| content |
HEADER LYASE 22-FEB-06 2G4L
TITLE ANOMALOUS SUBSTRUCTURE OF HYDROXYNITRILE LYASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-ACETONE-CYANOHYDRIN LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: S-HYDROXYNITRILE LYASE, S-HYDROXYNITRILASE,
COMPND 5 OXYNITRILASE;
COMPND 6 EC: 4.1.2.39
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_COMMON: PARA RUBBER TREE
KEYWDS ANOMALOUS SUBSTRUCTURE OF HYDROXYNITRILE LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MUELLER-DIECKMANN,M.S.WEISS
REVDAT 1 20-FEB-07 2G4L 0
JRNL AUTH C.MUELLER-DIECKMANN,S.PANJIKAR,A.SCHMIDT,S.MUELLER,
JRNL AUTH 2 J.KUPER,A.GEERLOF,M.WILMANNS,R.K.SINGH,P.A.TUCKER,
JRNL AUTH 3 M.S.WEISS
JRNL TITL EFFICIENT DETERMINATION OF ANOMALOUS SUBSTRUCTURES
JRNL TITL 2 IN BIO-MACROMOLECULES USING LONGER X-RAY
JRNL TITL 3 WAVELENGTHS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27695
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 + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 600
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2022
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.3490
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2325
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -1.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.211
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2194 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1958 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2975 ; 1.598 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4607 ; 1.678 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 260 ; 6.011 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;37.941 ;25.258
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 388 ;13.252 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ; 8.237 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2365 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 418 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 426 ; 0.272 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1931 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1045 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1145 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 158 ; 0.131 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 5 ; 0.046 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 28 ; 0.185 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.133 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1680 ; 1.174 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 531 ; 0.265 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2110 ; 1.534 ; 2.500
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1070 ; 4.162 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 864 ; 5.443 ;10.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6001 43.7535 14.8506
REMARK 3 T TENSOR
REMARK 3 T11: -0.0871 T22: -0.0747
REMARK 3 T33: -0.1158 T12: -0.0126
REMARK 3 T13: -0.0117 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.8699 L22: 0.9684
REMARK 3 L33: 0.8998 L12: -0.0983
REMARK 3 L13: -0.0536 L23: -0.0431
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: -0.0858 S13: 0.0084
REMARK 3 S21: 0.0828 S22: -0.0030 S23: 0.0256
REMARK 3 S31: -0.0046 S32: -0.0329 S33: -0.0071
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. RESIDUE (A CME 94 ) AND RESIDUE (A GLU 95 )
REMARK 3 ARE NOT LINKED. DISTANCE OF C-N BOND IS 1.78.
REMARK 4
REMARK 4 2G4L COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-2006.
REMARK 100 THE RCSB ID CODE IS RCSB036680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
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 : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28295
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: FFT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 64.09000
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 64.09000
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 23.54500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.02500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.54500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.02500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.09000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.54500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.02500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.09000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.54500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.02500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 106.05000
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 194 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 196 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CME A 94 C - N - CA ANGL. DEV. = -9.2 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 80 -115.30 52.40
REMARK 500 LYS A 129 -119.99 60.35
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G4H RELATED DB: PDB
REMARK 900 RELATED ID: 2G4I RELATED DB: PDB
REMARK 900 RELATED ID: 2G4J RELATED DB: PDB
REMARK 900 RELATED ID: 2G4K RELATED DB: PDB
REMARK 900 RELATED ID: 2G4M RELATED DB: PDB
REMARK 900 RELATED ID: 2G4N RELATED DB: PDB
REMARK 900 RELATED ID: 2G4O RELATED DB: PDB
REMARK 900 RELATED ID: 2G4P RELATED DB: PDB
REMARK 900 RELATED ID: 2G4Q RELATED DB: PDB
REMARK 900 RELATED ID: 2G4R RELATED DB: PDB
REMARK 900 RELATED ID: 2G4S RELATED DB: PDB
REMARK 900 RELATED ID: 2G4T RELATED DB: PDB
REMARK 900 RELATED ID: 2G4U RELATED DB: PDB
REMARK 900 RELATED ID: 2G4V RELATED DB: PDB
REMARK 900 RELATED ID: 2G4W RELATED DB: PDB
REMARK 900 RELATED ID: 2G4X RELATED DB: PDB
REMARK 900 RELATED ID: 2G4Y RELATED DB: PDB
REMARK 900 RELATED ID: 2G4Z RELATED DB: PDB
REMARK 900 RELATED ID: 2G51 RELATED DB: PDB
REMARK 900 RELATED ID: 2G52 RELATED DB: PDB
REMARK 900 RELATED ID: 2G55 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 RESIDUE (A CME 94 ) AND RESIDUE (A GLU 95 ) ARE NOT LINKED.
REMARK 999 DISTANCE OF C-N BOND IS 1.78.
DBREF 2G4L A 1 257 UNP P52704 HNL_HEVBR 1 257
SEQADV 2G4L CME A 94 UNP P52704 CYS 94 MODIFIED RESIDUE
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 CME 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
MODRES 2G4L CME A 94 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 94 11
HET SO4 301 5
HET SO4 302 5
HET SO4 303 5
HET SO4 304 5
HET SO4 305 5
HET CL 306 1
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 1 CME C5 H11 N1 O3 S2
FORMUL 2 SO4 5(O4 S1 2-)
FORMUL 7 CL CL1 1-
FORMUL 8 HOH *181(H2 O1)
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 CME 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 ALA A 35 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 ILE A 75 N VAL A 7
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 ILE A 200 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
CRYST1 47.090 106.050 128.180 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 0.021236 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007802 0.00000
TER 2119 ASN A 257
MASTER 336 0 7 14 8 0 0 6 2325 1 36 20
END |