HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-JUL-16 5L0N
TITLE PKG I'S CARBOXYL TERMINAL CYCLIC NUCLEOTIDE BINDING DOMAIN (CNB-B) IN
TITLE 2 A COMPLEX WITH RP-CGMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-DEPENDENT PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 219-351;
COMPND 5 SYNONYM: CGK1,CGMP-DEPENDENT PROTEIN KINASE I,CGKI;
COMPND 6 EC: 2.7.11.12;
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: PRKG1, PRKG1B, PRKGR1A, PRKGR1B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BINDING SITES, CYCLIC AMP, CYCLIC GMP, CYCLIC GMP-DEPENDENT PROTEIN
KEYWDS 2 KINASE TYPE I, MUTAGENESIS, SITE-DIRECTED, PROTEIN BINDING, ANALOGS,
KEYWDS 3 TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.CAMPBELL,B.SANKARAN,C.W.KIM
REVDAT 3 04-OCT-23 5L0N 1 REMARK
REVDAT 2 25-DEC-19 5L0N 1 REMARK
REVDAT 1 02-AUG-17 5L0N 0
JRNL AUTH J.C.CAMPBELL,B.SANKARAN,C.W.KIM
JRNL TITL STRUCTURE OF PKG I CNB-B BOUND TO RP-CGMP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31845
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1572
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.5873 - 2.8576 0.99 2897 156 0.1603 0.1649
REMARK 3 2 2.8576 - 2.2683 1.00 2807 156 0.1560 0.1672
REMARK 3 3 2.2683 - 1.9816 1.00 2766 150 0.1503 0.1781
REMARK 3 4 1.9816 - 1.8005 1.00 2782 123 0.1633 0.1854
REMARK 3 5 1.8005 - 1.6714 1.00 2756 128 0.1695 0.1967
REMARK 3 6 1.6714 - 1.5729 1.00 2739 120 0.1662 0.1689
REMARK 3 7 1.5729 - 1.4941 1.00 2740 140 0.1824 0.1933
REMARK 3 8 1.4941 - 1.4291 1.00 2709 137 0.1998 0.2075
REMARK 3 9 1.4291 - 1.3741 1.00 2702 151 0.2037 0.2600
REMARK 3 10 1.3741 - 1.3266 1.00 2685 166 0.2200 0.2669
REMARK 3 11 1.3266 - 1.2852 1.00 2690 145 0.2413 0.2333
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 1051
REMARK 3 ANGLE : 0.966 1427
REMARK 3 CHIRALITY : 0.084 160
REMARK 3 PLANARITY : 0.006 182
REMARK 3 DIHEDRAL : 12.289 373
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 220 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2738 51.8948 2.8674
REMARK 3 T TENSOR
REMARK 3 T11: 0.1943 T22: 0.1752
REMARK 3 T33: 0.1080 T12: 0.0105
REMARK 3 T13: -0.0020 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 6.6738 L22: 5.8451
REMARK 3 L33: 2.0003 L12: -1.1523
REMARK 3 L13: 4.5712 L23: -5.9113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: 0.6716 S13: -0.0752
REMARK 3 S21: -0.7831 S22: 0.0376 S23: 0.0826
REMARK 3 S31: 0.3109 S32: -0.0797 S33: -0.0606
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5848 59.2502 11.0705
REMARK 3 T TENSOR
REMARK 3 T11: 0.0956 T22: 0.1010
REMARK 3 T33: 0.0951 T12: 0.0214
REMARK 3 T13: -0.0098 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 4.2572 L22: 2.3365
REMARK 3 L33: 0.1503 L12: 2.8759
REMARK 3 L13: 0.3280 L23: 0.3751
REMARK 3 S TENSOR
REMARK 3 S11: -0.1036 S12: 0.2382 S13: 0.2207
REMARK 3 S21: -0.1163 S22: 0.0530 S23: 0.1581
REMARK 3 S31: -0.0580 S32: -0.0604 S33: 0.0517
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 293 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5945 63.9133 19.2667
REMARK 3 T TENSOR
REMARK 3 T11: 0.1519 T22: 0.1359
