HEADER LYASE 11-FEB-14 4OYB
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE SOLAC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE CYCLASE TYPE 10;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AH-RELATED PROTEIN, ADENYLATE CYCLASE HOMOLOG, GERM CELL
COMPND 5 SOLUBLE ADENYLYL CYCLASE, SAC, TESTICULAR SOLUBLE ADENYLYL CYCLASE;
COMPND 6 EC: 4.6.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADCY10,SAC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VINKOVIC
REVDAT 3 27-DEC-23 4OYB 1 SOURCE REMARK CRYST1 ATOM
REVDAT 2 01-OCT-14 4OYB 1 JRNL
REVDAT 1 02-APR-14 4OYB 0
JRNL AUTH S.M.SAALAU-BETHELL,V.BERDINI,A.CLEASBY,M.CONGREVE,J.E.COYLE,
JRNL AUTH 2 V.LOCK,C.W.MURRAY,M.A.O'BRIEN,S.J.RICH,T.SAMBROOK,
JRNL AUTH 3 M.VINKOVIC,J.R.YON,H.JHOTI
JRNL TITL CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLATE CYCLASE REVEALS
JRNL TITL 2 A DISTINCT, HIGHLY FLEXIBLE ALLOSTERIC BICARBONATE BINDING
JRNL TITL 3 POCKET.
JRNL REF CHEMMEDCHEM V. 9 823 2014
JRNL REFN ESSN 1860-7187
JRNL PMID 24616449
JRNL DOI 10.1002/CMDC.201300480
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0064
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 57466
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3036
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4239
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 243
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 606
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.234
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3914 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3740 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5294 ; 1.483 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8629 ; 0.883 ; 2.994
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 479 ; 6.088 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;34.127 ;24.462
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 695 ;15.323 ;15.288
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.091 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 580 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4390 ; 0.000 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 900 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1892 ; 4.108 ; 5.446
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1892 ; 4.106 ; 5.446
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2022 ; 5.531 ; 6.680
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2023 ; 5.530 ; 6.679
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1374 ;11.146 ;13.289
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1375 ;11.142 ;13.287
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 : NULL
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 0 A 468
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8286 25.4558 -2.0457
REMARK 3 T TENSOR
REMARK 3 T11: 0.0129 T22: 0.0289
REMARK 3 T33: 0.0136 T12: 0.0033
REMARK 3 T13: 0.0025 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.0681 L22: 0.1012
REMARK 3 L33: 0.1805 L12: -0.0160
REMARK 3 L13: 0.0616 L23: -0.0126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0273 S12: -0.0066 S13: -0.0059
REMARK 3 S21: 0.0057 S22: 0.0343 S23: 0.0298
REMARK 3 S31: -0.0142 S32: -0.0241 S33: -0.0070
