| content |
HEADER PLANT PROTEIN 27-AUG-22 8EA1
TITLE STRUCTURE OF KUDZU 2-HYDROXYISOFLAVANONE DEHYDRATASE IN COMPLEX WITH
TITLE 2 P-NITROPHENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXYISOFLAVANONE DEHYDRATASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PUERARIA MONTANA VAR. LOBATA;
SOURCE 3 ORGANISM_COMMON: KUDZU VINE;
SOURCE 4 ORGANISM_TAXID: 3893;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS DEHYDRATASE, DEHYDRATION, CARBOXYLESTERASE, PUERARIA LOBATA, PLANT
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.PAN,X.WANG
REVDAT 1 30-NOV-22 8EA1 0
JRNL AUTH X.WANG,H.PAN,S.SAGURTHI,V.PARIS,C.ZHUO,R.A.DIXON
JRNL TITL THE PROTEIN CONFORMATIONAL BASIS OF ISOFLAVONE BIOSYNTHESIS.
JRNL REF COMMUN BIOL V. 5 1249 2022
JRNL REFN ESSN 2399-3642
JRNL PMID 36376429
JRNL DOI 10.1038/S42003-022-04222-X
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 19467
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 996
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 30.3600 - 4.3900 0.99 2751 130 0.1525 0.1690
REMARK 3 2 4.3800 - 3.4800 1.00 2652 155 0.1655 0.1744
REMARK 3 3 3.4800 - 3.0400 1.00 2635 141 0.2076 0.2138
REMARK 3 4 3.0400 - 2.7600 1.00 2639 132 0.2228 0.2724
REMARK 3 5 2.7600 - 2.5700 1.00 2606 148 0.2143 0.2452
REMARK 3 6 2.5700 - 2.4200 1.00 2588 148 0.2179 0.2630
REMARK 3 7 2.4200 - 2.2900 1.00 2600 142 0.2343 0.3163
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.285
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.719
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2522
REMARK 3 ANGLE : 1.127 3441
REMARK 3 CHIRALITY : 0.077 377
REMARK 3 PLANARITY : 0.005 450
REMARK 3 DIHEDRAL : 12.737 891
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4561 14.8051 -0.5435
REMARK 3 T TENSOR
REMARK 3 T11: 0.4604 T22: 0.4164
REMARK 3 T33: 0.3952 T12: 0.0191
REMARK 3 T13: 0.1019 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.2983 L22: 2.8179
REMARK 3 L33: 1.7315 L12: -0.1896
REMARK 3 L13: 0.0534 L23: -0.1662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0922 S12: -0.0955 S13: -0.0397
REMARK 3 S21: 0.6688 S22: -0.0338 S23: 0.3233
REMARK 3 S31: -0.1747 S32: -0.3729 S33: -0.0540
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8EA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1000268085.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19522
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 42.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2O7R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.1 M HEPES PH7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 23.42667
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 46.85333
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 46.85333
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 23.42667
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 MET A -27
REMARK 465 SER A -26
REMARK 465 TYR A -25
REMARK 465 TYR A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 LEU A -17
REMARK 465 GLU A -16
REMARK 465 SER A -15
REMARK 465 THR A -14
REMARK 465 SER A -13
REMARK 465 LEU A -12
REMARK 465 TYR A -11
REMARK 465 LYS A -10
REMARK 465 LYS A -9
REMARK 465 ALA A -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 ALA A -5
REMARK 465 ALA A -4
REMARK 465 ALA A -3
REMARK 465 PRO A -2
REMARK 465 PHE A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 GLU A 4
REMARK 465 ASN A 5
REMARK 465 SER A 6
REMARK 465 ASN A 7
REMARK 465 LYS A 8
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 9 CB CG CD OE1 OE2
REMARK 470 LYS A 22 CB CG CD CE NZ
REMARK 470 ASN A 185 CB CG OD1 ND2
REMARK 470 ASP A 216 CB CG OD1 OD2
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 GLU A 40 105.22 -168.63
REMARK 500 ASN A 56 109.50 -162.29
REMARK 500 GLU A 89 178.56 67.94
REMARK 500 THR A 168 -114.80 39.74
REMARK 500 CYS A 231 68.13 -154.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8EA1 A 1 325 UNP E9M5G1 E9M5G1_PUEML 1 325
