HEADER TRANSFERASE 14-MAR-18 6CQD
TITLE CRYSTAL STRUCTURE OF HPK1 IN COMPLEX WITH ATP ANALOGUE (AMPPNP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HKP1, HEMATOPOIETIC PROGENITOR KINASE, MAPK/ERK KINASE
COMPND 5 KINASE KINASE 1, MEKKK 1;
COMPND 6 EC: 2.7.11.1;
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: MAP4K1, HPK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.WU,I.LEHOUX,Y.FRANKE,K.MORTARA,W.WANG
REVDAT 3 13-MAR-24 6CQD 1 LINK
REVDAT 2 16-JAN-19 6CQD 1 JRNL
REVDAT 1 19-DEC-18 6CQD 0
JRNL AUTH P.WU,C.J.SNEERINGER,K.E.PITTS,E.S.DAY,B.K.CHAN,B.WEI,
JRNL AUTH 2 I.LEHOUX,K.MORTARA,H.LI,J.WU,Y.FRANKE,J.G.MOFFAT,J.L.GROGAN,
JRNL AUTH 3 T.P.HEFFRON,W.WANG
JRNL TITL HEMATOPOIETIC PROGENITOR KINASE-1 STRUCTURE IN A
JRNL TITL 2 DOMAIN-SWAPPED DIMER.
JRNL REF STRUCTURE V. 27 125 2019
JRNL REFN ISSN 1878-4186
JRNL PMID 30503777
JRNL DOI 10.1016/J.STR.2018.10.025
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 34951
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3303
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 46.9981 - 6.1109 0.99 2654 156 0.1503 0.1715
REMARK 3 2 6.1109 - 4.8520 0.95 2523 165 0.1570 0.1847
REMARK 3 3 4.8520 - 4.2391 0.98 2618 158 0.1330 0.1855
REMARK 3 4 4.2391 - 3.8517 0.98 2622 147 0.1514 0.1975
REMARK 3 5 3.8517 - 3.5758 0.96 2570 151 0.1787 0.2097
REMARK 3 6 3.5758 - 3.3650 0.96 2614 132 0.1951 0.2616
REMARK 3 7 3.3650 - 3.1965 0.93 2523 120 0.2184 0.3349
REMARK 3 8 3.1965 - 3.0574 0.96 2549 116 0.2346 0.3037
REMARK 3 9 3.0574 - 2.9397 0.97 2637 145 0.2417 0.2869
REMARK 3 10 2.9397 - 2.8383 0.97 2561 147 0.2437 0.2855
REMARK 3 11 2.8383 - 2.7496 0.97 2588 158 0.2463 0.2955
REMARK 3 12 2.7496 - 2.6710 0.97 2618 119 0.2367 0.2894
REMARK 3 13 2.6710 - 2.6007 0.97 2628 119 0.2453 0.3362
REMARK 3 14 2.6007 - 2.5372 0.97 2636 135 0.2379 0.2966
REMARK 3 15 2.5372 - 2.4795 0.96 2607 121 0.2483 0.3021
REMARK 3 16 2.4795 - 2.4268 0.96 2522 138 0.2505 0.3309
REMARK 3 17 2.4268 - 2.3782 0.95 2580 111 0.2435 0.2846
REMARK 3 18 2.3782 - 2.3334 0.92 2437 158 0.2705 0.3244
REMARK 3 19 2.3334 - 2.2917 0.92 2494 141 0.2615 0.3597
REMARK 3 20 2.2917 - 2.2528 0.94 2523 120 0.2777 0.3298
REMARK 3 21 2.2528 - 2.2165 0.95 2622 166 0.2840 0.3310
REMARK 3 22 2.2165 - 2.1824 0.96 2497 146 0.2926 0.3008
REMARK 3 23 2.1824 - 2.1503 0.95 2610 104 0.2966 0.3504
REMARK 3 24 2.1503 - 2.1200 0.94 2527 130 0.3243 0.4060
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.010
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 : 0.005 4749
REMARK 3 ANGLE : 0.847 6415
REMARK 3 CHIRALITY : 0.030 719
REMARK 3 PLANARITY : 0.004 802
REMARK 3 DIHEDRAL : 14.486 1763
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESI 2:93
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4348 9.5852 12.8207
REMARK 3 T TENSOR
REMARK 3 T11: 0.3404 T22: 0.2227
REMARK 3 T33: 0.3081 T12: 0.0688
REMARK 3 T13: -0.0513 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.3843 L22: 0.2132
REMARK 3 L33: 0.5661 L12: 0.2034
REMARK 3 L13: 0.0040 L23: -0.1443
REMARK 3 S TENSOR