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 : A 502 A 502
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5077 25.0908 -3.0492
REMARK 3 T TENSOR
REMARK 3 T11: 0.0527 T22: 0.0286
REMARK 3 T33: 0.0190 T12: -0.0074
REMARK 3 T13: -0.0177 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.2753 L22: 2.9420
REMARK 3 L33: 10.0161 L12: -1.0682
REMARK 3 L13: -1.7250 L23: -2.5202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: -0.0085 S13: 0.1063
REMARK 3 S21: -0.0298 S22: 0.1823 S23: -0.0824
REMARK 3 S31: 0.1186 S32: -0.3327 S33: -0.1563
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4OYB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60896
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 86.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1UL OF PROTEIN SOLUTION WAS MIXED WITH
REMARK 280 1UL OF RESERVOIR SOLUTION (0.1M SODIUM ACETATE, PH 4.8, 0.2M
REMARK 280 TRISODIUM CITRATE, 16-18% PEG4K AND 10% GLYCEROL) AND LEFT TO
REMARK 280 EQUILIBRATE AT 4C, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
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 49.06300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.06300
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.06300
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 -0.500000 -0.866025 0.000000 99.74600
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 49.87300
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 86.38257
REMARK 350 BIOMT3 3 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 A 757 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 VAL A 469
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 LYS A 468 O
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ACE A 0 C MET A 1 N 0.183
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 GLU A 6 104.87 66.14
REMARK 500 HIS A 28 67.28 37.83
REMARK 500 GLU A 134 -164.92 -170.02
REMARK 500 GLU A 136 37.91 36.44
REMARK 500 GLU A 137 -55.17 71.28
REMARK 500 LEU A 139 116.22 -31.61
REMARK 500 ILE A 141 94.80 60.95
REMARK 500 ASP A 159 -154.89 -120.80
REMARK 500 ASN A 185 -0.80 77.74
REMARK 500 ASP A 258 94.18 -166.93
REMARK 500 PHE A 338 -115.62 -126.64
REMARK 500 PHE A 338 -115.32 -126.64
REMARK 500 ASP A 339 76.64 -51.02
REMARK 500 LYS A 340 -46.03 75.33
REMARK 500 PHE A 350 -173.00 -69.58
REMARK 500 PRO A 351 106.46 -43.21
REMARK 500 LYS A 378 -8.06 83.71
REMARK 500 ASN A 436 2.26 53.59
REMARK 500 ASP A 455 83.81 46.06
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 991 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A1043 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH A1044 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A1069 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A1077 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A1079 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH A1093 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH A1097 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A1114 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1118 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A1169 DISTANCE = 8.00 ANGSTROMS
REMARK 525 HOH A1171 DISTANCE = 8.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1VJ A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OYA RELATED DB: PDB