REMARK 3 T33: 0.1629 T12: -0.0015
REMARK 3 T13: -0.0087 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 7.4961 L22: 5.0892
REMARK 3 L33: 2.0012 L12: 3.0175
REMARK 3 L13: 4.1868 L23: 3.8895
REMARK 3 S TENSOR
REMARK 3 S11: 0.1321 S12: -0.4818 S13: 0.2371
REMARK 3 S21: 0.2650 S22: 0.0688 S23: -0.3979
REMARK 3 S31: -0.3283 S32: 0.1746 S33: -0.1992
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 294 THROUGH 340 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1050 60.0549 14.8075
REMARK 3 T TENSOR
REMARK 3 T11: 0.0832 T22: 0.0753
REMARK 3 T33: 0.1029 T12: 0.0025
REMARK 3 T13: 0.0048 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 3.2429 L22: 1.1356
REMARK 3 L33: 0.7515 L12: 0.8525
REMARK 3 L13: 0.4940 L23: 0.0847
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: -0.0455 S13: -0.0032
REMARK 3 S21: 0.0310 S22: -0.0258 S23: 0.1861
REMARK 3 S31: 0.0211 S32: -0.1163 S33: 0.0309
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 341 THROUGH 346 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3423 53.9532 22.5679
REMARK 3 T TENSOR
REMARK 3 T11: 0.2755 T22: 0.3874
REMARK 3 T33: 0.3100 T12: 0.0083
REMARK 3 T13: 0.0705 T23: 0.0976
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 2.0000
REMARK 3 L33: 7.2670 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 9.2958
REMARK 3 S TENSOR
REMARK 3 S11: 0.6781 S12: -2.4646 S13: 0.0202
REMARK 3 S21: 0.8233 S22: -0.5248 S23: 0.2113
REMARK 3 S31: 0.4862 S32: -0.2315 S33: -0.1538
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5L0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97741
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31866
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.280
REMARK 200 RESOLUTION RANGE LOW (A) : 39.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4KU8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M LITHIUM SULFATE MONOHYDRATE. 0.1
REMARK 280 M SODIUM ACETATE TRIHYDRATE PH 4.0, 4% V/V POLYETHYLENE GLYCOL
REMARK 280 200, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 19.94450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.22500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.15250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.22500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.94450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.15250
REMARK 290 SMTRY3 4 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 GLY A 217
REMARK 465 SER A 218
REMARK 465 THR A 219
REMARK 465 SER A 347
REMARK 465 ASN A 348
REMARK 465 LYS A 349
REMARK 465 ALA A 350
REMARK 465 TYR A 351
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 GLY A 220 N
REMARK 470 LEU A 221 CD1 CD2
REMARK 470 VAL A 251 CG1
REMARK 470 GLU A 253 CD OE1 OE2
REMARK 470 GLU A 258 CG CD OE1 OE2
REMARK 470 LYS A 278 CE NZ
REMARK 470 LYS A 301 NZ
REMARK 470 ARG A 333 CZ NH1 NH2
REMARK 470 LYS A 337 CD CE NZ
REMARK 470 ASP A 344 CG OD1 OD2
REMARK 470 ASP A 345 CG OD1 OD2
REMARK 470 VAL A 346 C O CB CG1 CG2
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 509 O HOH A 573 1.91
REMARK 500 O2 EDO A 402 O HOH A 501 1.94
