HEADER LYASE 15-JAN-14 4CLS
TITLE CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE WITH PYROPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE CYCLASE TYPE 10;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1-469;
COMPND 5 SYNONYM: AH-RELATED PROTEIN, ADENYLATE CYCLASE HOMOLOG, GERM CELL
COMPND 6 SOLUBLE ADENYLYL CYCLASE, HSAC, SAC, TESTICULAR SOLUBLE ADENYLYL
COMPND 7 CYCLASE, SOLUBLE ADENYLYL CYCLASE;
COMPND 8 EC: 4.6.1.1;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL1392
KEYWDS LYASE, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KLEINBOELTING,M.WEYAND,C.STEEGBORN
REVDAT 5 20-DEC-23 4CLS 1 REMARK LINK
REVDAT 4 16-OCT-19 4CLS 1 REMARK
REVDAT 3 03-APR-19 4CLS 1 SOURCE LINK
REVDAT 2 26-MAR-14 4CLS 1 JRNL
REVDAT 1 05-MAR-14 4CLS 0
JRNL AUTH S.KLEINBOELTING,A.DIAZ,S.MONIOT,J.VAN DEN HEUVEL,M.WEYAND,
JRNL AUTH 2 L.R.LEVIN,J.BUCK,C.STEEGBORN
JRNL TITL CRYSTAL STRUCTURES OF HUMAN SOLUBLE ADENYLYL CYCLASE REVEAL
JRNL TITL 2 MECHANISMS OF CATALYSIS AND OF ITS ACTIVATION THROUGH
JRNL TITL 3 BICARBONATE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 3727 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24567411
JRNL DOI 10.1073/PNAS.1322778111
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 45014
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2371
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3330
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3638
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -0.43000
REMARK 3 B12 (A**2) : 0.07000
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): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.311
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3781 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3618 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5122 ; 1.923 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8338 ; 0.924 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 469 ; 6.345 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 167 ;35.568 ;24.551
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 651 ;15.599 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;14.750 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 570 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4230 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 867 ; 0.001 ; 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): 1847 ; 2.669 ; 2.511
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1845 ; 2.667 ; 2.508
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2307 ; 4.078 ; 3.743
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2308 ; 4.079 ; 3.744
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1934 ; 3.779 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1926 ; 3.768 ; 2.980
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2797 ; 5.684 ; 4.276
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4330 ; 8.074 ;21.093
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4328 ; 8.073 ;21.057
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 : 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 1 A 467
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8683 -6.3990 0.9209
REMARK 3 T TENSOR
REMARK 3 T11: 0.0676 T22: 0.0116
REMARK 3 T33: 0.0289 T12: 0.0135
REMARK 3 T13: 0.0213 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.6073 L22: 0.6425
REMARK 3 L33: 0.7847 L12: -0.0159
REMARK 3 L13: -0.0350 L23: -0.3333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: 0.0379 S13: 0.1075
REMARK 3 S21: 0.1019 S22: -0.0172 S23: 0.0633
REMARK 3 S31: -0.1816 S32: -0.0585 S33: -0.0222