REMARK 900 RELATED ID: 4OYI RELATED DB: PDB
REMARK 900 RELATED ID: 4OYM RELATED DB: PDB
REMARK 900 RELATED ID: 4OYO RELATED DB: PDB
REMARK 900 RELATED ID: 4OYP RELATED DB: PDB
REMARK 900 RELATED ID: 4OYW RELATED DB: PDB
REMARK 900 RELATED ID: 4OYX RELATED DB: PDB
REMARK 900 RELATED ID: 4OYZ RELATED DB: PDB
REMARK 900 RELATED ID: 4OZ2 RELATED DB: PDB
REMARK 900 RELATED ID: 4OZ3 RELATED DB: PDB
DBREF 4OYB A 1 469 UNP Q96PN6 ADCYA_HUMAN 1 469
SEQADV 4OYB ACE A 0 UNP Q96PN6 ACETYLATION
SEQRES 1 A 470 ACE MET ASN THR PRO LYS GLU GLU PHE GLN ASP TRP PRO
SEQRES 2 A 470 ILE VAL ARG ILE ALA ALA HIS LEU PRO ASP LEU ILE VAL
SEQRES 3 A 470 TYR GLY HIS PHE SER PRO GLU ARG PRO PHE MET ASP TYR
SEQRES 4 A 470 PHE ASP GLY VAL LEU MET PHE VAL ASP ILE SER GLY PHE
SEQRES 5 A 470 THR ALA MET THR GLU LYS PHE SER SER ALA MET TYR MET
SEQRES 6 A 470 ASP ARG GLY ALA GLU GLN LEU VAL GLU ILE LEU ASN TYR
SEQRES 7 A 470 HIS ILE SER ALA ILE VAL GLU LYS VAL LEU ILE PHE GLY
SEQRES 8 A 470 GLY ASP ILE LEU LYS PHE ALA GLY ASP ALA LEU LEU ALA
SEQRES 9 A 470 LEU TRP ARG VAL GLU ARG LYS GLN LEU LYS ASN ILE ILE
SEQRES 10 A 470 THR VAL VAL ILE LYS CYS SER LEU GLU ILE HIS GLY LEU
SEQRES 11 A 470 PHE GLU THR GLN GLU TRP GLU GLU GLY LEU ASP ILE ARG
SEQRES 12 A 470 VAL LYS ILE GLY LEU ALA ALA GLY HIS ILE SER MET LEU
SEQRES 13 A 470 VAL PHE GLY ASP GLU THR HIS SER HIS PHE LEU VAL ILE
SEQRES 14 A 470 GLY GLN ALA VAL ASP ASP VAL ARG LEU ALA GLN ASN MET
SEQRES 15 A 470 ALA GLN MET ASN ASP VAL ILE LEU SER PRO ASN CYS TRP
SEQRES 16 A 470 GLN LEU CYS ASP ARG SER MET ILE GLU ILE GLU SER VAL
SEQRES 17 A 470 PRO ASP GLN ARG ALA VAL LYS VAL ASN PHE LEU LYS PRO
SEQRES 18 A 470 PRO PRO ASN PHE ASN PHE ASP GLU PHE PHE THR LYS CYS
SEQRES 19 A 470 THR THR PHE MET HIS TYR TYR PRO SER GLY GLU HIS LYS
SEQRES 20 A 470 ASN LEU LEU ARG LEU ALA CME THR LEU LYS PRO ASP PRO
SEQRES 21 A 470 GLU LEU GLU MET SER LEU GLN LYS TYR VAL MET GLU SER
SEQRES 22 A 470 ILE LEU LYS GLN ILE ASP ASN LYS GLN LEU GLN GLY TYR
SEQRES 23 A 470 LEU SER GLU LEU ARG PRO VAL THR ILE VAL PHE VAL ASN
SEQRES 24 A 470 LEU MET PHE GLU ASP GLN ASP LYS ALA GLU GLU ILE GLY
SEQRES 25 A 470 PRO ALA ILE GLN ASP ALA TYR MET HIS ILE THR SER VAL
SEQRES 26 A 470 LEU LYS ILE PHE GLN GLY GLN ILE ASN LYS VAL PHE MET
SEQRES 27 A 470 PHE ASP LYS GLY CYS SER PHE LEU CYS VAL PHE GLY PHE
SEQRES 28 A 470 PRO GLY GLU LYS VAL PRO ASP GLU LEU THR HIS ALA LEU
SEQRES 29 A 470 GLU CYS ALA MET ASP ILE PHE ASP PHE CYS SER GLN VAL
SEQRES 30 A 470 HIS LYS ILE GLN THR VAL SER ILE GLY VAL ALA SER GLY
SEQRES 31 A 470 ILE VAL PHE CYS GLY ILE VAL GLY HIS THR VAL ARG HIS
SEQRES 32 A 470 GLU TYR THR VAL ILE GLY GLN LYS VAL ASN LEU ALA ALA
SEQRES 33 A 470 ARG MET MET MET TYR TYR PRO GLY ILE VAL THR CYS ASP
SEQRES 34 A 470 SER VAL THR TYR ASN GLY SER ASN LEU PRO ALA TYR PHE
SEQRES 35 A 470 PHE LYS GLU LEU PRO LYS LYS VAL MET LYS GLY VAL ALA
SEQRES 36 A 470 ASP SER GLY PRO LEU TYR GLN TYR TRP GLY ARG THR GLU
SEQRES 37 A 470 LYS VAL
MODRES 4OYB CME A 253 CYS MODIFIED RESIDUE
HET ACE A 0 3
HET CME A 253 10
HET GOL A 501 12
HET 1VJ A 502 34
HETNAM ACE ACETYL GROUP
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM GOL GLYCEROL
HETNAM 1VJ ETHYL 2-[3-[(4-AZANYL-1,2,5-OXADIAZOL-3-YL)
