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HEADER LYASE 29-APR-23 8J82
TITLE GAHNL-12GEN (ARTIFICIAL S-HYDROXYNITRILE LYASE GENERATED BY
TITLE 2 GAOPTIMIZER)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630
KEYWDS S-HYDROXYNITRILE LYASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.OZAWA,I.UNNO,R.SEKINE,S.ITO,S.NAKANO
REVDAT 1 03-APR-24 8J82 0
JRNL AUTH H.OZAWA,I.UNNO,R.SEKINE,T.CHISUGA,S.ITO,S.NAKANO
JRNL TITL DEVELOPMENT OF EVOLUTIONARY ALGORITHM-BASED PROTEIN REDESIGN
JRNL TITL 2 METHOD
JRNL REF CELL REP PHYS SCI V. 5 2024
JRNL REFN ESSN 2666-3864
JRNL DOI 10.1016/J.XCRP.2023.101758
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19_4092
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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 111946
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 5635
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 45.2100 - 5.2600 1.00 3823 187 0.1727 0.2016
REMARK 3 2 5.2600 - 4.1800 1.00 3666 188 0.1405 0.1587
REMARK 3 3 4.1700 - 3.6500 1.00 3615 179 0.1403 0.1531
REMARK 3 4 3.6500 - 3.3100 1.00 3569 199 0.1503 0.1769
REMARK 3 5 3.3100 - 3.0800 1.00 3606 174 0.1555 0.1770
REMARK 3 6 3.0800 - 2.9000 1.00 3566 199 0.1629 0.2209
REMARK 3 7 2.9000 - 2.7500 1.00 3579 180 0.1611 0.1822
REMARK 3 8 2.7500 - 2.6300 1.00 3539 187 0.1637 0.2118
REMARK 3 9 2.6300 - 2.5300 1.00 3576 151 0.1586 0.1893
REMARK 3 10 2.5300 - 2.4400 1.00 3559 186 0.1568 0.2143
REMARK 3 11 2.4400 - 2.3700 1.00 3545 198 0.1577 0.2038
REMARK 3 12 2.3700 - 2.3000 1.00 3530 179 0.1612 0.1929
REMARK 3 13 2.3000 - 2.2400 1.00 3525 205 0.1541 0.1900
REMARK 3 14 2.2400 - 2.1800 1.00 3524 195 0.1521 0.1951
REMARK 3 15 2.1800 - 2.1300 1.00 3454 230 0.1508 0.2053
REMARK 3 16 2.1300 - 2.0900 1.00 3546 187 0.1563 0.2239
REMARK 3 17 2.0900 - 2.0500 1.00 3483 202 0.1605 0.2021
REMARK 3 18 2.0500 - 2.0100 1.00 3556 181 0.1605 0.1842
REMARK 3 19 2.0100 - 1.9700 1.00 3545 165 0.1720 0.2173
REMARK 3 20 1.9700 - 1.9400 1.00 3532 172 0.1717 0.2510
REMARK 3 21 1.9400 - 1.9100 1.00 3494 181 0.1689 0.2375
REMARK 3 22 1.9100 - 1.8800 1.00 3536 159 0.1699 0.2181
REMARK 3 23 1.8800 - 1.8500 1.00 3496 221 0.1760 0.2145
REMARK 3 24 1.8500 - 1.8200 1.00 3473 200 0.1709 0.2400
REMARK 3 25 1.8200 - 1.8000 1.00 3543 162 0.1714 0.2218
REMARK 3 26 1.8000 - 1.7800 1.00 3510 204 0.1797 0.2436
REMARK 3 27 1.7800 - 1.7500 1.00 3457 216 0.1875 0.2339
REMARK 3 28 1.7500 - 1.7300 1.00 3518 164 0.1862 0.2904
REMARK 3 29 1.7300 - 1.7100 1.00 3527 159 0.1900 0.2373
REMARK 3 30 1.7100 - 1.6900 0.99 3419 225 0.2108 0.2482
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) : 0.161
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.081
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.11
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 : 0.006 8516
REMARK 3 ANGLE : 0.889 11552
REMARK 3 CHIRALITY : 0.058 1280
REMARK 3 PLANARITY : 0.007 1464
REMARK 3 DIHEDRAL : 6.698 1108
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 8J82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-23.