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 4CLS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1290059440.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
REMARK 200 MONOCHROMATOR : SI111-DCM WITH SAGITTAL BENDER
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47385
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 86.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
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) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.88700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4CLF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.8, 0.2 M TRI
REMARK 280 -SODIUM-CITRATE, 15% (W/V) PEG 4000, 10% (V/V) GLYCEROL, PH 6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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 48.87500
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 48.87500
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 48.87500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.2 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 50.04500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -86.68048
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 100.09000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
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 A2059 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 GLN A 133
REMARK 465 GLU A 134
REMARK 465 TRP A 135
REMARK 465 GLU A 136
REMARK 465 GLU A 137
REMARK 465 GLY A 138
REMARK 465 LEU A 139
REMARK 465 ASP A 140
REMARK 465 LYS A 468
REMARK 465 VAL A 469
REMARK 465 HIS A 470
REMARK 465 HIS A 471
REMARK 465 HIS A 472
REMARK 465 HIS A 473
REMARK 465 HIS A 474
REMARK 465 HIS A 475
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 GLU A 131 CG CD OE1 OE2
REMARK 470 MET A 184 CG SD CE
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 GLU A 353 CG CD OE1 OE2
REMARK 470 VAL A 355 CG1 CG2
REMARK 470 ARG A 465 CG CD NE CZ NH1 NH2
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 10 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 MET A 418 CG - SD - CE ANGL. DEV. = -9.8 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 ASP A 10 53.96 -109.82
REMARK 500 HIS A 28 52.68 37.32
REMARK 500 ASP A 159 -161.10 -124.21
REMARK 500 MET A 184 113.58 -38.14
REMARK 500 ASN A 185 8.08 83.07
REMARK 500 ASP A 258 96.11 -171.36
REMARK 500 LYS A 378 -10.28 91.82
REMARK 500 ARG A 401 103.07 -160.46
REMARK 500 LYS A 451 108.24 -48.87
REMARK 500 ASP A 455 104.14 -167.68
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 A2040 DISTANCE = 5.98 ANGSTROMS
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 MG A1468 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 47 OD1
REMARK 620 2 ASP A 99 OD1 90.2
REMARK 620 3 POP A1470 O3 69.5 138.6
REMARK 620 N 1 2
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP A 1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1474
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CLF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE (APO FORM)
REMARK 900 RELATED ID: 4CLK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE IN COMPLEX WITH
REMARK 900 ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
REMARK 900 RELATED ID: 4CLL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE IN COMPLEX WITH
REMARK 900 BICARBONATE
REMARK 900 RELATED ID: 4CLP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE COMPLEX WITH
REMARK 900 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
REMARK 900 RELATED ID: 4CLT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE WITH ADENOSINE-
REMARK 900 3',5'-CYCLIC-MONOPHOSPHATE AND PYROPHOSPHATE
