HEADER TRANSFERASE 31-MAR-09 2WEL
TITLE CRYSTAL STRUCTURE OF SU6656-BOUND CALCIUM/CALMODULIN-DEPENDENT PROTEIN
TITLE 2 KINASE II DELTA IN COMPLEX WITH CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA
COMPND 3 CHAIN;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: KINASE DOMAIN, RESIDUES 11-335;
COMPND 6 SYNONYM: CALCIUM CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA,
COMPND 7 CAM-KINASE II DELTA CHAIN, CAM KINASE II SUBUNIT DELTA, CAMK-II
COMPND 8 SUBUNIT DELTA;
COMPND 9 EC: 2.7.11.17;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: CALMODULIN;
COMPND 13 CHAIN: D;
COMPND 14 SYNONYM: CAM;
COMPND 15 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS CELLULAR DIFFERENTIATION, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 2 PHOSPHOPROTEIN, CALMODULIN-BINDING, CALMODULIN BINDING, KINASE,
KEYWDS 3 TRANSFERASE, ATP-BINDING, NUCLEOTIDE-BINDING, VASCULAR SMOOTH
KEYWDS 4 MUSCLE, SERINE-THREONINE KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.W.PIKE,P.RELLOS,E.SALAH,N.BURGESS-BROWN,T.KEATES,J.MUNIZ,R.SETHI,
AUTHOR 2 A.ROOS,P.FILIPPAKOPOULOS,F.VON DELFT,A.EDWARDS,J.WEIGELT,
AUTHOR 3 C.H.ARROWSMITH,C.BOUNTRA,S.KNAPP
REVDAT 5 13-DEC-23 2WEL 1 REMARK LINK
REVDAT 4 24-JAN-18 2WEL 1 AUTHOR JRNL
REVDAT 3 10-AUG-11 2WEL 1 JRNL REMARK HETSYN
REVDAT 2 13-JUL-11 2WEL 1 VERSN
REVDAT 1 14-APR-09 2WEL 0
JRNL AUTH P.RELLOS,A.C.W.PIKE,F.H.NIESEN,E.SALAH,W.H.LEE,F.VON DELFT,
JRNL AUTH 2 S.KNAPP
JRNL TITL STRUCTURE OF THE CAMKIIDELTA/CALMODULIN COMPLEX REVEALS THE
JRNL TITL 2 MOLECULAR MECHANISM OF CAMKII KINASE ACTIVATION.
JRNL REF PLOS BIOL. V. 8 426 2010
JRNL REFN ISSN 1544-9173
JRNL PMID 20668654
JRNL DOI 10.1371/JOURNAL.PBIO.1000426
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0089
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 45074
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.800
REMARK 3 FREE R VALUE TEST SET COUNT : 827
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3286
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3544
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 405
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 20.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.92000
REMARK 3 B22 (A**2) : 1.02000
REMARK 3 B33 (A**2) : 0.90000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.064
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3702 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2529 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4991 ; 1.370 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6148 ; 0.911 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 446 ; 5.207 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;32.518 ;24.590
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 657 ;12.972 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;18.403 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 543 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4078 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 728 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 755 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2422 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1791 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1772 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 330 ; 0.156 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.096 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 14 ; 0.163 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.163 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 71 ; 0.170 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.230 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.047 ; 0.200
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): 2233 ; 3.306 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 909 ; 1.101 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3596 ; 4.709 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1469 ; 7.070 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1395 ; 9.372 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 276
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2686 -14.5916 -13.2017
REMARK 3 T TENSOR
REMARK 3 T11: 0.0060 T22: 0.0226
REMARK 3 T33: 0.0759 T12: -0.0012
REMARK 3 T13: -0.0061 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.5099 L22: 0.4313
REMARK 3 L33: 1.7413 L12: 0.0989
REMARK 3 L13: -0.2262 L23: -0.1534
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: 0.0163 S13: 0.0196
REMARK 3 S21: -0.0411 S22: 0.0383 S23: 0.0360
REMARK 3 S31: -0.0394 S32: -0.1191 S33: -0.0405
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 147
REMARK 3 RESIDUE RANGE : A 294 A 316
REMARK 3 ORIGIN FOR THE GROUP (A): 88.1056 -20.6549 -51.1215
REMARK 3 T TENSOR
REMARK 3 T11: 0.1168 T22: 0.0936
REMARK 3 T33: 0.0797 T12: 0.0058
REMARK 3 T13: -0.0190 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 1.2733 L22: 2.7636
REMARK 3 L33: 1.2672 L12: -0.5723
REMARK 3 L13: 0.0713 L23: 0.5465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: 0.2130 S13: 0.0167
REMARK 3 S21: -0.3417 S22: 0.0074 S23: 0.1598
REMARK 3 S31: -0.2259 S32: -0.0702 S33: -0.0379
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. U VALUES RESIDUAL ONLY.
