| content |
HEADER HYDROLASE 12-JUL-24 9CLR
TITLE HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS WITH SEVENTY-ONE
TITLE 2 MUTATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEVENTY-ONE-SUBSTITUTION VARIANTS OF HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_TAXID: 3981;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENGINEERED PROTEIN, ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.TAN,E.L.MEIXNER,A.NGUYEN,R.J.KAZLAUKAS,C.T.PIERCE,R.L.EVANS,K.SHI,
AUTHOR 2 H.AIHARA
REVDAT 1 18-DEC-24 9CLR 0
JRNL AUTH P.TAN,C.T.PIERCE,E.L.MEIXNER,A.NGUYEN,K.SHI,H.AIHARA,
JRNL AUTH 2 R.L.EVANS,R.J.KAZLAUKAS
JRNL TITL HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS WITH
JRNL TITL 2 SEVENTY-ONE MUTATIONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 36436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1815
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 42.4900 - 4.6800 1.00 3020 152 0.1912 0.1903
REMARK 3 2 4.6700 - 3.7100 0.95 2732 139 0.1637 0.1891
REMARK 3 3 3.7100 - 3.2400 0.87 2467 123 0.2149 0.2531
REMARK 3 4 3.2400 - 2.9500 1.00 2799 156 0.2252 0.2635
REMARK 3 5 2.9500 - 2.7300 1.00 2808 149 0.2326 0.2618
REMARK 3 6 2.7300 - 2.5700 0.90 2500 146 0.2199 0.2672
REMARK 3 7 2.5700 - 2.4400 1.00 2805 125 0.2288 0.2831
REMARK 3 8 2.4400 - 2.3400 1.00 2795 145 0.2455 0.3287
REMARK 3 9 2.3400 - 2.2500 1.00 2753 141 0.2598 0.3189
REMARK 3 10 2.2500 - 2.1700 0.87 2389 122 0.2846 0.3815
REMARK 3 11 2.1700 - 2.1000 0.99 2754 152 0.2941 0.3644
REMARK 3 12 2.1000 - 2.0400 0.80 2224 129 0.3064 0.3258
REMARK 3 13 2.0400 - 1.9900 0.93 2575 136 0.3260 0.3340
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.304
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.418
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.19
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 : 0.007 3828
REMARK 3 ANGLE : 0.899 5195
REMARK 3 CHIRALITY : 0.050 577
REMARK 3 PLANARITY : 0.006 654
REMARK 3 DIHEDRAL : 11.943 523
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 9CLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1000284606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.35-8.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36436
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 42.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 5.980
REMARK 200 R MERGE (I) : 0.99500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.87700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE HEXAHYDRATE, 25% W/V POLYETHYLENE GLYCOL 3,350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 24.98300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.72800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.37550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.72800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.98300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.37550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 1
REMARK 465 GLY A 142
REMARK 465 LYS A 143
REMARK 465 MET A 182
REMARK 465 GLU A 183
REMARK 465 ILE A 184
REMARK 465 LEU A 185
REMARK 465 ALA A 186
REMARK 465 LYS A 187
REMARK 465 ARG A 188
REMARK 465 ALA A 261
REMARK 465 ALA A 262
REMARK 465 LEU A 263
