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HEADER LYASE 06-FEB-08 3C6X
TITLE HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYNITRILASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: (S)-ACETONE-CYANOHYDRIN LYASE, (S)-HYDROXYNITRILE
COMPND 5 LYASE, OXYNITRILASE;
COMPND 6 EC: 4.1.2.37;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_COMMON: PARA RUBBER TREE;
SOURCE 4 GENE: HNL;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: BHIL-D2
KEYWDS ATOMIC RESOLUTION, HYDROXYNITRIL LYASE, CATALYSIS,
KEYWDS 2 PROTONATION STATE, AB INITIO CALCULATIONS, SUBSTRATE BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHMIDT
REVDAT 1 03-JUN-08 3C6X 0
JRNL AUTH A.SCHMIDT,K.GRUBER,C.KRATKY,V.S.LAMZIN
JRNL TITL ATOMIC RESOLUTION STRUCTURES AND QUANTUM CHEMISTRY
JRNL TITL 2 MEET TO REVEAL SUBTLETIES OF HYDROXYNITRILE LYASE
JRNL TITL 3 CATALYSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZUEGG,K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF ENZYME-SUBSTRATE
REMARK 1 TITL 2 COMPLEXES OF THE HYDROXYNITRILE LYASE FROM HEVEA
REMARK 1 TITL 3 BRASILIENSIS
REMARK 1 REF PROTEIN SCI. V. 8 1990 1999
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
REMARK 1 TITL ATOMIC RESOLUTION CRYSTAL STRUCTURE OF
REMARK 1 TITL 2 HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
REMARK 1 REF BIOL.CHEM. V. 380 993 1999
REMARK 1 REFN GE ISSN 1431-6730
REMARK 2
REMARK 2 RESOLUTION. 1.05 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) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 CROSS-VALIDATION METHOD : FREE R
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) : 0.105
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.105
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 145064
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.100
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)) : 129836
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4355
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 616
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2655.97
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2000.61
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 44
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 25692
REMARK 3 NUMBER OF RESTRAINTS : 31734
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.027
REMARK 3 ANGLE DISTANCES (A) : 0.034
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.031
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.092
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.100
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.126
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.042
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.107
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: FULL ANISOTROPIC REFINEMENT APPLIED
REMARK 4
REMARK 4 3C6X COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB046417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8430
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145064
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.050
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: REFMAC (RIGID BODY)
REMARK 200 STARTING MODEL: PDB ENTRY 1QJ4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG400, 2M AMMONIUM SULPHATE,
REMARK 280 0.1M HEPES-NA, PH7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 1/2+X,1/2-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.11000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.11000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 23.62550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.17150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.62550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.17150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.11000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.62550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.17150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.11000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.62550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.17150
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 19620 ANGSTROM**2
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -119 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 106.34300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2274 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2275 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2276 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2281 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2479 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A3036 LIES ON A SPECIAL POSITION.
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 1
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
REMARK 500 OE1 GLU A 66 O HOH A 2475 1.86
REMARK 500 OE2 GLU A 165 O HOH A 2358 2.11
REMARK 500 SG CYS A 113 O HOH A 2479 2.13
REMARK 500 O PRO A 45 O HOH A 2544 2.18
REMARK 500 OH TYR A 116 O3 SO4 A 1001 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 45 C ARG A 46 N 0.214
REMARK 500 CYS A 94 CB CYS A 94 SG -0.116
REMARK 500 CYS A 94 CB CYS A 94 SG -0.166
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 44 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 PRO A 45 CA - C - O ANGL. DEV. = 15.8 DEGREES
REMARK 500 ASP A 44 O - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 PRO A 45 C - N - CA ANGL. DEV. = 34.6 DEGREES
REMARK 500 PRO A 45 C - N - CD ANGL. DEV. = -39.7 DEGREES
REMARK 500 PRO A 45 CA - C - N ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG A 46 C - N - CA ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLU A 56 OE1 - CD - OE2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 PHE A 64 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 CYS A 94 CA - CB - SG ANGL. DEV. = 9.3 DEGREES
