HEADER PROTEIN BINDING 31-MAR-16 5J48
TITLE PKG I'S CARBOYL TERMINAL CYCLIC NUCLEOTIDE BINDING DOMAIN (CNB-B) IN A
TITLE 2 COMPLEX WITH 8-PCPT-CGMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-DEPENDENT PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 204-336;
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 II, MUTAGENESIS, SITE-DIRECTED, PROTEIN BINDING, ANALOGS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.CAMPBELL,B.SANKARAN,C.W.KIM
REVDAT 4 27-SEP-23 5J48 1 LINK
REVDAT 3 27-SEP-17 5J48 1 JRNL
REVDAT 2 23-AUG-17 5J48 1 JRNL
REVDAT 1 12-APR-17 5J48 0
JRNL AUTH J.C.CAMPBELL,P.HENNING,E.FRANZ,B.SANKARAN,F.W.HERBERG,C.KIM
JRNL TITL STRUCTURAL BASIS OF ANALOG SPECIFICITY IN PKG I AND II.
JRNL REF ACS CHEM. BIOL. V. 12 2388 2017
JRNL REFN ESSN 1554-8937
JRNL PMID 28793191
JRNL DOI 10.1021/ACSCHEMBIO.7B00369
REMARK 2
REMARK 2 RESOLUTION. 1.49 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 44528
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.490
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 34.9617 - 3.5900 0.98 3093 146 0.1680 0.1957
REMARK 3 2 3.5900 - 2.8499 0.99 3074 144 0.1506 0.1845
REMARK 3 3 2.8499 - 2.4898 1.00 3056 144 0.1484 0.1729
REMARK 3 4 2.4898 - 2.2622 0.99 3043 143 0.1461 0.1628
REMARK 3 5 2.2622 - 2.1000 0.99 3019 142 0.1415 0.1666
REMARK 3 6 2.1000 - 1.9762 0.99 3037 143 0.1490 0.1798
REMARK 3 7 1.9762 - 1.8773 0.99 3041 142 0.1626 0.1888
REMARK 3 8 1.8773 - 1.7956 0.99 3040 143 0.1659 0.1782
REMARK 3 9 1.7956 - 1.7264 0.99 3045 143 0.1784 0.1913
REMARK 3 10 1.7264 - 1.6669 0.99 3037 142 0.1863 0.2127
REMARK 3 11 1.6669 - 1.6147 0.99 3021 143 0.1893 0.2216
REMARK 3 12 1.6147 - 1.5686 0.99 3033 143 0.2018 0.2245
REMARK 3 13 1.5686 - 1.5273 0.99 3017 141 0.2258 0.2450
REMARK 3 14 1.5273 - 1.4900 0.97 2974 139 0.2566 0.2957
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.990
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 : 0.012 2150
REMARK 3 ANGLE : 1.253 2904
REMARK 3 CHIRALITY : 0.084 331
REMARK 3 PLANARITY : 0.006 362
REMARK 3 DIHEDRAL : 15.284 745
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 217 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6536 -7.9562 -37.9025
REMARK 3 T TENSOR
REMARK 3 T11: 0.1679 T22: 0.0822
REMARK 3 T33: 0.1645 T12: 0.0121
REMARK 3 T13: 0.0215 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 4.6881 L22: 1.0581
REMARK 3 L33: 1.9102 L12: 1.9686
REMARK 3 L13: 1.2160 L23: 1.1150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: -0.0227 S13: -0.2159
REMARK 3 S21: -0.0058 S22: 0.0459 S23: -0.1117
REMARK 3 S31: 0.2449 S32: 0.0919 S33: -0.0236
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 252 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8160 8.7287 -28.1533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.0633