REMARK 4
REMARK 4 2WEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1290039286.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45901
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 33.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2VN9, 1MXE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM POTASSIUM PHOSPHATE, 20%
REMARK 280 PEG3350 10% ETHYLENE GLYCOL, PH 7.5
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 34.13000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.99000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.99000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.13000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.42500
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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 THR A 277
REMARK 465 VAL A 278
REMARK 465 ALA A 279
REMARK 465 SER A 280
REMARK 465 ALA A 317
REMARK 465 LYS A 318
REMARK 465 SER A 319
REMARK 465 LEU A 320
REMARK 465 LEU A 321
REMARK 465 LYS A 322
REMARK 465 LYS A 323
REMARK 465 PRO A 324
REMARK 465 ASP A 325
REMARK 465 GLY A 326
REMARK 465 VAL A 327
REMARK 465 LYS A 328
REMARK 465 GLU A 329
REMARK 465 SER A 330
REMARK 465 THR A 331
REMARK 465 GLU A 332
REMARK 465 SER A 333
REMARK 465 SER A 334
REMARK 465 ASN A 335
REMARK 465 SER D -1
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 148
REMARK 465 LYS D 149
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 SER A 276 OG
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 LYS A 293 CE NZ
REMARK 470 PHE A 314 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 7 CG CD OE1 OE2
REMARK 470 GLU D 55 CD OE1 OE2
REMARK 470 ARG D 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 76 CG CD CE NZ
REMARK 470 LYS D 95 CD CE NZ
REMARK 470 LYS D 116 CD CE NZ
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 D 2046 O HOH D 2047 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 2034 O HOH A 2047 4545 2.06
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 PHE A 17 -136.94 -121.60
REMARK 500 GLU A 106 -56.46 74.94
REMARK 500 ARG A 135 -3.91 70.57
REMARK 500 ASP A 157 61.94 62.47
REMARK 500 PHE A 233 78.33 -119.11
REMARK 500 LEU A 253 48.22 -92.70
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 A2016 DISTANCE = 5.89 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 (2-OXO-3-(4,5,6,7-TETRAHYDRO-1 H-INDOL-2-YLMETHYLENE)-2,
REMARK 600 3-DIHYDRO-1H-INDOLE-5-SULFONIC ACID DIMETHYLAMIDE) (K88):
REMARK 600 SU6656
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 CA D 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 21 OD1
REMARK 620 2 ASP D 23 OD2 80.1
REMARK 620 3 ASP D 25 OD1 82.5 80.5
REMARK 620 4 THR D 27 O 76.8 151.0 79.4
REMARK 620 5 GLU D 32 OE1 109.7 127.5 150.2 77.3
REMARK 620 6 GLU D 32 OE2 92.7 78.1 158.6 119.9 50.8
REMARK 620 7 HOH D2019 O 164.3 86.5 87.3 113.1 85.0 92.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 57 OD1
REMARK 620 2 ASP D 59 OD1 75.2
REMARK 620 3 ASN D 61 OD1 91.3 80.7
REMARK 620 4 THR D 63 O 86.8 153.6 80.6
REMARK 620 5 GLU D 68 OE1 95.7 120.3 159.0 80.0
REMARK 620 6 GLU D 68 OE2 77.3 71.8 152.1 123.3 48.9
REMARK 620 7 HOH D2053 O 161.5 90.5 98.0 110.4 81.2 87.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 94 OD1
REMARK 620 2 ASP D 96 OD1 80.8
REMARK 620 3 ASN D 98 OD1 83.6 73.9
REMARK 620 4 TYR D 100 O 83.2 152.6 82.4
REMARK 620 5 GLU D 105 OE2 94.3 75.3 149.1 128.2
REMARK 620 6 GLU D 105 OE1 100.8 126.8 159.3 78.1 51.4