REMARK 3 S11: -0.1610 S12: -0.0468 S13: 0.0502
REMARK 3 S21: 0.1183 S22: 0.0745 S23: -0.0592
REMARK 3 S31: -0.5241 S32: -0.0580 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESI 94:294
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5789 -10.2274 26.9589
REMARK 3 T TENSOR
REMARK 3 T11: 0.1432 T22: 0.1518
REMARK 3 T33: 0.1844 T12: -0.0192
REMARK 3 T13: 0.0011 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.6434 L22: 0.9380
REMARK 3 L33: 1.8027 L12: -0.1932
REMARK 3 L13: 0.3552 L23: 0.0944
REMARK 3 S TENSOR
REMARK 3 S11: 0.0332 S12: -0.0403 S13: -0.0245
REMARK 3 S21: 0.0958 S22: -0.0582 S23: 0.0512
REMARK 3 S31: 0.0325 S32: -0.1285 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND RESI 4:93
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7691 24.9088 59.5205
REMARK 3 T TENSOR
REMARK 3 T11: 0.3650 T22: 0.5224
REMARK 3 T33: 0.3887 T12: 0.0772
REMARK 3 T13: 0.0357 T23: 0.0710
REMARK 3 L TENSOR
REMARK 3 L11: 0.1772 L22: 0.4252
REMARK 3 L33: 0.3893 L12: 0.0593
REMARK 3 L13: 0.1403 L23: 0.0294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0363 S12: 0.1278 S13: 0.0231
REMARK 3 S21: -0.3596 S22: 0.1569 S23: -0.0654
REMARK 3 S31: -0.2569 S32: -0.2039 S33: 0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESI 94:294
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4382 4.1211 61.2632
REMARK 3 T TENSOR
REMARK 3 T11: 0.4161 T22: 0.2129
REMARK 3 T33: 0.1787 T12: 0.0322
REMARK 3 T13: 0.0662 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.5888 L22: -0.2162
REMARK 3 L33: 1.1237 L12: -0.5525
REMARK 3 L13: 0.2566 L23: 0.3176
REMARK 3 S TENSOR
REMARK 3 S11: -0.1015 S12: -0.0684 S13: 0.0713
REMARK 3 S21: -0.1237 S22: -0.0165 S23: -0.0101
REMARK 3 S31: 0.6599 S32: -0.0044 S33: -0.1307
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 6CQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233214.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35007
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 12% PEG8000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 73.44300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.94100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.44300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.94100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 519 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 GLY A 0
REMARK 465 SER A 1
REMARK 465 LYS A 49
REMARK 465 MET A 50
REMARK 465 GLU A 51
REMARK 465 PRO A 52
REMARK 465 ASN A 295
REMARK 465 SER A 296
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASP B 2
REMARK 465 VAL B 3
REMARK 465 ASN B 295
REMARK 465 SER B 296
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 54 -145.26 -89.02
REMARK 500 LEU A 84 -121.52 49.62
REMARK 500 GLN A 85 32.98 -98.32
REMARK 500 ARG A 136 -6.64 70.86
REMARK 500 ASP A 155 83.06 65.60
REMARK 500 LEU A 188 -65.55 -90.01
REMARK 500 LEU A 255 40.96 -92.97
REMARK 500 ASN A 293 -95.35 -117.27
REMARK 500 LEU B 20 -102.69 -114.19
REMARK 500 ASP B 137 39.07 -145.98
REMARK 500 ASP B 155 77.54 58.68