REMARK 465 GLU A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 MET B 1
REMARK 465 ASP B 141
REMARK 465 GLY B 142
REMARK 465 LYS B 143
REMARK 465 GLU B 144
REMARK 465 MET B 182
REMARK 465 GLU B 183
REMARK 465 ILE B 184
REMARK 465 LEU B 185
REMARK 465 ALA B 186
REMARK 465 LYS B 187
REMARK 465 ARG B 188
REMARK 465 ALA B 260
REMARK 465 ALA B 261
REMARK 465 ALA B 262
REMARK 465 LEU B 263
REMARK 465 GLU B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
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 LYS A 32 NZ
REMARK 470 LEU A 36 CD1 CD2
REMARK 470 LEU A 54 CD2
REMARK 470 ASP A 55 CB CG OD1 OD2
REMARK 470 GLU A 66 CG CD OE1 OE2
REMARK 470 GLU A 72 CG CD OE1 OE2
REMARK 470 LYS A 73 CE NZ
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 GLU A 95 CG CD OE1 OE2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 ASN A 122 ND2
REMARK 470 GLU A 123 OE2
REMARK 470 THR A 125 CG2
REMARK 470 GLU A 128 CB CG CD OE1 OE2
REMARK 470 ASN A 129 CB CG OD1 ND2
REMARK 470 LEU A 131 CD1 CD2
REMARK 470 GLN A 134 NE2
REMARK 470 LEU A 136 CG CD1 CD2
REMARK 470 THR A 139 OG1 CG2
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 ASP A 141 O CB CG OD1 OD2
REMARK 470 GLU A 144 CB CG CD OE1 OE2
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 LYS A 158 NZ
REMARK 470 LEU A 180 CD1 CD2
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 GLU A 194 OE1
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 GLU A 215 OE1
REMARK 470 LYS A 228 NZ
REMARK 470 GLU A 233 OE1
REMARK 470 LYS A 245 CD CE NZ
REMARK 470 GLU A 246 CG CD OE1 OE2
REMARK 470 ASN A 259 O
REMARK 470 ALA B 2 CB
REMARK 470 LEU B 29 CD2
REMARK 470 LYS B 32 NZ
REMARK 470 ILE B 48 CD1
REMARK 470 LEU B 54 CD1 CD2
REMARK 470 ASP B 55 CG OD1 OD2
REMARK 470 GLU B 72 CG CD OE1 OE2
REMARK 470 LYS B 73 CE NZ
REMARK 470 LYS B 92 CG CD CE NZ
REMARK 470 GLU B 95 CG CD OE1 OE2
REMARK 470 GLU B 119 CG CD OE1 OE2
REMARK 470 ASN B 122 ND2
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 ARG B 124 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 128 CG CD OE1 OE2
REMARK 470 GLN B 134 CG CD OE1 NE2
REMARK 470 LEU B 136 CG CD1 CD2
REMARK 470 THR B 139 CG2
REMARK 470 LYS B 140 C O CD CE NZ
REMARK 470 LYS B 153 CD CE NZ
REMARK 470 LYS B 158 CE NZ
REMARK 470 LEU B 162 CD2
REMARK 470 LEU B 180 CB CG CD1 CD2
REMARK 470 LYS B 193 CD CE NZ
REMARK 470 GLU B 194 CG CD OE1 OE2
REMARK 470 LYS B 200 CE NZ
REMARK 470 LYS B 210 NZ
REMARK 470 GLU B 215 CD OE1 OE2
REMARK 470 ARG B 218 NE CZ NH1 NH2
REMARK 470 GLU B 222 CG CD OE1 OE2
REMARK 470 LYS B 225 CG CD CE NZ
REMARK 470 ASP B 227 CG OD1 OD2
REMARK 470 LYS B 231 CD CE NZ
REMARK 470 GLU B 233 CG CD OE1 OE2
REMARK 470 GLU B 246 CG CD OE1 OE2
REMARK 470 GLU B 249 CD OE1 OE2
REMARK 470 ASN B 259 O CB CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 409 O HOH B 426 2.14
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 CYS A 13 -0.45 69.38
REMARK 500 HIS A 14 -169.54 -108.36
REMARK 500 SER A 80 -127.59 58.89
REMARK 500 ASP A 109 -166.84 -128.33
REMARK 500 LEU A 131 -126.59 52.04
REMARK 500 TYR A 224 87.33 -157.77
REMARK 500 MET A 238 58.64 -102.82
REMARK 500 ASN A 259 -159.28 -174.65
REMARK 500 PHE B 3 106.81 79.56
REMARK 500 SER B 80 -122.15 55.59