REMARK 3 T33: 0.1290 T12: -0.0078
REMARK 3 T13: 0.0120 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 1.5863 L22: 2.8517
REMARK 3 L33: 3.4290 L12: -0.2818
REMARK 3 L13: -0.3148 L23: 0.2696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: -0.0195 S13: 0.0055
REMARK 3 S21: -0.0874 S22: 0.0022 S23: 0.0533
REMARK 3 S31: 0.0400 S32: -0.0361 S33: 0.0166
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 340 THROUGH 351 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2044 -0.2814 -21.7439
REMARK 3 T TENSOR
REMARK 3 T11: 0.3621 T22: 0.4542
REMARK 3 T33: 0.3996 T12: 0.0156
REMARK 3 T13: 0.0765 T23: 0.1288
REMARK 3 L TENSOR
REMARK 3 L11: 3.7032 L22: 1.0251
REMARK 3 L33: 2.0016 L12: 1.9492
REMARK 3 L13: 2.7237 L23: 1.4332
REMARK 3 S TENSOR
REMARK 3 S11: 0.3760 S12: 0.1300 S13: -0.0390
REMARK 3 S21: 0.0744 S22: -0.2764 S23: -0.3408
REMARK 3 S31: 0.1517 S32: 0.2656 S33: -0.1011
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 217 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9920 -14.4179 4.7225
REMARK 3 T TENSOR
REMARK 3 T11: 0.1319 T22: 0.0501
REMARK 3 T33: 0.1268 T12: -0.0043
REMARK 3 T13: 0.0299 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 6.6959 L22: 2.7927
REMARK 3 L33: 2.1287 L12: -1.9810
REMARK 3 L13: 0.6312 L23: -0.2654
REMARK 3 S TENSOR
REMARK 3 S11: -0.1092 S12: 0.0334 S13: -0.1253
REMARK 3 S21: 0.0821 S22: 0.0846 S23: 0.0940
REMARK 3 S31: 0.2417 S32: -0.0568 S33: 0.0159
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 252 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8805 3.6108 -2.1910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0563
REMARK 3 T33: 0.1149 T12: 0.0080
REMARK 3 T13: 0.0057 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.8313 L22: 3.5704
REMARK 3 L33: 4.0905 L12: 0.8491
REMARK 3 L13: -0.2387 L23: -1.8643
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: -0.0110 S13: -0.0007
REMARK 3 S21: 0.0378 S22: -0.0233 S23: -0.3170
REMARK 3 S31: -0.0229 S32: 0.1669 S33: 0.0547
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 286 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8527 5.5863 -10.2146
REMARK 3 T TENSOR
REMARK 3 T11: 0.0899 T22: 0.1110
REMARK 3 T33: 0.0883 T12: -0.0414
REMARK 3 T13: -0.0170 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 3.2399 L22: 4.2733
REMARK 3 L33: 5.0993 L12: 0.1036
REMARK 3 L13: -0.8281 L23: -1.6403
REMARK 3 S TENSOR
REMARK 3 S11: -0.0675 S12: 0.3456 S13: 0.1200
REMARK 3 S21: -0.3733 S22: 0.1391 S23: 0.0589
REMARK 3 S31: -0.0199 S32: -0.1378 S33: -0.0527
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 319 THROUGH 343 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4660 -4.1472 -4.0918
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.1063
REMARK 3 T33: 0.1343 T12: -0.0126