REMARK 900 RELATED ID: 4CLU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE WITH
REMARK 900 PYROPHOSPHATE
REMARK 900 RELATED ID: 4CLW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE IN COMPLEX WITH
REMARK 900 ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE SOAKED WITH BISULFITE
REMARK 900 RELATED ID: 4CLY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE SOAKED WITH
REMARK 900 BISELENITE
REMARK 900 RELATED ID: 4CLZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE WITH INHIBITOR
REMARK 900 4,4'-DIISOTHIOCYANO-2,2'-STILBENEDISULFONIC ACID
REMARK 900 RELATED ID: 4CM0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE WITH ALPHA,BETA-
REMARK 900 METHYLENEADENOSINE-5'-TRIPHOSPHATE SOAKED WITH BICARBONATE
REMARK 900 RELATED ID: 4CM2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLYL CYCLASE SOAKED WITH
REMARK 900 BISULFITE
DBREF 4CLS A 1 469 UNP Q96PN6 ADCYA_HUMAN 1 469
SEQADV 4CLS HIS A 470 UNP Q96PN6 EXPRESSION TAG
SEQADV 4CLS HIS A 471 UNP Q96PN6 EXPRESSION TAG
SEQADV 4CLS HIS A 472 UNP Q96PN6 EXPRESSION TAG
SEQADV 4CLS HIS A 473 UNP Q96PN6 EXPRESSION TAG
SEQADV 4CLS HIS A 474 UNP Q96PN6 EXPRESSION TAG
SEQADV 4CLS HIS A 475 UNP Q96PN6 EXPRESSION TAG
SEQRES 1 A 475 MET ASN THR PRO LYS GLU GLU PHE GLN ASP TRP PRO ILE
SEQRES 2 A 475 VAL ARG ILE ALA ALA HIS LEU PRO ASP LEU ILE VAL TYR
SEQRES 3 A 475 GLY HIS PHE SER PRO GLU ARG PRO PHE MET ASP TYR PHE
SEQRES 4 A 475 ASP GLY VAL LEU MET PHE VAL ASP ILE SER GLY PHE THR
SEQRES 5 A 475 ALA MET THR GLU LYS PHE SER SER ALA MET TYR MET ASP
SEQRES 6 A 475 ARG GLY ALA GLU GLN LEU VAL GLU ILE LEU ASN TYR HIS
SEQRES 7 A 475 ILE SER ALA ILE VAL GLU LYS VAL LEU ILE PHE GLY GLY
SEQRES 8 A 475 ASP ILE LEU LYS PHE ALA GLY ASP ALA LEU LEU ALA LEU
SEQRES 9 A 475 TRP ARG VAL GLU ARG LYS GLN LEU LYS ASN ILE ILE THR
SEQRES 10 A 475 VAL VAL ILE LYS CYS SER LEU GLU ILE HIS GLY LEU PHE
SEQRES 11 A 475 GLU THR GLN GLU TRP GLU GLU GLY LEU ASP ILE ARG VAL
SEQRES 12 A 475 LYS ILE GLY LEU ALA ALA GLY HIS ILE SER MET LEU VAL
SEQRES 13 A 475 PHE GLY ASP GLU THR HIS SER HIS PHE LEU VAL ILE GLY
SEQRES 14 A 475 GLN ALA VAL ASP ASP VAL ARG LEU ALA GLN ASN MET ALA
SEQRES 15 A 475 GLN MET ASN ASP VAL ILE LEU SER PRO ASN CYS TRP GLN
SEQRES 16 A 475 LEU CYS ASP ARG SER MET ILE GLU ILE GLU SER VAL PRO
SEQRES 17 A 475 ASP GLN ARG ALA VAL LYS VAL ASN PHE LEU LYS PRO PRO
SEQRES 18 A 475 PRO ASN PHE ASN PHE ASP GLU PHE PHE THR LYS CYS THR
SEQRES 19 A 475 THR PHE MET HIS TYR TYR PRO SER GLY GLU HIS LYS ASN
SEQRES 20 A 475 LEU LEU ARG LEU ALA CME THR LEU LYS PRO ASP PRO GLU
SEQRES 21 A 475 LEU GLU MET SER LEU GLN LYS TYR VAL MET GLU SER ILE
SEQRES 22 A 475 LEU LYS GLN ILE ASP ASN LYS GLN LEU GLN GLY TYR LEU
SEQRES 23 A 475 SER GLU LEU ARG PRO VAL THR ILE VAL PHE VAL ASN LEU
SEQRES 24 A 475 MET PHE GLU ASP GLN ASP LYS ALA GLU GLU ILE GLY PRO
SEQRES 25 A 475 ALA ILE GLN ASP ALA TYR MET HIS ILE THR SER VAL LEU
SEQRES 26 A 475 LYS ILE PHE GLN GLY GLN ILE ASN LYS VAL PHE MET PHE
SEQRES 27 A 475 ASP LYS GLY CYS SER PHE LEU CYS VAL PHE GLY PHE PRO
SEQRES 28 A 475 GLY GLU LYS VAL PRO ASP GLU LEU THR HIS ALA LEU GLU
SEQRES 29 A 475 CYS ALA MET ASP ILE PHE ASP PHE CYS SER GLN VAL HIS
SEQRES 30 A 475 LYS ILE GLN THR VAL SER ILE GLY VAL ALA SER GLY ILE
SEQRES 31 A 475 VAL PHE CYS GLY ILE VAL GLY HIS THR VAL ARG HIS GLU
SEQRES 32 A 475 TYR THR VAL ILE GLY GLN LYS VAL ASN LEU ALA ALA ARG
SEQRES 33 A 475 MET MET MET TYR TYR PRO GLY ILE VAL THR CYS ASP SER
SEQRES 34 A 475 VAL THR TYR ASN GLY SER ASN LEU PRO ALA TYR PHE PHE
SEQRES 35 A 475 LYS GLU LEU PRO LYS LYS VAL MET LYS GLY VAL ALA ASP