REMARK 500 TYR A 116 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR A 116 CG - CD1 - CE1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 GLY A 162 C - N - CA ANGL. DEV. = -14.4 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 GLU A 220 OE1 - CD - OE2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLU A 247 OE1 - CD - OE2 ANGL. DEV. = -7.9 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 SER A 80 -114.51 49.64
REMARK 500 ASN A 104 53.36 39.57
REMARK 500 LYS A 129 -122.07 63.62
REMARK 500 ILE A 209 -50.25 -124.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 44 PRO A 45 -148.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 44 -19.57
REMARK 500 PRO A 45 10.70
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 A2368 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH A2615 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A4017 DISTANCE = 5.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 1003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 1004
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 1005
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BME BINDING SITE FOR RESIDUE A 1006
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: PEG BINDING SITE FOR RESIDUE A 1501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QJ4 RELATED DB: PDB
REMARK 900 HNL AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 7YAS RELATED DB: PDB
REMARK 900 HNL LOW TEMPERATURE NATIVE STRUCTURE
REMARK 900 RELATED ID: 3C6Y RELATED DB: PDB
REMARK 900 HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION, COMPLEX
REMARK 900 WITH ACETONE
REMARK 900 RELATED ID: 3C6Z RELATED DB: PDB
REMARK 900 HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION, COMPLEX
REMARK 900 WITH ISOPROPANOL
REMARK 900 RELATED ID: 3C70 RELATED DB: PDB
REMARK 900 HNL FROM HEVEA BRASILIENSIS TO ATOMIC RESOLUTION, COMPLEX
REMARK 900 WITH RHODANIDE (SCN)
DBREF 3C6X A 1 257 UNP P52704 HNL_HEVBR 1 257
SEQRES 1 A 257 MET ALA PHE ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 A 257 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO LEU LEU
SEQRES 3 A 257 GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 257 ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU ILE GLY
SEQRES 5 A 257 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 257 GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 257 GLU SER CYS GLY GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 A 257 LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE HIS ASN
SEQRES 9 A 257 SER VAL LEU PRO ASP THR GLU HIS CYS PRO SER TYR VAL
SEQRES 10 A 257 VAL ASP LYS LEU MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 A 257 THR THR TYR PHE THR TYR THR LYS ASP GLY LYS GLU ILE
SEQRES 12 A 257 THR GLY LEU LYS LEU GLY PHE THR LEU LEU ARG GLU ASN
SEQRES 13 A 257 LEU TYR THR LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA
SEQRES 14 A 257 LYS MET LEU THR ARG LYS GLY SER LEU PHE GLN ASN ILE
SEQRES 15 A 257 LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY TYR GLY
SEQRES 16 A 257 SER ILE LYS LYS ILE TYR VAL TRP THR ASP GLN ASP GLU
SEQRES 17 A 257 ILE PHE LEU PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 A 257 TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP
SEQRES 19 A 257 HIS LYS LEU GLN LEU THR LYS THR LYS GLU ILE ALA GLU
SEQRES 20 A 257 ILE LEU GLN GLU VAL ALA ASP THR TYR ASN
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HET SO4 A1004 5
HET SO4 A1005 5
HET BME A1006 4
HET PEG A1501 7
HETNAM SO4 SULFATE ION
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 7 BME C2 H6 O S
FORMUL 8 PEG C4 H10 O3
FORMUL 9 HOH *604(H2 O)
HELIX 1 1 GLY A 15 HIS A 20 5 6
HELIX 2 2 LYS A 21 LEU A 29 1 9
HELIX 3 3 GLN A 47 ILE A 51 5 5
HELIX 4 4 SER A 53 SER A 58 1 6
HELIX 5 5 SER A 58 ALA A 67 1 10
HELIX 6 6 CYS A 81 CYS A 94 1 14
HELIX 7 7 SER A 115 PHE A 125 1 11
HELIX 8 8 GLY A 149 LEU A 157 1 9
HELIX 9 9 GLY A 162 THR A 173 1 12
HELIX 10 10 PHE A 179 ARG A 186 1 8
HELIX 11 11 GLY A 193 ILE A 197 5 5
HELIX 12 12 LEU A 211 TYR A 222 1 12
HELIX 13 13 LYS A 236 LYS A 241 1 6
HELIX 14 14 LYS A 241 TYR A 256 1 16
SHEET 1 A 6 LYS A 32 LEU A 36 0
SHEET 2 A 6 HIS A 5 ILE A 9 1 N LEU A 8 O THR A 34
SHEET 3 A 6 VAL A 74 SER A 80 1 O VAL A 77 N ILE A 9
SHEET 4 A 6 ILE A 97 SER A 105 1 O VAL A 101 N LEU A 76
SHEET 5 A 6 LYS A 199 TRP A 203 1 O VAL A 202 N PHE A 102
SHEET 6 A 6 LYS A 226 LYS A 229 1 O LYS A 226 N TYR A 201
SHEET 1 B 2 THR A 132 LYS A 138 0
SHEET 2 B 2 LYS A 141 LYS A 147 -1 O ILE A 143 N TYR A 136
LINK SG ACYS A 94 S2 BBME A1006 1555 1555 2.45
SITE 1 AC1 10 LYS A 23 LYS A 170 HOH A2030 HOH A2044
SITE 2 AC1 10 HOH A2123 HOH A2155 HOH A2286 HOH A2455
SITE 3 AC1 10 HOH A3040 HOH A3056
SITE 1 AC2 12 THR A 137 LYS A 138 ASP A 139 GLY A 140
SITE 2 AC2 12 GLY A 232 GLY A 233 LYS A 241 HOH A2208
SITE 3 AC2 12 HOH A2243 HOH A2320 HOH A2383 HOH A2386
SITE 1 AC3 5 THR A 110 GLY A 195 TYR A 222 HOH A2212
SITE 2 AC3 5 HOH A2454
SITE 1 AC4 6 LYS A 141 ASN A 181 LYS A 185 HOH A2086
SITE 2 AC4 6 HOH A2126 HOH A2152
SITE 1 AC5 9 TYR A 116 TRP A 217 LYS A 229 HOH A2090
SITE 2 AC5 9 HOH A2297 HOH A2400 HOH A2445 HOH A3028
SITE 3 AC5 9 HOH A4014
SITE 1 AC6 2 CYS A 94 GLU A 95
SITE 1 AC7 7 GLN A 47 LYS A 147 ARG A 174 LYS A 175
SITE 2 AC7 7 HOH A2147 HOH A2287 HOH A2417
CRYST1 47.251 106.343 128.220 90.00 90.00 90.00 C 2 2 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 0.021164 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009404 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007799 0.00000
END |