REMARK 3 T13: 0.0326 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.2675 L22: 6.4374
REMARK 3 L33: 2.0266 L12: -0.7337
REMARK 3 L13: 0.7749 L23: 0.7478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0768 S12: 0.1320 S13: -0.1582
REMARK 3 S21: -0.1378 S22: -0.0603 S23: -0.0990
REMARK 3 S31: 0.2477 S32: -0.0128 S33: -0.0289
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 5J48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000217487.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5-4.8
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 : 44551
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 59.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4KU7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 200 MM CAAC, 0.1M NAAC PH
REMARK 280 4.5-4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 29.62000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 SER A 288
REMARK 465 PRO A 289
REMARK 465 SER A 290
REMARK 465 GLU A 291
REMARK 465 ASP B 344
REMARK 465 ASP B 345
REMARK 465 VAL B 346
REMARK 465 SER B 347
REMARK 465 ASN B 348
REMARK 465 LYS B 349
REMARK 465 ALA B 350
REMARK 465 TYR B 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 LYS A 223 CE NZ
REMARK 470 GLU A 243 CG CD OE1 OE2
REMARK 470 GLU A 253 OE1 OE2
REMARK 470 LYS A 278 NZ
REMARK 470 ASP A 287 CG OD1 OD2
REMARK 470 ASP A 292 CG OD1 OD2
REMARK 470 GLN A 311 CG CD OE1 NE2
REMARK 470 LYS A 337 CD CE NZ
REMARK 470 ASP A 345 CG OD1 OD2
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 LYS B 232 NZ
REMARK 470 GLU B 242 CD OE1 OE2
REMARK 470 GLU B 243 CG CD OE1 OE2
REMARK 470 GLU B 253 OE2
REMARK 470 LYS B 278 CE NZ
REMARK 470 ASP B 292 CG OD1 OD2
REMARK 470 GLU B 313 CG CD OE1 OE2
REMARK 470 LYS B 337 CD CE NZ
REMARK 470 LEU B 343 C O
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 HG1 THR B 317 H311 6FW B 405 1.33
REMARK 500 O HOH B 585 O HOH B 591 1.91
REMARK 500 O HOH A 508 O HOH A 609 1.93
REMARK 500 O HOH A 545 O HOH A 577 1.95
REMARK 500 O HOH A 549 O HOH A 580 1.96
REMARK 500 O HOH B 630 O HOH B 632 1.96
REMARK 500 O HOH B 583 O HOH B 620 1.98
REMARK 500 O HOH B 631 O HOH B 636 1.99
REMARK 500 O HOH A 523 O HOH A 610 2.01
REMARK 500 O HOH B 526 O HOH B 598 2.01
REMARK 500 O HOH B 624 O HOH B 629 2.03
REMARK 500 O HOH B 553 O HOH B 615 2.04
REMARK 500 O HOH B 521 O HOH B 611 2.06
REMARK 500 O HOH A 540 O HOH A 549 2.08
REMARK 500 O HOH B 519 O HOH B 629 2.10
REMARK 500 O HOH A 619 O HOH A 624 2.12
REMARK 500 O HOH A 531 O HOH A 603 2.15
REMARK 500 O HOH B 539 O HOH B 543 2.17
REMARK 500 O HOH B 603 O HOH B 617 2.17
REMARK 500 O HOH A 599 O HOH A 618 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 595 O HOH B 553 2555 2.00
REMARK 500 O HOH A 631 O HOH B 639 1554 2.08
REMARK 500 O HOH A 586 O HOH A 591 2554 2.10
REMARK 500 O HOH B 610 O HOH B 627 2455 2.14