REMARK 100 THE DEPOSITION ID IS D_1300037397.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112048
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 45.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) POLYETHYLENE GLYCOL 3350,
REMARK 280 0.2 M POTASSIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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 42.87200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.51900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.19900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.51900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.87200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.19900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 LEU A 259
REMARK 465 GLU A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 LEU B 259
REMARK 465 GLU B 260
REMARK 465 HIS B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 LEU C 259
REMARK 465 GLU C 260
REMARK 465 HIS C 261
REMARK 465 HIS C 262
REMARK 465 HIS C 263
REMARK 465 HIS C 264
REMARK 465 HIS C 265
REMARK 465 HIS C 266
REMARK 465 LEU D 259
REMARK 465 GLU D 260
REMARK 465 HIS D 261
REMARK 465 HIS D 262
REMARK 465 HIS D 263
REMARK 465 HIS D 264
REMARK 465 HIS D 265
REMARK 465 HIS D 266
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 D 317 O HOH D 633 2.09
REMARK 500 O HOH D 358 O HOH D 618 2.10
REMARK 500 O HOH A 426 O HOH A 707 2.10
REMARK 500 O HOH A 325 O HOH A 600 2.12
REMARK 500 O HOH A 348 O HOH A 379 2.12
REMARK 500 O HOH C 337 O HOH C 377 2.13
REMARK 500 O HOH A 511 O HOH A 549 2.13
REMARK 500 O HOH C 513 O HOH C 561 2.13
REMARK 500 O HOH C 301 O HOH C 619 2.14
REMARK 500 O HOH A 415 O HOH A 621 2.14
REMARK 500 O HOH B 542 O HOH B 649 2.15
REMARK 500 O HOH D 347 O HOH D 384 2.15
REMARK 500 O HOH B 307 O HOH B 390 2.16
REMARK 500 O HOH A 622 O HOH A 636 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 341 O HOH C 604 4445 2.12
REMARK 500 O HOH A 642 O HOH D 312 4555 2.13
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 -23.32 83.77
REMARK 500 SER A 80 -114.14 54.45
REMARK 500 ASN A 104 53.04 38.07
REMARK 500 ASP A 109 -168.61 -123.95
REMARK 500 ARG A 129 -122.24 65.84
REMARK 500 TYR A 223 84.86 -152.17
REMARK 500 LYS A 237 66.52 -100.97
REMARK 500 CYS B 13 -21.84 80.27
REMARK 500 SER B 80 -113.17 52.22
REMARK 500 ASP B 109 -164.15 -127.42
REMARK 500 ARG B 129 -121.06 67.11
REMARK 500 THR B 140 30.02 -95.04
REMARK 500 CYS C 13 -23.17 79.87
REMARK 500 SER C 80 -112.55 56.96
REMARK 500 ASP C 109 -168.67 -123.40
REMARK 500 ARG C 129 -119.48 68.61
REMARK 500 CYS D 13 -22.68 80.02
REMARK 500 HIS D 14 -157.77 -91.67
REMARK 500 SER D 80 -111.07 54.90
REMARK 500 ASN D 104 53.10 37.35
REMARK 500 ARG D 129 -120.02 66.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 762 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 763 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A 764 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH B 699 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B 700 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B 701 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 702 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C 691 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 692 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH D 714 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH D 715 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH D 716 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH D 717 DISTANCE = 6.62 ANGSTROMS
DBREF 8J82 A 1 266 PDB 8J82 8J82 1 266
DBREF 8J82 B 1 266 PDB 8J82 8J82 1 266
DBREF 8J82 C 1 266 PDB 8J82 8J82 1 266
DBREF 8J82 D 1 266 PDB 8J82 8J82 1 266
SEQRES 1 A 266 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 A 266 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 A 266 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 A 266 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 A 266 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 266 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 A 266 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 A 266 LYS TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE HIS ASN
SEQRES 9 A 266 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR VAL
SEQRES 10 A 266 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 A 266 THR GLU TYR PHE THR TYR THR ASN ASN THR GLY GLU THR
SEQRES 12 A 266 ILE THR THR MET LYS LEU GLY PHE LYS LEU LEU ARG GLU