SEQRES 36 A 475 SER GLY PRO LEU TYR GLN TYR TRP GLY ARG THR GLU LYS
SEQRES 37 A 475 VAL HIS HIS HIS HIS HIS HIS
MODRES 4CLS CME A 253 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 253 10
HET MG A1468 1
HET CL A1469 1
HET POP A1470 9
HET GOL A1471 6
HET ACT A1472 4
HET EDO A1473 4
HET EDO A1474 4
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM POP PYROPHOSPHATE 2-
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 MG MG 2+
FORMUL 3 CL CL 1-
FORMUL 4 POP H2 O7 P2 2-
FORMUL 5 GOL C3 H8 O3
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 HOH *162(H2 O)
HELIX 1 MET A 1 ALA A 18 0 18
HELIX 2 MET A 1 TYR A 26 0 26
HELIX 3 MET A 1 SER A 59 0 59
HELIX 4 MET A 1 PHE A 89 0 89
HELIX 5 MET A 1 PHE A 130 0 130
HELIX 6 MET A 1 ALA A 182 0 174
HELIX 7 MET A 1 CYS A 197 0 189
HELIX 8 MET A 1 THR A 235 0 227
HELIX 9 MET A 1 LYS A 246 0 238
HELIX 10 MET A 1 LEU A 255 0 247
HELIX 11 MET A 1 LYS A 267 0 259
HELIX 12 MET A 1 ASP A 278 0 270
HELIX 13 MET A 1 SER A 287 0 279
HELIX 14 MET A 1 PHE A 328 0 320
HELIX 15 MET A 1 SER A 374 0 366
HELIX 16 MET A 1 TYR A 421 0 413
HELIX 17 MET A 1 SER A 435 0 427
SHEET 1 AA 5 ASP A 92 ALA A 97 0
SHEET 2 AA 5 ALA A 100 ARG A 106 -1 O ALA A 100 N ALA A 97
SHEET 3 AA 5 PHE A 35 SER A 49 -1 O VAL A 42 N TRP A 105
SHEET 4 AA 5 ARG A 142 GLY A 158 -1 O ARG A 142 N SER A 49
SHEET 5 AA 5 SER A 163 ILE A 168 1 O HIS A 164 N PHE A 157
SHEET 1 AB 7 ASP A 92 ALA A 97 0
SHEET 2 AB 7 ALA A 100 ARG A 106 -1 O ALA A 100 N ALA A 97
SHEET 3 AB 7 PHE A 35 SER A 49 -1 O VAL A 42 N TRP A 105
SHEET 4 AB 7 ARG A 142 GLY A 158 -1 O ARG A 142 N SER A 49
SHEET 5 AB 7 VAL A 187 LEU A 189 1 O ILE A 188 N LEU A 147
SHEET 6 AB 7 GLN A 210 LEU A 218 -1 O VAL A 213 N LEU A 189
SHEET 7 AB 7 ILE A 202 VAL A 207 -1 O GLU A 203 N ASN A 216
SHEET 1 AC 2 SER A 163 ILE A 168 0
SHEET 2 AC 2 ARG A 142 GLY A 158 1 O SER A 153 N ILE A 168
SHEET 1 AD 5 GLY A 330 MET A 337 0
SHEET 2 AD 5 CYS A 342 PHE A 348 -1 O SER A 343 N PHE A 336
SHEET 3 AD 5 GLU A 288 PHE A 301 -1 O THR A 293 N PHE A 348
SHEET 4 AD 5 ILE A 379 HIS A 398 -1 N GLN A 380 O MET A 300
SHEET 5 AD 5 ARG A 401 ILE A 407 1 O ARG A 401 N HIS A 398
SHEET 1 AE 7 GLY A 330 MET A 337 0
SHEET 2 AE 7 CYS A 342 PHE A 348 -1 O SER A 343 N PHE A 336
SHEET 3 AE 7 GLU A 288 PHE A 301 -1 O THR A 293 N PHE A 348
SHEET 4 AE 7 ILE A 379 HIS A 398 -1 N GLN A 380 O MET A 300
SHEET 5 AE 7 VAL A 425 CYS A 427 1 O THR A 426 N VAL A 386
SHEET 6 AE 7 TYR A 460 TYR A 462 -1 O TYR A 460 N CYS A 427
SHEET 7 AE 7 PHE A 442 GLU A 444 -1 O LYS A 443 N GLN A 461
SHEET 1 AF 2 ARG A 401 ILE A 407 0
SHEET 2 AF 2 ILE A 379 HIS A 398 1 O PHE A 392 N ILE A 407
LINK C ALA A 252 N CME A 253 1555 1555 1.33
LINK C CME A 253 N THR A 254 1555 1555 1.33
LINK OD1 ASP A 47 MG MG A1468 1555 1555 2.56
LINK OD1 ASP A 99 MG MG A1468 1555 1555 2.22
LINK MG MG A1468 O3 POP A1470 1555 1555 2.93
CISPEP 1 ARG A 33 PRO A 34 0 -0.51
SITE 1 AC1 3 ASP A 47 ASP A 99 POP A1470
SITE 1 AC2 4 LYS A 95 LEU A 166 VAL A 167 HOH A2076
SITE 1 AC3 11 ASP A 47 ILE A 48 SER A 49 GLY A 50
SITE 2 AC3 11 PHE A 51 THR A 52 ASP A 99 LYS A 144
SITE 3 AC3 11 ASN A 412 MG A1468 HOH A2033
SITE 1 AC4 6 ASP A 22 GLY A 90 HIS A 238 TYR A 239
SITE 2 AC4 6 TYR A 240 HOH A2051
SITE 1 AC5 2 PHE A 45 ARG A 176
SITE 1 AC6 8 PHE A 29 SER A 30 PRO A 31 ARG A 33
SITE 2 AC6 8 SER A 264 LYS A 267 HOH A2029 HOH A2100
SITE 1 AC7 7 LYS A 95 HIS A 164 ASN A 333 LYS A 334
SITE 2 AC7 7 VAL A 335 HOH A2073 HOH A2075
CRYST1 100.090 100.090 97.750 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 0.009991 0.005768 0.000000 0.00000
SCALE2 0.000000 0.011537 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
