HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 18-JUL-07 2QNG
TITLE CRYSTAL STRUCTURE OF UNKNOWN FUNCTION PROTEIN SAV2460
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN SAV2460;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AVERMITILIS;
SOURCE 3 ORGANISM_TAXID: 33903;
SOURCE 4 STRAIN: DSM 46492, JCM 5070, NCIMB 12804, NRRL 8165;
SOURCE 5 ATCC: 31267;
SOURCE 6 GENE: SAV2460;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) DERIVATIVE;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PET DERIVATIVE
KEYWDS STREPTOMYCES AVERMITILIS, STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 3 UNCHARACTERIZED PROTEIN, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,X.XU,H.ZHENG,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 5 08-FEB-17 2QNG 1 JRNL
REVDAT 4 14-DEC-16 2QNG 1 TITLE VERSN
REVDAT 3 24-FEB-09 2QNG 1 VERSN
REVDAT 2 14-AUG-07 2QNG 1 AUTHOR JRNL
REVDAT 1 31-JUL-07 2QNG 0
JRNL AUTH C.CHANG,X.XU,H.ZHENG,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF SAV2460.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 31877
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1706
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2257
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1310
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.070
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.782
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1454 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1991 ; 1.413 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 197 ; 5.449 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 73 ;30.742 ;22.740
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 233 ;13.365 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.690 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 210 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1170 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 643 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1000 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 127 ; 0.162 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 11 ; 0.114 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 26 ; 0.207 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.080 ; 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): 921 ; 1.446 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1452 ; 2.047 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 607 ; 2.845 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 528 ; 3.705 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1528 ; 1.863 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 161 ; 6.641 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1408 ; 3.040 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2QNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-07.
REMARK 100 THE RCSB ID CODE IS RCSB043818.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33631
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.960
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 0.2M CACL2, 25%
REMARK 280 PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
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,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 20.35050
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MSE A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ASN A 2
REMARK 465 GLY A 3
REMARK 465 LEU A 4
REMARK 465 ASN A 5
REMARK 465 ASP A 176
REMARK 465 SER A 177
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 A 252 O HOH A 327 1.92
REMARK 500 O HOH A 252 O HOH A 298 2.11
REMARK 500 OE2 GLU A 76 O HOH A 245 2.18
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 ASP A 40 57.98 -176.99
REMARK 500 ASP A 68 -6.16 -148.61
REMARK 500 ALA A 103 140.94 -177.28
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 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 17 O
REMARK 620 2 GLY A 69 O 85.8
REMARK 620 3 GLY A 71 O 159.6 95.3
REMARK 620 4 ASP A 75 OD1 121.4 84.0 79.0
REMARK 620 5 ASP A 75 OD2 77.0 106.8 121.8 51.9
REMARK 620 6 HOH A 208 O 91.9 169.4 83.2 106.0 82.7
REMARK 620 7 HOH A 204 O 80.6 86.4 79.1 155.1 152.9 83.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 28 OD1
REMARK 620 2 LEU A 29 O 88.8
REMARK 620 3 ASP A 30 OD1 89.1 83.0
REMARK 620 4 SER A 66 O 81.6 109.5 164.1
REMARK 620 5 GLU A 76 OE1 160.8 78.9 103.7 88.7
REMARK 620 6 GLU A 76 OE2 157.5 85.0 111.4 80.2 9.1
REMARK 620 7 HOH A 217 O 104.3 157.4 79.0 90.8 92.3 89.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC7410 RELATED DB: TARGETDB
DBREF 2QNG A 1 177 UNP Q82KE3 Q82KE3_STRAW 1 177