REMARK 500 LEU B 131 -119.98 50.50
REMARK 500 TYR B 224 85.13 -153.39
REMARK 500 MET B 238 52.02 -103.37
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 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 40 O
REMARK 620 2 PRO B 177 O 97.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 109 OD1
REMARK 620 2 CYS B 113 O 124.9
REMARK 620 3 HOH B 415 O 141.0 83.1
REMARK 620 N 1 2
DBREF 9CLR A 1 270 PDB 9CLR 9CLR 1 270
DBREF 9CLR B 1 270 PDB 9CLR 9CLR 1 270
SEQRES 1 A 270 MET ALA PHE ALA HIS PHE VAL LEU VAL HIS GLY ALA CYS
SEQRES 2 A 270 HIS GLY GLY TRP SER TRP HIS LYS LEU LYS PRO LEU LEU
SEQRES 3 A 270 GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 270 ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU LEU GLY
SEQRES 5 A 270 THR LEU ASP GLU TYR THR GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 270 GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 270 HIS SER LEU GLY GLY MET ASN LEU GLY ILE ALA ALA ASP
SEQRES 8 A 270 LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE LEU ALA
SEQRES 9 A 270 ALA PHE MET PRO ASP THR GLU HIS CYS SER SER PHE VAL
SEQRES 10 A 270 LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN TRP
SEQRES 11 A 270 LEU ASP THR GLN PHE LEU THR TYR THR LYS ASP GLY LYS
SEQRES 12 A 270 GLU ILE THR SER MET PHE PHE GLY PRO LYS PHE LEU ALA
SEQRES 13 A 270 HIS LYS LEU TYR GLN LEU CSO GLY PRO GLU ASP LEU GLU
SEQRES 14 A 270 LEU ALA SER MET LEU VAL ARG PRO SER SER LEU MET MET
SEQRES 15 A 270 GLU ILE LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY
SEQRES 16 A 270 TYR GLY SER ILE LYS LYS ILE TYR ILE VAL CYS THR GLU
SEQRES 17 A 270 ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN ILE
SEQRES 18 A 270 GLU ASN TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY
SEQRES 19 A 270 ALA ASP HIS MET ALA MET LEU CYS LYS THR LYS GLU LEU
SEQRES 20 A 270 ALA GLU ILE LEU GLN GLU VAL ALA ASP THR TYR ASN ALA
SEQRES 21 A 270 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 MET ALA PHE ALA HIS PHE VAL LEU VAL HIS GLY ALA CYS
SEQRES 2 B 270 HIS GLY GLY TRP SER TRP HIS LYS LEU LYS PRO LEU LEU
SEQRES 3 B 270 GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 B 270 ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU LEU GLY
SEQRES 5 B 270 THR LEU ASP GLU TYR THR GLU PRO LEU LEU THR PHE LEU
SEQRES 6 B 270 GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 B 270 HIS SER LEU GLY GLY MET ASN LEU GLY ILE ALA ALA ASP
SEQRES 8 B 270 LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE LEU ALA
SEQRES 9 B 270 ALA PHE MET PRO ASP THR GLU HIS CYS SER SER PHE VAL
SEQRES 10 B 270 LEU GLU GLN TYR ASN GLU ARG THR PRO ALA GLU ASN TRP
SEQRES 11 B 270 LEU ASP THR GLN PHE LEU THR TYR THR LYS ASP GLY LYS
SEQRES 12 B 270 GLU ILE THR SER MET PHE PHE GLY PRO LYS PHE LEU ALA
SEQRES 13 B 270 HIS LYS LEU TYR GLN LEU CSO GLY PRO GLU ASP LEU GLU
SEQRES 14 B 270 LEU ALA SER MET LEU VAL ARG PRO SER SER LEU MET MET
SEQRES 15 B 270 GLU ILE LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY
SEQRES 16 B 270 TYR GLY SER ILE LYS LYS ILE TYR ILE VAL CYS THR GLU
SEQRES 17 B 270 ASP LYS GLY ILE PRO GLU GLU PHE GLN ARG TRP GLN ILE
SEQRES 18 B 270 GLU ASN TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY
