HEADER LYASE 13-FEB-14 4OYW
TITLE CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLATE CYCLASE
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 ADENYLATE CYCLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VINKOVIC
REVDAT 3 27-DEC-23 4OYW 1 SOURCE REMARK CRYST1
REVDAT 2 01-OCT-14 4OYW 1 JRNL
REVDAT 1 02-APR-14 4OYW 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 : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 59877
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3025
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4448
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2216
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4220
REMARK 3 BIN R VALUE (WORKING SET) : 0.2205
REMARK 3 BIN FREE R VALUE : 0.2406
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.13
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 228
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
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 : 7
REMARK 3 SOLVENT ATOMS : 420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30690
REMARK 3 B22 (A**2) : -0.30690
REMARK 3 B33 (A**2) : 0.61380
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.222
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.099
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.096
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.097
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.095
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3896 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5276 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1369 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 99 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 576 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3890 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 501 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5179 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.17
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.55
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|0 - A|468 }
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8638 25.3748 -2.2701
REMARK 3 T TENSOR
REMARK 3 T11: -0.0854 T22: -0.0212
REMARK 3 T33: -0.0136 T12: 0.0117
REMARK 3 T13: 0.0041 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 0.4195 L22: 0.5369
REMARK 3 L33: 0.5889 L12: -0.0952
REMARK 3 L13: 0.2401 L23: -0.1746
REMARK 3 S TENSOR
REMARK 3 S11: -0.0379 S12: -0.0274 S13: -0.0015
REMARK 3 S21: 0.0193 S22: 0.1009 S23: 0.1785
REMARK 3 S31: -0.0466 S32: -0.1788 S33: -0.0630
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4OYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-05
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) : 0.97560
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 : 59877
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
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 (%): 52.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
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 48.69550
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 48.69550
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 48.69550
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: 9870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 99.42400
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 49.71200
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 86.10371
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 734 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1018 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: 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 HIS A 28 63.89 27.94
REMARK 500 THR A 132 62.26 -107.72
REMARK 500 GLU A 136 22.40 47.11
REMARK 500 GLU A 137 -49.00 -162.16
REMARK 500 ASP A 140 31.47 -76.10
REMARK 500 ASP A 159 -156.09 -127.16
REMARK 500 ASP A 258 95.89 -166.03
REMARK 500 ASP A 305 30.09 -145.78
REMARK 500 LYS A 354 -98.38 12.15
REMARK 500 VAL A 355 117.14 66.66
REMARK 500 LYS A 378 -6.82 82.05
REMARK 500 ASN A 436 0.15 55.03
REMARK 500 ALA A 454 113.45 -163.21
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 941 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A 944 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A1018 DISTANCE = 7.57 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 CL A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OYA RELATED DB: PDB
REMARK 900 RELATED ID: 4OYB 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: 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 4OYW A 1 469 UNP Q96PN6 ADCYA_HUMAN 1 469
SEQADV 4OYW 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 4OYW CME A 253 CYS MODIFIED RESIDUE
HET ACE A 0 3
HET CME A 253 10
HET GOL A 501 6
HET CL A 502 1
HETNAM ACE ACETYL GROUP
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
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 CL CL 1-
FORMUL 4 HOH *420(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 SER A 59 1 6
HELIX 5 AA5 SER A 60 MET A 64 5 5
HELIX 6 AA6 ARG A 66 PHE A 89 1 24
HELIX 7 AA7 GLU A 108 LYS A 110 5 3
HELIX 8 AA8 GLN A 111 PHE A 130 1 20
HELIX 9 AA9 GLY A 169 ALA A 182 1 14
HELIX 10 AB1 SER A 190 CYS A 197 1 8
HELIX 11 AB2 ASN A 225 THR A 235 1 11
HELIX 12 AB3 SER A 242 LYS A 246 5 5
HELIX 13 AB4 ARG A 250 LEU A 255 5 6
HELIX 14 AB5 ASP A 258 LYS A 267 1 10
HELIX 15 AB6 MET A 270 ASP A 278 1 9
HELIX 16 AB7 LYS A 306 PHE A 328 1 23
HELIX 17 AB8 ASP A 357 SER A 374 1 18
HELIX 18 AB9 GLY A 408 TYR A 421 1 14
HELIX 19 AC1 ASP A 428 ASN A 436 1 9
HELIX 20 AC2 PRO A 438 TYR A 440 5 3
SHEET 1 AA1 5 ASP A 92 PHE A 96 0
SHEET 2 AA1 5 ALA A 100 ARG A 106 -1 O LEU A 104 N ASP A 92
SHEET 3 AA1 5 PHE A 35 ASP A 47 -1 N VAL A 46 O LEU A 101
SHEET 4 AA1 5 LYS A 144 GLY A 158 -1 O ILE A 152 N PHE A 39
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 PHE A 96 0
SHEET 2 AA2 7 ALA A 100 ARG A 106 -1 O LEU A 104 N ASP A 92
SHEET 3 AA2 7 PHE A 35 ASP A 47 -1 N VAL A 46 O LEU A 101
SHEET 4 AA2 7 LYS A 144 GLY A 158 -1 O ILE A 152 N PHE A 39
SHEET 5 AA2 7 VAL A 187 LEU A 189 1 O ILE A 188 N LEU A 147
SHEET 6 AA2 7 VAL A 213 LEU A 218 -1 O VAL A 213 N LEU A 189
SHEET 7 AA2 7 ILE A 202 SER A 206 -1 N GLU A 205 O LYS A 214
SHEET 1 AA3 5 GLN A 331 PHE A 338 0
SHEET 2 AA3 5 GLY A 341 PHE A 348 -1 O LEU A 345 N LYS A 334
SHEET 3 AA3 5 GLU A 288 PHE A 301 -1 N THR A 293 O PHE A 348
SHEET 4 AA3 5 ILE A 379 HIS A 398 -1 O SER A 383 N ASN A 298
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 PHE A 338 0
SHEET 2 AA4 7 GLY A 341 PHE A 348 -1 O LEU A 345 N LYS A 334
SHEET 3 AA4 7 GLU A 288 PHE A 301 -1 N THR A 293 O PHE A 348
SHEET 4 AA4 7 ILE A 379 HIS A 398 -1 O SER A 383 N ASN A 298
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 1.32
LINK C ALA A 252 N CME A 253 1555 1555 1.36
LINK C CME A 253 N THR A 254 1555 1555 1.33
CISPEP 1 ARG A 33 PRO A 34 0 3.07
CISPEP 2 ALA A 454 ASP A 455 0 -7.17
SITE 1 AC1 6 THR A 322 LEU A 325 LYS A 326 GLY A 330
SITE 2 AC1 6 HOH A 818 HOH A1007
SITE 1 AC2 3 LYS A 95 VAL A 167 HOH A 863
CRYST1 99.424 99.424 97.391 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 0.010058 0.005807 0.000000 0.00000
SCALE2 0.000000 0.011614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010268 0.00000
HETATM 1 C ACE A 0 63.198 12.741 24.855 1.00 27.70 C
ANISOU 1 C ACE A 0 3733 3317 3475 347 -882 53 C
HETATM 2 O ACE A 0 63.810 13.735 24.468 1.00 27.19 O
ANISOU 2 O ACE A 0 3629 3266 3435 319 -902 42 O
HETATM 3 CH3 ACE A 0 63.336 12.223 26.330 1.00 29.72 C
ANISOU 3 CH3 ACE A 0 4054 3551 3686 372 -932 65 C
(ATOM LINES ARE NOT SHOWN.)
END