SEQRES 13 A 266 ASN LEU TYR THR LYS CYS THR ASP GLU GLU TYR GLU LEU
SEQRES 14 A 266 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 A 266 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 A 266 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 A 266 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 A 266 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 A 266 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 A 266 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA LEU GLU
SEQRES 21 A 266 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 266 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 B 266 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 B 266 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 B 266 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 B 266 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 B 266 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 B 266 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 B 266 LYS TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE HIS ASN
SEQRES 9 B 266 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR VAL
SEQRES 10 B 266 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 B 266 THR GLU TYR PHE THR TYR THR ASN ASN THR GLY GLU THR
SEQRES 12 B 266 ILE THR THR MET LYS LEU GLY PHE LYS LEU LEU ARG GLU
SEQRES 13 B 266 ASN LEU TYR THR LYS CYS THR ASP GLU GLU TYR GLU LEU
SEQRES 14 B 266 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 B 266 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 B 266 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 B 266 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 B 266 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 B 266 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 B 266 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA LEU GLU
SEQRES 21 B 266 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 266 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 C 266 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 C 266 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 C 266 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 C 266 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 C 266 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 C 266 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 C 266 LYS TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE HIS ASN
SEQRES 9 C 266 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR VAL
SEQRES 10 C 266 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 C 266 THR GLU TYR PHE THR TYR THR ASN ASN THR GLY GLU THR
SEQRES 12 C 266 ILE THR THR MET LYS LEU GLY PHE LYS LEU LEU ARG GLU
SEQRES 13 C 266 ASN LEU TYR THR LYS CYS THR ASP GLU GLU TYR GLU LEU
SEQRES 14 C 266 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 C 266 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 C 266 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 C 266 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 C 266 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 C 266 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 C 266 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA LEU GLU
SEQRES 21 C 266 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 266 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 D 266 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 D 266 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 D 266 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 D 266 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 D 266 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 D 266 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 D 266 LYS TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE HIS ASN
SEQRES 9 D 266 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR VAL
SEQRES 10 D 266 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 D 266 THR GLU TYR PHE THR TYR THR ASN ASN THR GLY GLU THR
SEQRES 12 D 266 ILE THR THR MET LYS LEU GLY PHE LYS LEU LEU ARG GLU
SEQRES 13 D 266 ASN LEU TYR THR LYS CYS THR ASP GLU GLU TYR GLU LEU
SEQRES 14 D 266 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 D 266 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 D 266 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 D 266 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 D 266 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 D 266 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 D 266 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA LEU GLU