SEQRES 19 B 270 ALA ASP HIS MET ALA MET LEU CYS LYS THR LYS GLU LEU
SEQRES 20 B 270 ALA GLU ILE LEU GLN GLU VAL ALA ASP THR TYR ASN ALA
SEQRES 21 B 270 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET CSO A 163 7
HET CSO B 163 7
HET GOL A 401 6
HET MG A 402 1
HET MG A 403 1
HET MG B 301 1
HET MG B 302 1
HET MG B 303 1
HET CL B 304 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 3 GOL C3 H8 O3
FORMUL 4 MG 5(MG 2+)
FORMUL 9 CL CL 1-
FORMUL 10 HOH *59(H2 O)
HELIX 1 AA1 GLY A 15 HIS A 20 5 6
HELIX 2 AA2 LYS A 21 LEU A 29 1 9
HELIX 3 AA3 GLN A 47 LEU A 51 5 5
HELIX 4 AA4 THR A 53 THR A 58 1 6
HELIX 5 AA5 THR A 58 ALA A 67 1 10
HELIX 6 AA6 LEU A 81 TYR A 93 1 13
HELIX 7 AA7 SER A 115 THR A 125 1 11
HELIX 8 AA8 PRO A 126 LEU A 131 5 6
HELIX 9 AA9 GLY A 151 LEU A 159 1 9
HELIX 10 AB1 GLY A 164 VAL A 175 1 12
HELIX 11 AB2 GLY A 195 ILE A 199 5 5
HELIX 12 AB3 PRO A 213 TYR A 224 1 12
HELIX 13 AB4 MET A 238 LYS A 243 1 6
HELIX 14 AB5 LYS A 243 TYR A 258 1 16
HELIX 15 AB6 GLY B 15 HIS B 20 5 6
HELIX 16 AB7 LYS B 21 ALA B 28 1 8
HELIX 17 AB8 GLN B 47 LEU B 51 5 5
HELIX 18 AB9 THR B 53 THR B 58 1 6
HELIX 19 AC1 THR B 58 ALA B 67 1 10
HELIX 20 AC2 LEU B 81 CYS B 94 1 14
HELIX 21 AC3 SER B 115 ARG B 124 1 10
HELIX 22 AC4 PRO B 126 LEU B 131 5 6
HELIX 23 AC5 GLY B 151 LEU B 159 1 9
HELIX 24 AC6 GLY B 164 VAL B 175 1 12
HELIX 25 AC7 GLY B 195 ILE B 199 5 5
HELIX 26 AC8 PRO B 213 TYR B 224 1 12
HELIX 27 AC9 MET B 238 LYS B 243 1 6
HELIX 28 AD1 LYS B 243 TYR B 258 1 16
SHEET 1 AA1 6 LYS A 32 ALA A 35 0
SHEET 2 AA1 6 HIS A 5 VAL A 9 1 N LEU A 8 O THR A 34
SHEET 3 AA1 6 VAL A 74 HIS A 79 1 O VAL A 77 N VAL A 9
SHEET 4 AA1 6 ILE A 97 LEU A 103 1 O VAL A 101 N LEU A 76
SHEET 5 AA1 6 LYS A 201 CYS A 206 1 O ILE A 202 N PHE A 102
SHEET 6 AA1 6 LYS A 228 VAL A 232 1 O TYR A 230 N VAL A 205
SHEET 1 AA2 2 GLN A 134 TYR A 138 0
SHEET 2 AA2 2 ILE A 145 PHE A 149 -1 O SER A 147 N LEU A 136
SHEET 1 AA3 6 LYS B 32 ALA B 35 0
SHEET 2 AA3 6 HIS B 5 VAL B 9 1 N PHE B 6 O LYS B 32
SHEET 3 AA3 6 VAL B 74 HIS B 79 1 O VAL B 77 N VAL B 9
SHEET 4 AA3 6 ILE B 97 LEU B 103 1 O VAL B 101 N LEU B 76
SHEET 5 AA3 6 LYS B 201 CYS B 206 1 O ILE B 202 N PHE B 102
SHEET 6 AA3 6 LYS B 228 VAL B 232 1 O TYR B 230 N VAL B 205
SHEET 1 AA4 3 GLN B 134 THR B 137 0
SHEET 2 AA4 3 THR B 146 PHE B 149 -1 O SER B 147 N LEU B 136
SHEET 3 AA4 3 SER B 178 SER B 179 -1 O SER B 178 N MET B 148
LINK C LEU A 162 N CSO A 163 1555 1555 1.33
LINK C CSO A 163 N GLY A 164 1555 1555 1.33
LINK C LEU B 162 N CSO B 163 1555 1555 1.33
LINK C CSO B 163 N GLY B 164 1555 1555 1.33
LINK OD1 ASP A 37 MG MG A 403 1555 1555 2.65
LINK O CSO A 163 MG MG A 402 1555 1555 2.69
LINK O ALA B 40 MG MG B 302 1555 1555 2.61
LINK OD1 ASP B 109 MG MG B 303 1555 1555 2.67
LINK O CYS B 113 MG MG B 303 1555 1555 2.94
LINK O PRO B 177 MG MG B 302 1555 1555 2.94
LINK OH TYR B 224 MG MG B 301 1555 1555 2.66
LINK MG MG B 303 O HOH B 415 1555 1555 2.82
CRYST1 49.966 80.751 135.456 90.00 90.00 90.00 P 21 21 21 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 0.020014 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007382 0.00000
TER 1884 ALA A 260
TER 3725 ASN B 259
MASTER 393 0 9 28 17 0 0 6 3794 2 36 42
END |