REMARK 500 O HOH A 623 O HOH B 527 1554 2.17
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 271 14.39 -140.63
REMARK 500 GLU A 324 -171.10 -176.84
REMARK 500 ASP B 287 -80.36 -107.18
REMARK 500 GLU B 324 -170.61 -177.41
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 639 DISTANCE = 7.02 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 NA A 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 308 O
REMARK 620 2 GLN A 311 O 86.0
REMARK 620 3 GLU A 313 O 109.6 87.2
REMARK 620 4 EDO A 403 O2 132.7 99.7 117.5
REMARK 620 5 HOH A 573 O 93.3 168.6 82.3 89.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 348 O
REMARK 620 2 LYS B 308 O 41.6
REMARK 620 3 GLN B 311 O 40.2 4.7
REMARK 620 4 GLU B 313 O 37.3 4.3 4.6
REMARK 620 5 HOH B 571 O 36.4 5.7 7.7 3.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO 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 6FW A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6FW B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 407
DBREF 5J48 A 219 351 UNP Q13976 KGP1_HUMAN 204 336
DBREF 5J48 B 219 351 UNP Q13976 KGP1_HUMAN 204 336
SEQADV 5J48 GLY A 217 UNP Q13976 EXPRESSION TAG
SEQADV 5J48 SER A 218 UNP Q13976 EXPRESSION TAG
SEQADV 5J48 GLY B 217 UNP Q13976 EXPRESSION TAG
SEQADV 5J48 SER B 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
SEQRES 1 B 135 GLY SER THR GLY LEU ILE LYS HIS THR GLU TYR MET GLU
SEQRES 2 B 135 PHE LEU LYS SER VAL PRO THR PHE GLN SER LEU PRO GLU
SEQRES 3 B 135 GLU ILE LEU SER LYS LEU ALA ASP VAL LEU GLU GLU THR
SEQRES 4 B 135 HIS TYR GLU ASN GLY GLU TYR ILE ILE ARG GLN GLY ALA
SEQRES 5 B 135 ARG GLY ASP THR PHE PHE ILE ILE SER LYS GLY THR VAL
SEQRES 6 B 135 ASN VAL THR ARG GLU ASP SER PRO SER GLU ASP PRO VAL
SEQRES 7 B 135 PHE LEU ARG THR LEU GLY LYS GLY ASP TRP PHE GLY GLU
SEQRES 8 B 135 LYS ALA LEU GLN GLY GLU ASP VAL ARG THR ALA ASN VAL
SEQRES 9 B 135 ILE ALA ALA GLU ALA VAL THR CYS LEU VAL ILE ASP ARG
SEQRES 10 B 135 ASP SER PHE LYS HIS LEU ILE GLY GLY LEU ASP ASP VAL
SEQRES 11 B 135 SER ASN LYS ALA TYR
HET EDO A 401 10
HET EDO A 402 10
HET EDO A 403 10
HET 6FW A 404 46
HET EDO A 405 10
HET NA A 406 1
HET EDO B 401 10
HET EDO B 402 10
HET EDO B 403 10
HET EDO B 404 10
HET 6FW B 405 46
HET CA B 406 1
HET NA B 407 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 6FW 2-AMINO-8-[(4-CHLOROPHENYL)SULFANYL]-9-[(2S,4AR,6R,7R,
HETNAM 2 6FW 7AS)-2,7-DIHYDROXY-2-OXOTETRAHYDRO-2H,4H-2LAMBDA~5~-
HETNAM 3 6FW FURO[3,2-D][1,3,2]DIOXAPHOSPHININ-6-YL]-3,9-DIHYDRO-
HETNAM 4 6FW 6H-PURIN-6-ONE
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 8(C2 H6 O2)
FORMUL 6 6FW 2(C16 H15 CL N5 O7 P S)
FORMUL 8 NA 2(NA 1+)
FORMUL 14 CA CA 2+
FORMUL 16 HOH *280(H2 O)
HELIX 1 AA1 SER A 218 SER A 233 1 16
HELIX 2 AA2 VAL A 234 SER A 239 1 6
