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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 20-MAY-04 1VKH
TITLE CRYSTAL STRUCTURE OF PUTATIVE SERINE HYDROLASE (YDR428C)
TITLE 2 FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SERINE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 GENE: YDR428C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS YDR428C, PUTATIVE SERINE HYDROLASE, STRUCTURAL GENOMICS,
KEYWDS 2 JCSG
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS
REVDAT 1 08-JUN-04 1VKH 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE SERINE HYDROLASE
JRNL TITL 2 (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.9999
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39479
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2060
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2453
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1740
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4659
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.127
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.233
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4282 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3868 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5801 ; 1.698 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9055 ; 0.909 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 505 ; 5.771 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 203 ;40.422 ;25.271
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 782 ;13.328 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.530 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 669 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4625 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 811 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 955 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4037 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2356 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 424 ; 0.170 ; 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): 26 ; 0.245 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 71 ; 0.266 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.237 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 2801 ; 1.496 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1030 ; 0.373 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4214 ; 1.659 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1876 ; 3.072 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1587 ; 4.247 ; 4.500
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 : 2
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 7 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6850 31.7140 73.8620
REMARK 3 T TENSOR
REMARK 3 T11: -0.1074 T22: -0.2667
REMARK 3 T33: -0.2105 T12: -0.0010
REMARK 3 T13: 0.0052 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.6720 L22: 0.5367
REMARK 3 L33: 1.1790 L12: 0.1523
REMARK 3 L13: -0.0172 L23: -0.0587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: -0.0893 S13: -0.0363
REMARK 3 S21: 0.0354 S22: -0.0006 S23: -0.0654
REMARK 3 S31: 0.0542 S32: -0.0167 S33: 0.0147
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 261
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0750 37.6100 41.8350
REMARK 3 T TENSOR
REMARK 3 T11: -0.1262 T22: -0.2414
REMARK 3 T33: -0.2004 T12: -0.0111
REMARK 3 T13: 0.0130 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.9365 L22: 0.8011
REMARK 3 L33: 1.7341 L12: 0.0487
REMARK 3 L13: 0.0372 L23: 0.1341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0503 S12: 0.1310 S13: -0.0146
REMARK 3 S21: -0.0491 S22: 0.0193 S23: -0.0483
REMARK 3 S31: -0.0038 S32: -0.0144 S33: -0.0696
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS 2. NON-ROTOMERS: LEU 156 AND LEU 160
REMARK 3 (MOLECULE A AND B).
REMARK 4
REMARK 4 1VKH COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-2004.
REMARK 100 THE RCSB ID CODE IS RCSB001951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-2003
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 : APS
REMARK 200 BEAMLINE : 8BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9464, 0.979326, 0.979179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42225
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 : 3.890
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 FOR THE DATA SET : 17.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.57
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34300
REMARK 200 FOR SHELL : 3.570
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.00% PEG MME 2000, 0.10M HEPES,
REMARK 280 0.00M HEPES_NA, 5% GLYCEROL , VAPOR DIFFUSION,SITTING DROP,
REMARK 280 NANODROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 42.97950
REMARK 290 SMTRY3 2 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 2 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, 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 THR B 4
REMARK 465 VAL B 5
REMARK 465 ARG B 6
REMARK 465 ALA B 7
REMARK 465 ILE B 8
REMARK 465 SER B 9
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 ARG A 6 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN A 26 CG CD OE1 NE2
REMARK 470 ARG A 29 NE CZ NH1 NH2
REMARK 470 ARG B 29 NE CZ NH1 NH2
REMARK 470 GLU B 78 CG CD OE1 OE2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLONING ARTIFACT. THE CONSTRUCT WAS PCR AMPLIFIED WITH
REMARK 999 TAQ POLYMERASE. SEQUENCING OF THE CLONED CONSTRUCT
REMARK 999 INDICATED THAT VAL IN POSITION 161 WAS MUTATED TO ILE.
