TRANSFERASE, PHOSPHOGLYCERATE KINSE, ENZYME-SUBSTRATE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.SAWYER,A.F.MONZINGO,E.C.POTEET,J.D.ROBERTUS
REVDAT 5 30-AUG-23 2P9T 1 REMARK
REVDAT 4 18-OCT-17 2P9T 1 REMARK
REVDAT 3 24-FEB-09 2P9T 1 VERSN
REVDAT 2 22-APR-08 2P9T 1 JRNL
REVDAT 1 27-NOV-07 2P9T 0
JRNL AUTH G.M.SAWYER,A.F.MONZINGO,E.C.POTEET,D.A.O'BRIEN,J.D.ROBERTUS
JRNL TITL X-RAY ANALYSIS OF PHOSPHOGLYCERATE KINASE 2, A
JRNL TITL 2 SPERM-SPECIFIC ISOFORM FROM MUS MUSCULUS.
JRNL REF PROTEINS V. 71 1134 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 18004764
JRNL DOI 10.1002/PROT.21801
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 24465
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 SET) : 0.221
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1223
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 24
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 289
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.93900
REMARK 3 B22 (A**2) : 3.12100
REMARK 3 B33 (A**2) : 1.81800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.56700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.208 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.796 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.008 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 43.21
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : 3PG.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : 3PG.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2P9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : BLUE MAX-FLUX CONFOCAL OPTICAL
REMARK 200 SYSTEM
REMARK 200 OPTICS : BLUE MAX-FLUX CONFOCAL OPTICAL
REMARK 200 SYSTEM
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24578
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.20900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1VJD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM D-3-PHOSPHOGLYCERATE, 30%
REMARK 280 PEG6000, 0.1 M TRIS-HCL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K, PH 8.00
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 32.15000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ALA A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
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 LYS A 29 104.57 -167.08
REMARK 500 ASN A 35 107.79 -164.90
REMARK 500 LYS A 74 -1.09 -142.47
REMARK 500 ASN A 109 67.47 -156.46
REMARK 500 ASN A 120 116.44 -36.10
REMARK 500 LYS A 229 -31.42 -132.96
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 3PG A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P9Q RELATED DB: PDB
REMARK 900 APO PHOSPHOGLYCERATE KINASE-2
REMARK 900 RELATED ID: 2PAA RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS A GLN -> ARG SEQUENCE CONFLICT AT RESIDUE 151 IN
REMARK 999 THE UNIPROT DATABASE. AUTHORS STATE THAT PROTEIN SEQUENCE
REMARK 999 USED IN THIS PDB ENTRY IS FROM C3H/HE STRAIN WHICH HAS
REMARK 999 ARG AT RESIDUE 150, WHEREAS UNIPROT SEQUENCE IS FROM
REMARK 999 BALB/C STRAIN THAT HAS GLN AT RESIDUE 151.
DBREF 2P9T A 1 416 UNP P09041 PGK2_MOUSE 2 417
SEQADV 2P9T ARG A 150 UNP P09041 GLN 151 SEE REMARK 999
SEQRES 1 A 416 ALA LEU SER ALA LYS LEU THR LEU ASP LYS VAL ASP LEU
SEQRES 2 A 416 LYS GLY LYS ARG VAL ILE MET ARG VAL ASP PHE ASN VAL
SEQRES 3 A 416 PRO MET LYS ASN ASN GLN ILE THR ASN ASN GLN ARG ILE
SEQRES 4 A 416 LYS ALA ALA ILE PRO SER ILE LYS HIS CYS LEU ASP ASN
SEQRES 5 A 416 GLY ALA LYS SER VAL VAL LEU MET SER HIS LEU GLY ARG
SEQRES 6 A 416 PRO ASP GLY ILE PRO MET PRO ASP LYS TYR SER LEU GLU
SEQRES 7 A 416 PRO VAL ALA ASP GLU LEU LYS SER LEU LEU ASN LYS ASP
SEQRES 8 A 416 VAL ILE PHE LEU LYS ASP CYS VAL GLY PRO GLU VAL GLU
SEQRES 9 A 416 GLN ALA CYS ALA ASN PRO ASP ASN GLY SER ILE ILE LEU
SEQRES 10 A 416 LEU GLU ASN LEU ARG PHE HIS VAL GLU GLU GLU GLY LYS