REMARK 500 PHE B 156 33.74 -93.97
REMARK 500 LYS B 189 60.83 -172.59
REMARK 500 LEU B 211 -2.32 71.95
REMARK 500 LEU B 255 47.80 -92.43
REMARK 500 ASN B 293 -87.74 -139.85
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 B 492 DISTANCE = 5.85 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 A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 142 OD1
REMARK 620 2 ASP A 155 OD2 86.1
REMARK 620 3 ANP A 301 O1G 152.0 119.6
REMARK 620 4 ANP A 301 O2A 98.8 61.8 103.1
REMARK 620 5 HOH A 402 O 93.8 173.6 62.0 112.0
REMARK 620 6 HOH A 445 O 96.0 81.6 78.5 139.1 104.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 155 OD1
REMARK 620 2 ASP A 155 OD2 62.0
REMARK 620 3 ANP A 301 O3G 130.2 84.6
REMARK 620 4 ANP A 301 O2B 84.9 87.7 56.2
REMARK 620 5 HOH A 405 O 137.3 93.7 75.7 131.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 142 OD1
REMARK 620 2 ASP B 155 OD2 88.4
REMARK 620 3 ANP B 302 O2G 162.3 94.3
REMARK 620 4 ANP B 302 O3A 134.7 66.0 61.4
REMARK 620 5 ANP B 302 O2A 82.6 86.0 115.1 60.0
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 ANP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 302
DBREF 6CQD A 2 293 UNP Q92918 M4K1_HUMAN 2 293
DBREF 6CQD B 2 293 UNP Q92918 M4K1_HUMAN 2 293
SEQADV 6CQD GLY A 0 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD SER A 1 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD GLU A 165 UNP Q92918 THR 165 CONFLICT
SEQADV 6CQD GLU A 171 UNP Q92918 SER 171 CONFLICT
SEQADV 6CQD GLY A 294 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD ASN A 295 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD SER A 296 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD GLY B 0 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD SER B 1 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD GLU B 165 UNP Q92918 THR 165 CONFLICT
SEQADV 6CQD GLU B 171 UNP Q92918 SER 171 CONFLICT
SEQADV 6CQD GLY B 294 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD ASN B 295 UNP Q92918 EXPRESSION TAG
SEQADV 6CQD SER B 296 UNP Q92918 EXPRESSION TAG
SEQRES 1 A 297 GLY SER ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG ASP
SEQRES 2 A 297 PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY GLY
SEQRES 3 A 297 GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS VAL
SEQRES 4 A 297 SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET GLU
SEQRES 5 A 297 PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE LEU
SEQRES 6 A 297 ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA TYR
SEQRES 7 A 297 HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE CYS
SEQRES 8 A 297 MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE TYR
SEQRES 9 A 297 GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER TYR
SEQRES 10 A 297 VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU HIS
SEQRES 11 A 297 SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA ASN
SEQRES 12 A 297 ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA ASP
SEQRES 13 A 297 PHE GLY ILE SER ALA GLN ILE GLY ALA GLU LEU ALA ARG