DBREF 1VKH A 1 261 GB 6320636 NP_010716 1 261
DBREF 1VKH B 1 261 GB 6320636 NP_010716 1 261
SEQADV 1VKH MET A -11 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH GLY A -10 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH SER A -9 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH ASP A -8 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH LYS A -7 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH ILE A -6 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS A -5 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS A -4 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS A -3 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS A -2 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS A -1 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS A 0 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH MSE A 1 GB 6320636 MET 1 MODIFIED RESIDUE
SEQADV 1VKH MSE A 60 GB 6320636 MET 60 MODIFIED RESIDUE
SEQADV 1VKH MSE A 106 GB 6320636 MET 106 MODIFIED RESIDUE
SEQADV 1VKH MSE A 130 GB 6320636 MET 130 MODIFIED RESIDUE
SEQADV 1VKH MSE A 137 GB 6320636 MET 137 MODIFIED RESIDUE
SEQADV 1VKH ILE A 161 GB 6320636 VAL 161 SEE REMARK 999
SEQADV 1VKH MSE A 180 GB 6320636 MET 180 MODIFIED RESIDUE
SEQADV 1VKH MSE A 189 GB 6320636 MET 189 MODIFIED RESIDUE
SEQADV 1VKH MSE A 203 GB 6320636 MET 203 MODIFIED RESIDUE
SEQADV 1VKH MET B -11 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH GLY B -10 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH SER B -9 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH ASP B -8 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH LYS B -7 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH ILE B -6 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS B -5 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS B -4 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS B -3 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS B -2 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS B -1 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH HIS B 0 GB 6320636 LEADER SEQUENCE
SEQADV 1VKH MSE B 1 GB 6320636 MET 1 MODIFIED RESIDUE
SEQADV 1VKH MSE B 60 GB 6320636 MET 60 MODIFIED RESIDUE
SEQADV 1VKH MSE B 106 GB 6320636 MET 106 MODIFIED RESIDUE
SEQADV 1VKH MSE B 130 GB 6320636 MET 130 MODIFIED RESIDUE
SEQADV 1VKH MSE B 137 GB 6320636 MET 137 MODIFIED RESIDUE
SEQADV 1VKH ILE B 161 GB 6320636 VAL 161 SEE REMARK 999
SEQADV 1VKH MSE B 180 GB 6320636 MET 180 MODIFIED RESIDUE
SEQADV 1VKH MSE B 189 GB 6320636 MET 189 MODIFIED RESIDUE
SEQADV 1VKH MSE B 203 GB 6320636 MET 203 MODIFIED RESIDUE
SEQRES 1 A 273 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 273 SER ASN THR VAL ARG ALA ILE SER PRO ASP ILE THR LEU
SEQRES 3 A 273 PHE ASN LYS THR LEU THR PHE GLN GLU ILE SER GLN ASN
SEQRES 4 A 273 THR ARG GLU ALA VAL ILE TYR ILE HIS GLY GLY ALA TRP
SEQRES 5 A 273 ASN ASP PRO GLU ASN THR PRO ASN ASP PHE ASN GLN LEU