SEQRES 21 D 266 HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *1675(H2 O)
HELIX 1 AA1 GLY A 15 HIS A 20 5 6
HELIX 2 AA2 LYS A 21 ALA A 29 1 9
HELIX 3 AA3 GLN A 47 ILE A 51 5 5
HELIX 4 AA4 SER A 53 SER A 58 1 6
HELIX 5 AA5 SER A 58 LEU A 68 1 11
HELIX 6 AA6 ALA A 82 VAL A 94 1 13
HELIX 7 AA7 SER A 115 PHE A 125 1 11
HELIX 8 AA8 GLY A 150 ASN A 157 1 8
HELIX 9 AA9 THR A 163 MET A 174 1 12
HELIX 10 AB1 PHE A 180 GLN A 186 1 7
HELIX 11 AB2 GLY A 194 ILE A 198 5 5
HELIX 12 AB3 LEU A 212 TYR A 223 1 12
HELIX 13 AB4 LYS A 237 LYS A 242 1 6
HELIX 14 AB5 LYS A 242 ALA A 258 1 17
HELIX 15 AB6 GLY B 15 HIS B 20 5 6
HELIX 16 AB7 LYS B 21 ALA B 29 1 9
HELIX 17 AB8 GLN B 47 ILE B 51 5 5
HELIX 18 AB9 SER B 53 SER B 58 1 6
HELIX 19 AC1 SER B 58 LEU B 68 1 11
HELIX 20 AC2 ALA B 82 ASP B 91 1 10
HELIX 21 AC3 LYS B 92 ASP B 95 5 4
HELIX 22 AC4 SER B 115 PHE B 125 1 11
HELIX 23 AC5 GLY B 150 ASN B 157 1 8
HELIX 24 AC6 THR B 163 MET B 174 1 12
HELIX 25 AC7 PHE B 180 GLN B 186 1 7
HELIX 26 AC8 GLY B 194 ILE B 198 5 5
HELIX 27 AC9 LEU B 212 TYR B 223 1 12
HELIX 28 AD1 LYS B 237 LYS B 242 1 6
HELIX 29 AD2 LYS B 242 ALA B 258 1 17
HELIX 30 AD3 GLY C 15 HIS C 20 5 6
HELIX 31 AD4 LYS C 21 ALA C 29 1 9
HELIX 32 AD5 GLN C 47 ILE C 51 5 5
HELIX 33 AD6 SER C 53 SER C 58 1 6
HELIX 34 AD7 SER C 58 LEU C 68 1 11
HELIX 35 AD8 ALA C 82 VAL C 94 1 13
HELIX 36 AD9 SER C 115 PHE C 125 1 11
HELIX 37 AE1 GLY C 150 ASN C 157 1 8
HELIX 38 AE2 THR C 163 MET C 174 1 12
HELIX 39 AE3 PHE C 180 ALA C 185 1 6
HELIX 40 AE4 GLY C 194 ILE C 198 5 5
HELIX 41 AE5 LEU C 212 TYR C 223 1 12
HELIX 42 AE6 LYS C 237 LYS C 242 1 6
HELIX 43 AE7 LYS C 242 ALA C 258 1 17
HELIX 44 AE8 GLY D 15 HIS D 20 5 6
HELIX 45 AE9 LYS D 21 ALA D 29 1 9
HELIX 46 AF1 GLN D 47 ILE D 51 5 5
HELIX 47 AF2 SER D 53 SER D 58 1 6
HELIX 48 AF3 SER D 58 SER D 67 1 10
HELIX 49 AF4 ALA D 82 TYR D 93 1 12
HELIX 50 AF5 SER D 115 PHE D 125 1 11
HELIX 51 AF6 GLY D 150 ASN D 157 1 8
HELIX 52 AF7 THR D 163 MET D 174 1 12
HELIX 53 AF8 PHE D 180 ALA D 185 1 6
HELIX 54 AF9 GLY D 194 ILE D 198 5 5
HELIX 55 AG1 LEU D 212 TYR D 223 1 12
HELIX 56 AG2 LYS D 237 LYS D 242 1 6
HELIX 57 AG3 LYS D 242 ALA D 258 1 17
SHEET 1 AA1 6 LYS A 32 LEU A 36 0
SHEET 2 AA1 6 HIS A 5 ILE A 9 1 N PHE A 6 O LYS A 32
SHEET 3 AA1 6 VAL A 74 GLU A 79 1 O VAL A 77 N ILE A 9
SHEET 4 AA1 6 ILE A 97 HIS A 103 1 O VAL A 101 N GLY A 78
SHEET 5 AA1 6 LYS A 200 TRP A 204 1 O ILE A 203 N PHE A 102
SHEET 6 AA1 6 LYS A 227 GLN A 230 1 O TYR A 229 N TYR A 202
SHEET 1 AA2 2 GLU A 132 THR A 137 0
SHEET 2 AA2 2 THR A 143 LYS A 148 -1 O ILE A 144 N TYR A 136
SHEET 1 AA3 6 LYS B 32 LEU B 36 0
SHEET 2 AA3 6 HIS B 5 ILE B 9 1 N LEU B 8 O THR B 34
SHEET 3 AA3 6 VAL B 74 GLU B 79 1 O VAL B 77 N ILE B 9
SHEET 4 AA3 6 ILE B 97 HIS B 103 1 O VAL B 101 N ILE B 76
SHEET 5 AA3 6 LYS B 200 TRP B 204 1 O ILE B 203 N PHE B 102
SHEET 6 AA3 6 LYS B 227 GLN B 230 1 O TYR B 229 N TYR B 202
SHEET 1 AA4 3 GLU B 132 THR B 137 0
SHEET 2 AA4 3 THR B 143 LYS B 148 -1 O ILE B 144 N TYR B 136
SHEET 3 AA4 3 GLY B 177 SER B 178 -1 O GLY B 177 N MET B 147
SHEET 1 AA5 6 LYS C 32 LEU C 36 0
SHEET 2 AA5 6 HIS C 5 ILE C 9 1 N LEU C 8 O THR C 34
SHEET 3 AA5 6 VAL C 74 GLU C 79 1 O VAL C 77 N ILE C 9
SHEET 4 AA5 6 ILE C 97 HIS C 103 1 O VAL C 101 N ILE C 76
SHEET 5 AA5 6 LYS C 200 TRP C 204 1 O VAL C 201 N PHE C 102
SHEET 6 AA5 6 LYS C 227 GLN C 230 1 O TYR C 229 N TYR C 202
SHEET 1 AA6 2 GLU C 132 THR C 137 0
SHEET 2 AA6 2 THR C 143 LYS C 148 -1 O ILE C 144 N TYR C 136
SHEET 1 AA7 6 LYS D 32 LEU D 36 0
SHEET 2 AA7 6 HIS D 5 ILE D 9 1 N PHE D 6 O LYS D 32
SHEET 3 AA7 6 VAL D 74 GLU D 79 1 O VAL D 77 N ILE D 9
SHEET 4 AA7 6 ILE D 97 HIS D 103 1 O VAL D 101 N ILE D 76
SHEET 5 AA7 6 LYS D 200 TRP D 204 1 O ILE D 203 N PHE D 102
SHEET 6 AA7 6 LYS D 227 GLN D 230 1 O TYR D 229 N TYR D 202
SHEET 1 AA8 2 GLU D 132 THR D 137 0
SHEET 2 AA8 2 THR D 143 LYS D 148 -1 O ILE D 144 N TYR D 136
CRYST1 85.744 86.398 135.038 90.00 90.00 90.00 P 21 21 21 16
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 0.011663 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007405 0.00000
TER 2078 ALA A 258
TER 4156 ALA B 258
TER 6234 ALA C 258
TER 8312 ALA D 258
MASTER 379 0 0 57 33 0 0 6 9983 4 0 84
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