SEQADV 2QNG MSE A -21 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG GLY A -20 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG SER A -19 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG SER A -18 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A -17 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A -16 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A -15 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A -14 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A -13 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A -12 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG SER A -11 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG SER A -10 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG GLY A -9 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG ARG A -8 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG GLU A -7 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG ASN A -6 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG LEU A -5 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG TYR A -4 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG PHE A -3 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG GLN A -2 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG GLY A -1 UNP Q82KE3 CLONING ARTIFACT
SEQADV 2QNG HIS A 0 UNP Q82KE3 CLONING ARTIFACT
SEQRES 1 A 199 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 199 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ASN GLY LEU
SEQRES 3 A 199 ASN LYS GLY ILE ARG LYS VAL GLU LEU ALA VAL LYS TRP
SEQRES 4 A 199 ASP PRO SER PRO PRO GLY ASP PRO ALA THR ASP LEU ASP
SEQRES 5 A 199 ILE VAL ALA ALA THR PHE LEU ALA GLY ASP ALA TYR GLY
SEQRES 6 A 199 LYS PRO ALA TYR VAL VAL HIS PHE ASP SER ARG SER PRO
SEQRES 7 A 199 ASP GLY THR ILE TYR LEU ASN ARG ASP SER LYS ASP GLY
SEQRES 8 A 199 LYS GLY PHE GLY TRP ASP GLU VAL MSE THR LEU GLU LEU
SEQRES 9 A 199 ASN ARG LEU ASP SER ARG TYR ALA ARG VAL VAL VAL GLY
SEQRES 10 A 199 VAL VAL ILE GLN GLN ARG ASP ALA HIS ARG THR PHE VAL
SEQRES 11 A 199 GLY VAL LEU ASN PRO GLY LEU ARG MSE ARG GLU GLY TYR
SEQRES 12 A 199 THR VAL LEU ALA GLU ASP ASP PHE GLY GLY VAL LEU GLY
SEQRES 13 A 199 SER THR ALA ALA THR VAL GLY GLU PHE VAL ARG ASP ASP
SEQRES 14 A 199 SER GLY GLU TRP THR PHE HIS PRO GLY ILE HIS GLY TYR
SEQRES 15 A 199 ASP SER ASP PRO ALA THR PHE ALA ARG VAL MSE GLY GLY
SEQRES 16 A 199 ARG GLN ASP SER
MODRES 2QNG MSE A 78 MET SELENOMETHIONINE
MODRES 2QNG MSE A 117 MET SELENOMETHIONINE
MODRES 2QNG MSE A 171 MET SELENOMETHIONINE
HET MSE A 78 13
HET MSE A 117 13
HET MSE A 171 8
HET CA A 201 1
HET CA A 202 1
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 CA 2(CA 2+)
FORMUL 4 HOH *159(H2 O)
HELIX 1 1 GLY A 39 ALA A 41 5 3
HELIX 2 2 LEU A 82 LEU A 85 5 4
HELIX 3 3 THR A 106 VAL A 110 5 5
HELIX 4 4 ASP A 163 MSE A 171 1 9
SHEET 1 A 5 ILE A 60 ARG A 64 0
SHEET 2 A 5 GLU A 76 LEU A 80 -1 O THR A 79 N TYR A 61
SHEET 3 A 5 VAL A 11 ASP A 18 -1 N VAL A 11 O LEU A 80
SHEET 4 A 5 LEU A 111 GLU A 119 -1 O ARG A 116 N ALA A 14
SHEET 5 A 5 THR A 122 ASP A 127 -1 O LEU A 124 N MSE A 117
SHEET 1 B 5 TYR A 47 VAL A 49 0
SHEET 2 B 5 LEU A 29 LEU A 37 -1 N ALA A 33 O VAL A 49
SHEET 3 B 5 TYR A 89 ILE A 98 -1 O GLY A 95 N VAL A 32
SHEET 4 B 5 ALA A 137 ARG A 145 -1 O ALA A 138 N VAL A 96
SHEET 5 B 5 TRP A 151 HIS A 154 -1 O HIS A 154 N GLU A 142
SHEET 1 C 5 TYR A 47 VAL A 49 0
SHEET 2 C 5 LEU A 29 LEU A 37 -1 N ALA A 33 O VAL A 49
SHEET 3 C 5 TYR A 89 ILE A 98 -1 O GLY A 95 N VAL A 32
SHEET 4 C 5 ALA A 137 ARG A 145 -1 O ALA A 138 N VAL A 96
SHEET 5 C 5 HIS A 158 TYR A 160 -1 O TYR A 160 N ALA A 137
LINK O TRP A 17 CA CA A 201 1555 1555 2.36
LINK OD1 ASP A 28 CA CA A 202 1555 1555 2.31
LINK O LEU A 29 CA CA A 202 1555 1555 2.32
LINK OD1 ASP A 30 CA CA A 202 1555 1555 2.24
LINK O SER A 66 CA CA A 202 1555 1555 2.33
LINK O GLY A 69 CA CA A 201 1555 1555 2.36
LINK O GLY A 71 CA CA A 201 1555 1555 2.35
LINK OD1 ASP A 75 CA CA A 201 1555 1555 2.55
LINK OD2 ASP A 75 CA CA A 201 1555 1555 2.43
LINK OE1AGLU A 76 CA CA A 202 1555 1555 2.62
LINK OE2BGLU A 76 CA CA A 202 1555 1555 2.19
LINK CA CA A 201 O HOH A 208 1555 1555 2.35
LINK CA CA A 201 O HOH A 204 1555 1555 2.39
LINK CA CA A 202 O HOH A 217 1555 1555 2.34
LINK C VAL A 77 N MSE A 78 1555 1555 1.33
LINK C MSE A 78 N THR A 79 1555 1555 1.33
LINK C ARG A 116 N MSE A 117 1555 1555 1.32
LINK C MSE A 117 N ARG A 118 1555 1555 1.34
LINK C VAL A 170 N MSE A 171 1555 1555 1.34
LINK C MSE A 171 N GLY A 172 1555 1555 1.33
SITE 1 AC1 6 TRP A 17 GLY A 69 GLY A 71 ASP A 75
SITE 2 AC1 6 HOH A 204 HOH A 208
SITE 1 AC2 6 ASP A 28 LEU A 29 ASP A 30 SER A 66
SITE 2 AC2 6 GLU A 76 HOH A 217
CRYST1 43.231 40.701 49.436 90.00 96.66 90.00 P 1 21 1 2
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 0.023132 0.000000 0.002701 0.00000
SCALE2 0.000000 0.024569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020366 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