SEQRES 6 A 273 ALA ASN THR ILE LYS SER MSE ASP THR GLU SER THR VAL
SEQRES 7 A 273 CYS GLN TYR SER ILE GLU TYR ARG LEU SER PRO GLU ILE
SEQRES 8 A 273 THR ASN PRO ARG ASN LEU TYR ASP ALA VAL SER ASN ILE
SEQRES 9 A 273 THR ARG LEU VAL LYS GLU LYS GLY LEU THR ASN ILE ASN
SEQRES 10 A 273 MSE VAL GLY HIS SER VAL GLY ALA THR PHE ILE TRP GLN
SEQRES 11 A 273 ILE LEU ALA ALA LEU LYS ASP PRO GLN GLU LYS MSE SER
SEQRES 12 A 273 GLU ALA GLN LEU GLN MSE LEU GLY LEU LEU GLN ILE VAL
SEQRES 13 A 273 LYS ARG VAL PHE LEU LEU ASP GLY ILE TYR SER LEU LYS
SEQRES 14 A 273 GLU LEU LEU ILE GLU TYR PRO GLU TYR ASP CYS PHE THR
SEQRES 15 A 273 ARG LEU ALA PHE PRO ASP GLY ILE GLN MSE TYR GLU GLU
SEQRES 16 A 273 GLU PRO SER ARG VAL MSE PRO TYR VAL LYS LYS ALA LEU
SEQRES 17 A 273 SER ARG PHE SER ILE ASP MSE HIS LEU VAL HIS SER TYR
SEQRES 18 A 273 SER ASP GLU LEU LEU THR LEU ARG GLN THR ASN CYS LEU
SEQRES 19 A 273 ILE SER CYS LEU GLN ASP TYR GLN LEU SER PHE LYS LEU
SEQRES 20 A 273 TYR LEU ASP ASP LEU GLY LEU HIS ASN ASP VAL TYR LYS
SEQRES 21 A 273 ASN GLY LYS VAL ALA LYS TYR ILE PHE ASP ASN ILE CYS
SEQRES 1 B 273 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 273 SER ASN THR VAL ARG ALA ILE SER PRO ASP ILE THR LEU
SEQRES 3 B 273 PHE ASN LYS THR LEU THR PHE GLN GLU ILE SER GLN ASN
SEQRES 4 B 273 THR ARG GLU ALA VAL ILE TYR ILE HIS GLY GLY ALA TRP
SEQRES 5 B 273 ASN ASP PRO GLU ASN THR PRO ASN ASP PHE ASN GLN LEU
SEQRES 6 B 273 ALA ASN THR ILE LYS SER MSE ASP THR GLU SER THR VAL
SEQRES 7 B 273 CYS GLN TYR SER ILE GLU TYR ARG LEU SER PRO GLU ILE
SEQRES 8 B 273 THR ASN PRO ARG ASN LEU TYR ASP ALA VAL SER ASN ILE
SEQRES 9 B 273 THR ARG LEU VAL LYS GLU LYS GLY LEU THR ASN ILE ASN
SEQRES 10 B 273 MSE VAL GLY HIS SER VAL GLY ALA THR PHE ILE TRP GLN
SEQRES 11 B 273 ILE LEU ALA ALA LEU LYS ASP PRO GLN GLU LYS MSE SER
SEQRES 12 B 273 GLU ALA GLN LEU GLN MSE LEU GLY LEU LEU GLN ILE VAL
SEQRES 13 B 273 LYS ARG VAL PHE LEU LEU ASP GLY ILE TYR SER LEU LYS
SEQRES 14 B 273 GLU LEU LEU ILE GLU TYR PRO GLU TYR ASP CYS PHE THR
SEQRES 15 B 273 ARG LEU ALA PHE PRO ASP GLY ILE GLN MSE TYR GLU GLU
SEQRES 16 B 273 GLU PRO SER ARG VAL MSE PRO TYR VAL LYS LYS ALA LEU
SEQRES 17 B 273 SER ARG PHE SER ILE ASP MSE HIS LEU VAL HIS SER TYR
SEQRES 18 B 273 SER ASP GLU LEU LEU THR LEU ARG GLN THR ASN CYS LEU
SEQRES 19 B 273 ILE SER CYS LEU GLN ASP TYR GLN LEU SER PHE LYS LEU
SEQRES 20 B 273 TYR LEU ASP ASP LEU GLY LEU HIS ASN ASP VAL TYR LYS
SEQRES 21 B 273 ASN GLY LYS VAL ALA LYS TYR ILE PHE ASP ASN ILE CYS
MODRES 1VKH MSE A 1 MET SELENOMETHIONINE
MODRES 1VKH MSE A 60 MET SELENOMETHIONINE
MODRES 1VKH MSE A 106 MET SELENOMETHIONINE
MODRES 1VKH MSE A 130 MET SELENOMETHIONINE
MODRES 1VKH MSE A 137 MET SELENOMETHIONINE
MODRES 1VKH MSE A 180 MET SELENOMETHIONINE
MODRES 1VKH MSE A 189 MET SELENOMETHIONINE
MODRES 1VKH MSE A 203 MET SELENOMETHIONINE
MODRES 1VKH MSE B 60 MET SELENOMETHIONINE
MODRES 1VKH MSE B 106 MET SELENOMETHIONINE
MODRES 1VKH MSE B 130 MET SELENOMETHIONINE