SEQRES 11 A 416 GLY LYS ASP SER SER GLY LYS LYS ILE SER ALA ASP PRO
SEQRES 12 A 416 ALA LYS VAL GLU ALA PHE ARG ALA SER LEU SER LYS LEU
SEQRES 13 A 416 GLY ASP VAL TYR VAL ASN ASP ALA PHE GLY THR ALA HIS
SEQRES 14 A 416 ARG ALA HIS SER SER MET VAL GLY VAL ASN LEU PRO GLN
SEQRES 15 A 416 LYS ALA SER GLY PHE LEU MET LYS LYS GLU LEU ASP TYR
SEQRES 16 A 416 PHE SER LYS ALA LEU GLU LYS PRO GLU ARG PRO PHE LEU
SEQRES 17 A 416 ALA ILE LEU GLY GLY ALA LYS VAL LYS ASP LYS ILE GLN
SEQRES 18 A 416 LEU ILE LYS ASN MET LEU ASP LYS VAL ASN PHE MET ILE
SEQRES 19 A 416 ILE GLY GLY GLY MET ALA TYR THR PHE LEU LYS GLU LEU
SEQRES 20 A 416 LYS ASN MET GLN ILE GLY ALA SER LEU PHE ASP GLU GLU
SEQRES 21 A 416 GLY ALA THR ILE VAL LYS GLU ILE MET GLU LYS ALA GLU
SEQRES 22 A 416 LYS ASN GLY VAL LYS ILE VAL PHE PRO VAL ASP PHE VAL
SEQRES 23 A 416 THR GLY ASP LYS PHE ASP GLU ASN ALA LYS VAL GLY GLN
SEQRES 24 A 416 ALA THR ILE GLU SER GLY ILE PRO SER GLY TRP MET GLY
SEQRES 25 A 416 LEU ASP CYS GLY PRO GLU SER ILE LYS ILE ASN ALA GLN
SEQRES 26 A 416 ILE VAL ALA GLN ALA LYS LEU ILE VAL TRP ASN GLY PRO
SEQRES 27 A 416 ILE GLY VAL PHE GLU TRP ASP ALA PHE ALA LYS GLY THR
SEQRES 28 A 416 LYS ALA LEU MET ASP GLU VAL VAL LYS ALA THR SER ASN
SEQRES 29 A 416 GLY CYS VAL THR ILE ILE GLY GLY GLY ASP THR ALA THR
SEQRES 30 A 416 CYS CYS ALA LYS TRP GLY THR GLU ASP LYS VAL SER HIS
SEQRES 31 A 416 VAL SER THR GLY GLY GLY ALA SER LEU GLU LEU LEU GLU
SEQRES 32 A 416 GLY LYS ILE LEU PRO GLY VAL GLU ALA LEU SER ASN MET
HET 3PG A 500 11
HETNAM 3PG 3-PHOSPHOGLYCERIC ACID
FORMUL 2 3PG C3 H7 O7 P
FORMUL 3 HOH *289(H2 O)
HELIX 1 1 THR A 7 VAL A 11 5 5
HELIX 2 2 ASN A 36 ASN A 52 1 17
HELIX 3 3 MET A 71 SER A 76 1 6
HELIX 4 4 LEU A 77 ASN A 89 1 13
HELIX 5 5 GLY A 100 ASN A 109 1 10
HELIX 6 6 ASN A 120 HIS A 124 5 5
HELIX 7 7 ASP A 142 LYS A 155 1 14
HELIX 8 8 ALA A 164 ALA A 168 5 5
HELIX 9 9 HIS A 172 GLY A 177 1 6
HELIX 10 10 GLY A 186 LYS A 202 1 17
HELIX 11 11 VAL A 216 ASP A 218 5 3
HELIX 12 12 LYS A 219 LEU A 227 1 9
HELIX 13 13 GLY A 238 ASN A 249 1 12
HELIX 14 14 ASP A 258 THR A 263 1 6
HELIX 15 15 ILE A 264 ASN A 275 1 12
HELIX 16 16 GLY A 316 GLN A 329 1 14
HELIX 17 17 TRP A 344 PHE A 347 5 4
HELIX 18 18 ALA A 348 ASN A 364 1 17
HELIX 19 19 GLY A 373 TRP A 382 1 10
HELIX 20 20 GLY A 394 LEU A 402 1 9
HELIX 21 21 LEU A 407 ALA A 412 1 6
SHEET 1 A 6 ILE A 93 PHE A 94 0
SHEET 2 A 6 SER A 114 LEU A 117 1 O LEU A 117 N ILE A 93
SHEET 3 A 6 SER A 56 MET A 60 1 N LEU A 59 O ILE A 116
SHEET 4 A 6 ARG A 17 ARG A 21 1 N VAL A 18 O VAL A 58
SHEET 5 A 6 VAL A 159 ASN A 162 1 O VAL A 159 N ILE A 19
SHEET 6 A 6 LYS A 183 SER A 185 1 O ALA A 184 N TYR A 160
SHEET 1 B 2 MET A 28 LYS A 29 0
SHEET 2 B 2 GLN A 32 ILE A 33 -1 O GLN A 32 N LYS A 29
SHEET 1 C 2 LYS A 130 LYS A 132 0
SHEET 2 C 2 LYS A 138 SER A 140 -1 O ILE A 139 N GLY A 131
SHEET 1 D 6 LYS A 278 VAL A 280 0
SHEET 2 D 6 PHE A 232 GLY A 236 1 N MET A 233 O VAL A 280
SHEET 3 D 6 PHE A 207 GLY A 212 1 N LEU A 211 O ILE A 234
SHEET 4 D 6 LEU A 332 ASN A 336 1 O ASN A 336 N ILE A 210
SHEET 5 D 6 VAL A 367 ILE A 370 1 O ILE A 369 N ILE A 333
SHEET 6 D 6 HIS A 390 VAL A 391 1 O HIS A 390 N ILE A 370
SHEET 1 E 3 VAL A 297 THR A 301 0
SHEET 2 E 3 ASP A 284 GLY A 288 -1 N PHE A 285 O ALA A 300
SHEET 3 E 3 MET A 311 CYS A 315 -1 O LEU A 313 N VAL A 286
CISPEP 1 ARG A 205 PRO A 206 0 0.14
SITE 1 AC1 13 ASP A 23 ASN A 25 ARG A 38 HIS A 62
SITE 2 AC1 13 ARG A 65 ARG A 122 GLY A 166 ARG A 170
SITE 3 AC1 13 HOH A 580 HOH A 607 HOH A 634 HOH A 756
SITE 4 AC1 13 HOH A 763
CRYST1 42.100 64.300 72.200 90.00 97.80 90.00 P 1 21 1 2
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 0.023753 0.000000 0.003254 0.00000
SCALE2 0.000000 0.015552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013980 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