REMARK 500 O HOH A 509 O HOH A 593 2.01
REMARK 500 OD2 ASP A 332 O HOH A 502 2.12
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 324 -174.88 -178.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6ZA A 406
DBREF 5L0N A 219 351 UNP Q13976 KGP1_HUMAN 219 351
SEQADV 5L0N GLY A 217 UNP Q13976 EXPRESSION TAG
SEQADV 5L0N SER A 218 UNP Q13976 EXPRESSION TAG
SEQRES 1 A 135 GLY SER THR GLY LEU ILE LYS HIS THR GLU TYR MET GLU
SEQRES 2 A 135 PHE LEU LYS SER VAL PRO THR PHE GLN SER LEU PRO GLU
SEQRES 3 A 135 GLU ILE LEU SER LYS LEU ALA ASP VAL LEU GLU GLU THR
SEQRES 4 A 135 HIS TYR GLU ASN GLY GLU TYR ILE ILE ARG GLN GLY ALA
SEQRES 5 A 135 ARG GLY ASP THR PHE PHE ILE ILE SER LYS GLY THR VAL
SEQRES 6 A 135 ASN VAL THR ARG GLU ASP SER PRO SER GLU ASP PRO VAL
SEQRES 7 A 135 PHE LEU ARG THR LEU GLY LYS GLY ASP TRP PHE GLY GLU
SEQRES 8 A 135 LYS ALA LEU GLN GLY GLU ASP VAL ARG THR ALA ASN VAL
SEQRES 9 A 135 ILE ALA ALA GLU ALA VAL THR CYS LEU VAL ILE ASP ARG
SEQRES 10 A 135 ASP SER PHE LYS HIS LEU ILE GLY GLY LEU ASP ASP VAL
SEQRES 11 A 135 SER ASN LYS ALA TYR
HET SO4 A 401 5
HET EDO A 402 10
HET EDO A 403 10
HET EDO A 404 10
HET CA A 405 1
HET 6ZA A 406 34
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CA CALCIUM ION
HETNAM 6ZA 2-AMINO-9-[(2R,4AR,6R,7R,7AS)-2,7-DIHYDROXY-2-
HETNAM 2 6ZA SULFANYLIDENETETRAHYDRO-2H,4H-2LAMBDA~5~-FURO[3,2-
HETNAM 3 6ZA D][1,3,2]DIOXAPHOSPHININ-6-YL]-3,9-DIHYDRO-6H-PURIN-6-
HETNAM 4 6ZA ONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 O4 S 2-
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 CA CA 2+
FORMUL 7 6ZA C10 H12 N5 O6 P S
FORMUL 8 HOH *141(H2 O)
HELIX 1 AA1 LYS A 223 SER A 233 1 11
HELIX 2 AA2 VAL A 234 GLN A 238 5 5
HELIX 3 AA3 PRO A 241 LEU A 252 1 12
HELIX 4 AA4 GLY A 306 GLY A 312 5 7
HELIX 5 AA5 ARG A 333 GLY A 341 1 9
HELIX 6 AA6 GLY A 342 VAL A 346 5 5
SHEET 1 AA1 4 GLU A 253 TYR A 257 0
SHEET 2 AA1 4 VAL A 326 ASP A 332 -1 O VAL A 330 N GLU A 253
SHEET 3 AA1 4 THR A 272 LYS A 278 -1 N ILE A 275 O LEU A 329
SHEET 4 AA1 4 TRP A 304 PHE A 305 -1 O PHE A 305 N PHE A 274
SHEET 1 AA2 4 TYR A 262 ILE A 264 0
SHEET 2 AA2 4 ASN A 319 ALA A 322 -1 O VAL A 320 N ILE A 263
SHEET 3 AA2 4 VAL A 281 ARG A 285 -1 N THR A 284 O ASN A 319
SHEET 4 AA2 4 VAL A 294 LEU A 299 -1 O ARG A 297 N VAL A 283
LINK CA CA A 405 O HOH A 616 1555 1555 3.09
SITE 1 AC1 8 TRP A 304 PHE A 305 GLY A 306 GLU A 307
SITE 2 AC1 8 6ZA A 406 HOH A 503 HOH A 522 HOH A 535
SITE 1 AC2 6 LYS A 247 THR A 284 PHE A 295 HIS A 338
SITE 2 AC2 6 HOH A 501 HOH A 550
SITE 1 AC3 3 ARG A 285 6ZA A 406 HOH A 571
SITE 1 AC4 3 GLY A 270 ASP A 271 ASP A 314
SITE 1 AC5 2 ARG A 269 HOH A 616
SITE 1 AC6 14 ILE A 264 LEU A 296 ARG A 297 PHE A 305
SITE 2 AC6 14 GLY A 306 LYS A 308 ARG A 316 THR A 317
SITE 3 AC6 14 ALA A 318 VAL A 320 SO4 A 401 EDO A 403
SITE 4 AC6 14 HOH A 522 HOH A 571
CRYST1 39.889 54.305 56.450 90.00 90.00 90.00 P 21 21 21 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 0.025069 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017715 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