HELIX 3 AA3 PRO A 241 LEU A 252 1 12
HELIX 4 AA4 GLU A 307 GLN A 311 5 5
HELIX 5 AA5 ARG A 333 ILE A 340 1 8
HELIX 6 AA6 LEU A 343 ASN A 348 1 6
HELIX 7 AA7 SER B 218 SER B 233 1 16
HELIX 8 AA8 VAL B 234 SER B 239 1 6
HELIX 9 AA9 PRO B 241 LEU B 252 1 12
HELIX 10 AB1 GLU B 307 GLN B 311 5 5
HELIX 11 AB2 ARG B 333 ILE B 340 1 8
SHEET 1 AA1 4 GLU A 253 TYR A 257 0
SHEET 2 AA1 4 VAL A 326 ASP A 332 -1 O CYS A 328 N THR A 255
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 VAL A 294 N ARG A 285
SHEET 1 AA3 4 GLU B 253 TYR B 257 0
SHEET 2 AA3 4 VAL B 326 ASP B 332 -1 O CYS B 328 N THR B 255
SHEET 3 AA3 4 THR B 272 LYS B 278 -1 N ILE B 275 O LEU B 329
SHEET 4 AA3 4 TRP B 304 PHE B 305 -1 O PHE B 305 N PHE B 274
SHEET 1 AA4 4 TYR B 262 ILE B 264 0
SHEET 2 AA4 4 ASN B 319 ALA B 322 -1 O VAL B 320 N ILE B 263
SHEET 3 AA4 4 VAL B 281 ARG B 285 -1 N THR B 284 O ASN B 319
SHEET 4 AA4 4 VAL B 294 LEU B 299 -1 O ARG B 297 N VAL B 283
LINK O LYS A 308 NA NA A 406 1555 1555 2.28
LINK O GLN A 311 NA NA A 406 1555 1555 2.22
LINK O GLU A 313 NA NA A 406 1555 1555 2.26
LINK O ASN A 348 NA NA B 407 1555 1655 2.76
LINK O2 EDO A 403 NA NA A 406 1555 1555 2.39
LINK NA NA A 406 O HOH A 573 1555 1555 2.48
LINK O LYS B 308 NA NA B 407 1555 1555 2.41
LINK O GLN B 311 NA NA B 407 1555 1555 2.40
LINK O GLU B 313 NA NA B 407 1555 1555 2.34
LINK NA NA B 407 O HOH B 571 1555 1555 2.45
SITE 1 AC1 2 HIS A 256 GLU A 261
SITE 1 AC2 4 ASP A 303 TRP A 304 6FW A 404 HOH A 539
SITE 1 AC3 6 GLN A 311 GLU A 313 EDO A 405 NA A 406
SITE 2 AC3 6 6FW B 405 CA B 406
SITE 1 AC4 17 ILE A 264 LEU A 296 ARG A 297 LEU A 299
SITE 2 AC4 17 TRP A 304 PHE A 305 GLY A 306 GLU A 307
SITE 3 AC4 17 LYS A 308 ALA A 309 ARG A 316 THR A 317
SITE 4 AC4 17 ALA A 318 TYR A 351 EDO A 402 ASP B 287
SITE 5 AC4 17 HOH B 505
SITE 1 AC5 7 LYS A 308 THR A 317 EDO A 403 HOH A 533
SITE 2 AC5 7 ARG B 285 ASP B 287 LEU B 296
SITE 1 AC6 5 LYS A 308 GLN A 311 GLU A 313 EDO A 403
SITE 2 AC6 5 HOH A 573
SITE 1 AC7 2 HIS B 338 HOH B 529
SITE 1 AC8 5 GLU B 226 TYR B 227 SER B 277 HOH B 507
SITE 2 AC8 5 HOH B 543
SITE 1 AC9 4 GLY B 220 TYR B 227 ALA B 249 HOH B 508
SITE 1 AD1 4 ASP B 303 TRP B 304 6FW B 405 HOH B 535
SITE 1 AD2 16 EDO A 403 ILE B 264 LEU B 296 ARG B 297
SITE 2 AD2 16 LEU B 299 TRP B 304 PHE B 305 GLY B 306
SITE 3 AD2 16 GLU B 307 LYS B 308 ALA B 309 ARG B 316
SITE 4 AD2 16 THR B 317 ALA B 318 EDO B 404 CA B 406
SITE 1 AD3 4 LYS A 308 EDO A 403 ARG B 285 6FW B 405
SITE 1 AD4 5 ASN A 348 LYS B 308 GLN B 311 GLU B 313
SITE 2 AD4 5 HOH B 571
CRYST1 35.510 59.240 67.320 90.00 100.17 90.00 P 1 21 1 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 0.028161 0.000000 0.005052 0.00000
SCALE2 0.000000 0.016880 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015092 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