MODRES 1VKH MSE B 137 MET SELENOMETHIONINE
MODRES 1VKH MSE B 180 MET SELENOMETHIONINE
MODRES 1VKH MSE B 189 MET SELENOMETHIONINE
MODRES 1VKH MSE B 203 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 60 8
HET MSE A 106 12
HET MSE A 130 8
HET MSE A 137 8
HET MSE A 180 8
HET MSE A 189 8
HET MSE A 203 8
HET MSE B 60 8
HET MSE B 106 12
HET MSE B 130 8
HET MSE B 137 8
HET MSE B 180 8
HET MSE B 189 8
HET MSE B 203 12
HET CL 455 2
HET GOL 456 6
HET GOL 457 6
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
FORMUL 1 MSE 15(C5 H11 N1 O2 SE1)
FORMUL 3 CL CL1 1-
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 HOH *454(H2 O1)
HELIX 1 1 LEU A 14 THR A 18 5 5
HELIX 2 2 THR A 46 ASP A 49 5 4
HELIX 3 3 PHE A 50 ASP A 61 1 12
HELIX 4 4 PRO A 82 GLY A 100 1 19
HELIX 5 5 SER A 110 ALA A 121 1 12
HELIX 6 6 ALA A 122 ASP A 125 5 4
HELIX 7 7 SER A 131 GLN A 142 1 12
HELIX 8 8 SER A 155 TYR A 163 1 9
HELIX 9 9 TYR A 166 PHE A 174 1 9
HELIX 10 10 GLY A 177 TYR A 181 5 5
HELIX 11 11 GLU A 184 SER A 200 1 17
HELIX 12 12 LEU A 216 TYR A 229 1 14
HELIX 13 13 LEU A 242 LYS A 248 5 7
HELIX 14 14 ASN A 249 ASN A 259 1 11
HELIX 15 15 LEU B 14 THR B 18 5 5
HELIX 16 16 THR B 46 ASP B 49 5 4
HELIX 17 17 PHE B 50 ASP B 61 1 12
HELIX 18 18 PRO B 82 GLY B 100 1 19
HELIX 19 19 SER B 110 ALA B 121 1 12
HELIX 20 20 ALA B 122 ASP B 125 5 4
HELIX 21 21 SER B 131 GLN B 142 1 12
HELIX 22 22 SER B 155 TYR B 163 1 9
HELIX 23 23 TYR B 166 PHE B 174 1 9
HELIX 24 24 GLY B 177 TYR B 181 5 5
HELIX 25 25 GLU B 184 SER B 200 1 17
HELIX 26 26 LEU B 216 TYR B 229 1 14
HELIX 27 27 LEU B 242 LYS B 248 5 7
HELIX 28 28 ASN B 249 ASN B 259 1 11
SHEET 1 A14 LEU A 19 GLN A 22 0
SHEET 2 A14 VAL A 66 ILE A 71 -1 O GLN A 68 N GLN A 22
SHEET 3 A14 GLU A 30 ILE A 35 1 N TYR A 34 O TYR A 69
SHEET 4 A14 ILE A 104 HIS A 109 1 O VAL A 107 N ILE A 33
SHEET 5 A14 VAL A 144 LEU A 150 1 O LYS A 145 N ILE A 104
SHEET 6 A14 ASP A 202 SER A 208 1 O HIS A 204 N LEU A 149
SHEET 7 A14 PHE A 233 ASP A 238 1 O LYS A 234 N LEU A 205
SHEET 8 A14 PHE B 233 ASP B 238 -1 O PHE B 233 N LEU A 237
SHEET 9 A14 ASP B 202 SER B 208 1 N LEU B 205 O LYS B 234
SHEET 10 A14 VAL B 144 LEU B 150 1 N LEU B 149 O HIS B 204
SHEET 11 A14 ILE B 104 HIS B 109 1 N GLY B 108 O LEU B 150
SHEET 12 A14 GLU B 30 ILE B 35 1 N ILE B 33 O ASN B 105
SHEET 13 A14 VAL B 66 ILE B 71 1 O TYR B 69 N TYR B 34
SHEET 14 A14 LEU B 19 GLN B 22 -1 N LEU B 19 O SER B 70
CISPEP 1 SER A 9 PRO A 10 0 -11.49
CISPEP 2 SER A 76 PRO A 77 0 7.00
CISPEP 3 ASN A 81 PRO A 82 0 1.42
CISPEP 4 SER B 76 PRO B 77 0 13.13
CISPEP 5 ASN B 81 PRO B 82 0 5.17
CRYST1 41.967 85.959 70.479 90.00 97.71 90.00 P 1 21 1 4
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 0.023828 0.000000 0.003226 0.00000
SCALE2 0.000000 0.011633 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014318 0.00000
TER 2121 CYS A 261
TER 4189 CYS B 261
MASTER 308 0 18 28 14 0 0 6 4659 2 144 42
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