SEQADV 8EA1 MET A -27 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 SER A -26 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 TYR A -25 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 TYR A -24 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 HIS A -23 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 HIS A -22 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 HIS A -21 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 HIS A -20 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 HIS A -19 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 HIS A -18 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 LEU A -17 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 GLU A -16 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 SER A -15 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 THR A -14 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 SER A -13 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 LEU A -12 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 TYR A -11 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 LYS A -10 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 LYS A -9 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 ALA A -8 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 GLY A -7 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 SER A -6 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 ALA A -5 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 ALA A -4 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 ALA A -3 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 PRO A -2 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 PHE A -1 UNP E9M5G1 EXPRESSION TAG
SEQADV 8EA1 THR A 0 UNP E9M5G1 EXPRESSION TAG
SEQRES 1 A 353 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 A 353 THR SER LEU TYR LYS LYS ALA GLY SER ALA ALA ALA PRO
SEQRES 3 A 353 PHE THR MET ALA ASN GLU ASN SER ASN LYS GLU ILE VAL
SEQRES 4 A 353 LYS GLU VAL LEU PRO LEU ILE ARG VAL TYR LYS ASP GLY
SEQRES 5 A 353 THR VAL GLU ARG LEU LEU SER SER PRO ASN VAL ALA ALA
SEQRES 6 A 353 SER PRO GLU ASP PRO GLU THR GLY VAL SER SER LYS ASP
SEQRES 7 A 353 ILE VAL ILE ALA HIS ASN PRO TYR VAL SER ALA ARG ILE
SEQRES 8 A 353 PHE LEU PRO ASN ILE ASN LYS SER HIS ASN LYS LEU PRO
SEQRES 9 A 353 ILE PHE VAL TYR PHE HIS GLY GLY ALA PHE CYS VAL GLU
SEQRES 10 A 353 SER ALA PHE SER PHE PHE VAL HIS ARG TYR LEU ASN ILE
SEQRES 11 A 353 LEU ALA SER GLN ALA ASN ILE ILE ALA VAL SER VAL ASP
SEQRES 12 A 353 PHE ARG LEU LEU PRO HIS HIS PRO LEU PRO ALA ALA TYR
SEQRES 13 A 353 GLU ASP GLY TRP THR THR LEU GLN TRP ILE ALA SER HIS
SEQRES 14 A 353 ALA ASN ASN THR ALA THR ASN PRO GLU PRO TRP LEU LEU
SEQRES 15 A 353 ASN HIS ALA ASP PHE ASN LYS LEU TYR VAL GLY GLY GLU
SEQRES 16 A 353 THR SER GLY ALA ASN LEU ALA HIS ASN LEU LEU LEU ARG
SEQRES 17 A 353 ALA GLY ASN GLY ASN GLN SER LEU PRO GLY ASP LEU LYS
SEQRES 18 A 353 ILE LEU GLY GLY LEU LEU CYS CYS PRO PHE PHE TRP GLY
SEQRES 19 A 353 SER LYS PRO ILE GLY SER GLU PRO VAL ASP GLU HIS GLU
SEQRES 20 A 353 GLN SER LEU ALA MET LYS VAL TRP ASN LEU ALA CYS PRO
SEQRES 21 A 353 ASP ALA PRO GLY GLY ILE ASP ASN PRO TRP ILE ASN PRO
SEQRES 22 A 353 CYS VAL ALA GLY ALA PRO SER LEU ALA THR LEU GLY CYS
SEQRES 23 A 353 SER LYS LEU LEU VAL THR ILE THR GLY ARG ASP GLU PHE
SEQRES 24 A 353 ARG ASP ARG ASP ILE LEU TYR HIS ASP THR VAL LYS LYS
SEQRES 25 A 353 SER GLY TRP GLU GLY GLN LEU GLU LEU PHE ASP ALA GLY
SEQRES 26 A 353 ASP GLU GLU HIS ALA PHE GLN LEU PHE LYS PRO GLU THR
SEQRES 27 A 353 ASP THR ALA LYS ALA MET ILE LYS ARG LEU ALA SER PHE
SEQRES 28 A 353 LEU VAL
HET NPO A3001 10
HETNAM NPO P-NITROPHENOL
FORMUL 2 NPO C6 H5 N O3
FORMUL 3 HOH *83(H2 O)
HELIX 1 AA1 SER A 93 ASN A 108 1 16
HELIX 2 AA2 PRO A 125 ASN A 143 1 19
HELIX 3 AA3 GLU A 150 HIS A 156 1 7
HELIX 4 AA4 THR A 168 GLY A 182 1 15
HELIX 5 AA5 LEU A 188 LEU A 192 5 5
HELIX 6 AA6 GLU A 217 GLN A 220 5 4
HELIX 7 AA7 SER A 221 CYS A 231 1 11
HELIX 8 AA8 GLY A 236 ASN A 240 5 5
HELIX 9 AA9 SER A 252 LEU A 256 5 5
HELIX 10 AB1 PHE A 271 LYS A 284 1 14
HELIX 11 AB2 ALA A 302 LYS A 307 1 6
HELIX 12 AB3 THR A 310 LEU A 324 1 15
SHEET 1 AA1 3 ILE A 10 VAL A 14 0
SHEET 2 AA1 3 ILE A 18 TYR A 21 -1 O VAL A 20 N LYS A 12
SHEET 3 AA1 3 VAL A 26 ARG A 28 -1 O GLU A 27 N ARG A 19
SHEET 1 AA2 8 SER A 47 ALA A 54 0
SHEET 2 AA2 8 VAL A 59 LEU A 65 -1 O LEU A 65 N SER A 47
SHEET 3 AA2 8 ILE A 110 ASP A 115 -1 O SER A 113 N ARG A 62
SHEET 4 AA2 8 LEU A 75 PHE A 81 1 N PHE A 78 O VAL A 112
SHEET 5 AA2 8 ALA A 157 GLU A 167 1 O TYR A 163 N ILE A 77
SHEET 6 AA2 8 GLY A 196 CYS A 200 1 O CYS A 200 N GLY A 166
SHEET 7 AA2 8 LYS A 260 ILE A 265 1 O LYS A 260 N GLY A 197
SHEET 8 AA2 8 GLN A 290 ASP A 295 1 O GLU A 292 N LEU A 261
CISPEP 1 LEU A 15 PRO A 16 0 2.69
CISPEP 2 ASN A 56 PRO A 57 0 -2.46
CISPEP 3 LEU A 119 PRO A 120 0 7.74
CISPEP 4 LEU A 124 PRO A 125 0 5.33
CRYST1 102.844 102.844 70.280 90.00 90.00 120.00 P 31 2 1 6
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 0.009723 0.005614 0.000000 0.00000
SCALE2 0.000000 0.011228 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014229 0.00000
TER 2443 VAL A 325
MASTER 291 0 1 12 11 0 0 6 2535 1 10 28
END |