SEQRES 14 A 297 ARG LEU GLU PHE ILE GLY THR PRO TYR TRP MET ALA PRO
SEQRES 15 A 297 GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN GLU
SEQRES 16 A 297 LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE GLU
SEQRES 17 A 297 LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS PRO
SEQRES 18 A 297 LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR GLN
SEQRES 19 A 297 PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA ALA
SEQRES 20 A 297 PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER PRO
SEQRES 21 A 297 LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS GLN
SEQRES 22 A 297 LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE LEU
SEQRES 23 A 297 ASP LEU LEU ASP LYS LEU LYS ASN GLY ASN SER
SEQRES 1 B 297 GLY SER ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG ASP
SEQRES 2 B 297 PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY GLY
SEQRES 3 B 297 GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS VAL
SEQRES 4 B 297 SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET GLU
SEQRES 5 B 297 PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE LEU
SEQRES 6 B 297 ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA TYR
SEQRES 7 B 297 HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE CYS
SEQRES 8 B 297 MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE TYR
SEQRES 9 B 297 GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER TYR
SEQRES 10 B 297 VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU HIS
SEQRES 11 B 297 SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA ASN
SEQRES 12 B 297 ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA ASP
SEQRES 13 B 297 PHE GLY ILE SER ALA GLN ILE GLY ALA GLU LEU ALA ARG
SEQRES 14 B 297 ARG LEU GLU PHE ILE GLY THR PRO TYR TRP MET ALA PRO
SEQRES 15 B 297 GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN GLU
SEQRES 16 B 297 LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE GLU
SEQRES 17 B 297 LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS PRO
SEQRES 18 B 297 LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR GLN
SEQRES 19 B 297 PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA ALA
SEQRES 20 B 297 PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER PRO
SEQRES 21 B 297 LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS GLN
SEQRES 22 B 297 LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE LEU
SEQRES 23 B 297 ASP LEU LEU ASP LYS LEU LYS ASN GLY ASN SER
HET ANP A 301 31
HET MG A 302 1
HET MG A 303 1
HET MG B 301 1
HET ANP B 302 31
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 3 ANP 2(C10 H17 N6 O12 P3)
FORMUL 4 MG 3(MG 2+)
FORMUL 8 HOH *217(H2 O)
HELIX 1 AA1 ASP A 12 ASP A 15 5 4
HELIX 2 AA2 ASP A 55 GLN A 60 1 6
HELIX 3 AA3 GLN A 60 CYS A 69 1 10
HELIX 4 AA4 SER A 98 GLY A 107 1 10
HELIX 5 AA5 SER A 110 GLN A 131 1 22
HELIX 6 AA6 LYS A 139 ALA A 141 5 3
HELIX 7 AA7 PHE A 156 ARG A 168 1 13
HELIX 8 AA8 THR A 175 MET A 179 5 5
HELIX 9 AA9 ALA A 180 GLY A 190 1 11
HELIX 10 AB1 GLU A 194 LEU A 211 1 18
HELIX 11 AB2 HIS A 219 LYS A 229 1 11