HETNAM 2 1VJ CARBONYL]PHENOXY]ETHANOATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 ACE C2 H4 O
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 GOL C3 H8 O3
FORMUL 3 1VJ C13 H13 N3 O5
FORMUL 4 HOH *606(H2 O)
HELIX 1 AA1 TRP A 11 ALA A 18 1 8
HELIX 2 AA2 PRO A 21 TYR A 26 1 6
HELIX 3 AA3 ILE A 48 ALA A 53 1 6
HELIX 4 AA4 MET A 54 MET A 64 5 11
HELIX 5 AA5 ARG A 66 PHE A 89 1 24
HELIX 6 AA6 GLU A 108 LYS A 110 5 3
HELIX 7 AA7 GLN A 111 PHE A 130 1 20
HELIX 8 AA8 GLY A 169 ALA A 182 1 14
HELIX 9 AA9 SER A 190 CYS A 197 1 8
HELIX 10 AB1 ASN A 225 THR A 235 1 11
HELIX 11 AB2 SER A 242 LYS A 246 5 5
HELIX 12 AB3 ARG A 250 LEU A 255 5 6
HELIX 13 AB4 ASP A 258 LYS A 267 1 10
HELIX 14 AB5 MET A 270 ASP A 278 1 9
HELIX 15 AB6 LYS A 306 PHE A 328 1 23
HELIX 16 AB7 ASP A 357 SER A 374 1 18
HELIX 17 AB8 GLY A 408 TYR A 421 1 14
HELIX 18 AB9 ASP A 428 ASN A 436 1 9
HELIX 19 AC1 PRO A 438 TYR A 440 5 3
SHEET 1 AA1 5 ASP A 92 ALA A 97 0
SHEET 2 AA1 5 ALA A 100 ARG A 106 -1 O ALA A 100 N ALA A 97
SHEET 3 AA1 5 PHE A 35 ASP A 47 -1 N MET A 44 O ALA A 103
SHEET 4 AA1 5 LYS A 144 GLY A 158 -1 O LYS A 144 N ASP A 47
SHEET 5 AA1 5 SER A 163 ILE A 168 -1 O LEU A 166 N LEU A 155
SHEET 1 AA2 7 ASP A 92 ALA A 97 0
SHEET 2 AA2 7 ALA A 100 ARG A 106 -1 O ALA A 100 N ALA A 97
SHEET 3 AA2 7 PHE A 35 ASP A 47 -1 N MET A 44 O ALA A 103
SHEET 4 AA2 7 LYS A 144 GLY A 158 -1 O LYS A 144 N ASP A 47
SHEET 5 AA2 7 VAL A 187 LEU A 189 1 O ILE A 188 N LEU A 147
SHEET 6 AA2 7 GLN A 210 LEU A 218 -1 O VAL A 213 N LEU A 189
SHEET 7 AA2 7 ILE A 202 VAL A 207 -1 N GLU A 203 O ASN A 216
SHEET 1 AA3 5 GLN A 331 MET A 337 0
SHEET 2 AA3 5 CYS A 342 PHE A 348 -1 O SER A 343 N PHE A 336
SHEET 3 AA3 5 GLU A 288 PHE A 301 -1 N VAL A 297 O PHE A 344
SHEET 4 AA3 5 ILE A 379 HIS A 398 -1 O ALA A 387 N ILE A 294
SHEET 5 AA3 5 ARG A 401 ILE A 407 -1 O GLU A 403 N VAL A 396
SHEET 1 AA4 7 GLN A 331 MET A 337 0
SHEET 2 AA4 7 CYS A 342 PHE A 348 -1 O SER A 343 N PHE A 336
SHEET 3 AA4 7 GLU A 288 PHE A 301 -1 N VAL A 297 O PHE A 344
SHEET 4 AA4 7 ILE A 379 HIS A 398 -1 O ALA A 387 N ILE A 294
SHEET 5 AA4 7 VAL A 425 CYS A 427 1 O THR A 426 N ILE A 384
SHEET 6 AA4 7 TYR A 460 TYR A 462 -1 O TYR A 460 N CYS A 427
SHEET 7 AA4 7 PHE A 442 GLU A 444 -1 N LYS A 443 O GLN A 461
LINK C ACE A 0 N MET A 1 1555 1555 1.52
LINK C ALA A 252 N CME A 253 1555 1555 1.34
LINK C CME A 253 N THR A 254 1555 1555 1.33
CISPEP 1 ARG A 33 PRO A 34 0 3.83
SITE 1 AC1 9 HIS A 162 THR A 322 LYS A 326 GLY A 330
SITE 2 AC1 9 GLN A 331 ILE A 332 HOH A 868 HOH A1017
SITE 3 AC1 9 HOH A1030
SITE 1 AC2 11 PHE A 45 LYS A 95 ALA A 97 LEU A 102
SITE 2 AC2 11 LEU A 166 VAL A 167 ARG A 176 PHE A 336
SITE 3 AC2 11 MET A 337 PHE A 338 SER A 343
CRYST1 99.746 99.746 98.126 90.00 90.00 120.00 P 63 6
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 0.010025 0.005788 0.000000 0.00000
SCALE2 0.000000 0.011576 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010191 0.00000
HETATM 1 C ACE A 0 63.802 12.937 25.052 1.00 44.32 C
ANISOU 1 C ACE A 0 5571 5856 5413 385 -175 -94 C
HETATM 2 O ACE A 0 64.126 14.081 24.829 1.00 42.43 O
ANISOU 2 O ACE A 0 5321 5626 5175 368 -178 -96 O
HETATM 3 CH3 ACE A 0 63.730 12.269 26.436 1.00 47.38 C
ANISOU 3 CH3 ACE A 0 5979 6230 5793 407 -183 -92 C
(ATOM LINES ARE NOT SHOWN.)
END