HELIX 12 AB3 SER A 244 LEU A 255 1 12
HELIX 13 AB4 SER A 264 LEU A 269 1 6
HELIX 14 AB5 SER A 270 SER A 275 5 6
HELIX 15 AB6 ARG A 281 ASN A 293 1 13
HELIX 16 AB7 ASP B 12 ASP B 15 5 4
HELIX 17 AB8 VAL B 56 THR B 68 1 13
HELIX 18 AB9 LEU B 99 GLY B 107 1 9
HELIX 19 AC1 SER B 110 SER B 130 1 21
HELIX 20 AC2 LYS B 139 ALA B 141 5 3
HELIX 21 AC3 PHE B 156 GLU B 171 1 16
HELIX 22 AC4 ALA B 180 GLY B 190 1 11
HELIX 23 AC5 LEU B 195 LEU B 211 1 17
HELIX 24 AC6 HIS B 219 LYS B 229 1 11
HELIX 25 AC7 SER B 244 LEU B 255 1 12
HELIX 26 AC8 SER B 264 SER B 270 1 7
HELIX 27 AC9 HIS B 271 GLN B 276 1 6
HELIX 28 AD1 ARG B 281 LYS B 292 1 12
SHEET 1 AA1 5 TYR A 17 GLY A 24 0
SHEET 2 AA1 5 VAL A 31 ASP A 36 -1 O VAL A 31 N LEU A 23
SHEET 3 AA1 5 LEU A 42 MET A 47 -1 O LEU A 45 N PHE A 32
SHEET 4 AA1 5 LYS A 86 GLU A 92 -1 O ILE A 89 N LYS A 46
SHEET 5 AA1 5 TYR A 77 TRP A 83 -1 N GLY A 79 O CYS A 90
SHEET 1 AA2 2 ILE A 143 ILE A 145 0
SHEET 2 AA2 2 VAL A 151 LEU A 153 -1 O ARG A 152 N LEU A 144
SHEET 1 AA3 5 TYR B 17 GLY B 24 0
SHEET 2 AA3 5 GLY B 29 ASP B 36 -1 O VAL B 31 N LEU B 23
SHEET 3 AA3 5 LEU B 42 LYS B 49 -1 O LEU B 45 N PHE B 32
SHEET 4 AA3 5 LYS B 86 GLU B 92 -1 O LEU B 87 N VAL B 48
SHEET 5 AA3 5 TYR B 77 TRP B 83 -1 N TYR B 81 O TRP B 88
SHEET 1 AA4 3 GLY B 97 SER B 98 0
SHEET 2 AA4 3 ILE B 143 ILE B 145 -1 O ILE B 145 N GLY B 97
SHEET 3 AA4 3 VAL B 151 LEU B 153 -1 O ARG B 152 N LEU B 144
LINK OD1 ASN A 142 MG MG A 302 1555 1555 2.17
LINK OD2 ASP A 155 MG MG A 302 1555 1555 2.15
LINK OD1 ASP A 155 MG MG A 303 1555 1555 2.18
LINK OD2 ASP A 155 MG MG A 303 1555 1555 2.12
LINK O1G ANP A 301 MG MG A 302 1555 1555 2.16
LINK O2A ANP A 301 MG MG A 302 1555 1555 2.15
LINK O3G ANP A 301 MG MG A 303 1555 1555 2.21
LINK O2B ANP A 301 MG MG A 303 1555 1555 2.29
LINK MG MG A 302 O HOH A 402 1555 1555 2.15
LINK MG MG A 302 O HOH A 445 1555 1555 2.17
LINK MG MG A 303 O HOH A 405 1555 1555 2.14
LINK OD1 ASN B 142 MG MG B 301 1555 1555 2.17
LINK OD2 ASP B 155 MG MG B 301 1555 1555 2.17
LINK MG MG B 301 O2G ANP B 302 1555 1555 2.17
LINK MG MG B 301 O3A ANP B 302 1555 1555 2.72
LINK MG MG B 301 O2A ANP B 302 1555 1555 2.17
SITE 1 AC1 21 LEU A 23 GLY A 26 VAL A 31 ALA A 44
SITE 2 AC1 21 LYS A 46 MET A 91 GLU A 92 CYS A 94
SITE 3 AC1 21 ASP A 101 ALA A 141 ASN A 142 LEU A 144
SITE 4 AC1 21 ASP A 155 MG A 302 MG A 303 HOH A 402
SITE 5 AC1 21 HOH A 405 HOH A 418 HOH A 445 HOH A 480
SITE 6 AC1 21 HOH A 498
SITE 1 AC2 5 ASN A 142 ASP A 155 ANP A 301 HOH A 402
SITE 2 AC2 5 HOH A 445
SITE 1 AC3 3 ASP A 155 ANP A 301 HOH A 405
SITE 1 AC4 3 ASN B 142 ASP B 155 ANP B 302
SITE 1 AC5 15 LEU B 23 GLY B 25 GLY B 26 VAL B 31
SITE 2 AC5 15 ALA B 44 LYS B 46 MET B 91 GLU B 92
SITE 3 AC5 15 CYS B 94 ASP B 101 ALA B 141 ASN B 142
SITE 4 AC5 15 LEU B 144 ASP B 155 MG B 301
CRYST1 146.886 51.882 107.500 90.00 131.03 90.00 C 1 2 1 8
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 0.006808 0.000000 0.005924 0.00000
SCALE2 0.000000 0.019275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END