REMARK 620 7 HOH D2104 O 159.7 107.2 81.0 81.7 105.7 89.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 130 OD1
REMARK 620 2 ASP D 132 OD1 79.0
REMARK 620 3 ASP D 134 OD1 86.5 82.2
REMARK 620 4 GLN D 136 O 85.6 154.0 76.0
REMARK 620 5 GLU D 141 OE2 89.5 75.7 157.9 125.3
REMARK 620 6 GLU D 141 OE1 106.1 125.6 150.7 78.7 50.7
REMARK 620 7 HOH D2102 O 164.4 93.5 78.9 96.0 102.0 89.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K88 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2F3Z RELATED DB: PDB
REMARK 900 CALMODULIN/IQ-AA DOMAIN COMPLEX
REMARK 900 RELATED ID: 1J7P RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CALCIUM CALMODULIN C- TERMINAL DOMAIN
REMARK 900 RELATED ID: 1NKF RELATED DB: PDB
REMARK 900 CALCIUM-BINDING PEPTIDE, NMR, 30 STRUCTURES
REMARK 900 RELATED ID: 2JL2 RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX
REMARK 900 RELATED ID: 1K93 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EDEMA FACTOR COMPLEXED WITH CALMODULIN
REMARK 900 RELATED ID: 1XFV RELATED DB: PDB
REMARK 900 FULL LENTH EF COMPLEXED CAM AND 3'-DEOXY- ATP
REMARK 900 RELATED ID: 1SK6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EF3/CALMODULIN COMPLEXED WITHCAMP/
REMARK 900 PYROPHOSPHATE
REMARK 900 RELATED ID: 1Y6W RELATED DB: PDB
REMARK 900 TRAPPED INTERMEDIATE OF CALMODULIN
REMARK 900 RELATED ID: 1IWQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MARCKS CALMODULIN BINDING DOMAINPEPTIDE
REMARK 900 COMPLEXED WITH CA2+/CALMODULIN
REMARK 900 RELATED ID: 1K90 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EDEMA FACTOR WITH CALMODULIN AND3'-DATP
REMARK 900 RELATED ID: 1YRT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE ADENYLYL CYCLAESCATALYTIC DOMAIN
REMARK 900 OF ADENYLYL CYCLASE TOXIN OF BORDETELLAPERTUSSIS IN PRESENCE OF C-
REMARK 900 TERMINAL CALMODULIN
REMARK 900 RELATED ID: 1LVC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EF-CAM COMPLEXED WITH 3'-ANT-2'-DATP
REMARK 900 RELATED ID: 2W73 RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION STRUCTURE OF THE COMPLEX BETWEEN CALMODULIN AND A
REMARK 900 PEPTIDE FROM CALCINEURIN A
REMARK 900 RELATED ID: 1CLL RELATED DB: PDB
REMARK 900 CALMODULIN (VERTEBRATE)
REMARK 900 RELATED ID: 1CDL RELATED DB: PDB
REMARK 900 CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTIDE FROM SMOOTH
REMARK 900 MUSCLE MYOSIN LIGHT CHAIN KINASE
REMARK 900 RELATED ID: 1XFY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULLEF-CAM WITH 1 UM CALCIUM
REMARK 900 RELATED ID: 1XFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULL-EF-DELTA64 COMPLEX WITH CAM
REMARK 900 RELATED ID: 2F3Y RELATED DB: PDB
REMARK 900 CALMODULIN/IQ DOMAIN COMPLEX
REMARK 900 RELATED ID: 1XFX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULL-EF-CAM COMPLEX AT 10 MM CALCIUM
REMARK 900 RELATED ID: 1S26 RELATED DB: PDB
REMARK 900 STRUCTURE OF ANTHRAX EDEMA FACTOR-CALMODULIN- ALPHA,BETA-
REMARK 900 METHYLENEADENOSINE 5'-TRIPHOSPHATE COMPLEX REVEALS ANALTERNATIVE
REMARK 900 MODE OF ATP BINDING TO THE CATALYTIC SITE
REMARK 900 RELATED ID: 1J7O RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CALCIUM-CALMODULIN N- TERMINAL DOMAIN
REMARK 900 RELATED ID: 2W2C RELATED DB: PDB
REMARK 900 STRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM-
REMARK 900 CALMODULIN DEPENDENT PROTEIN KINASE II DELTA
REMARK 900 RELATED ID: 2VN9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CALCIUM CALMODULIN DEPENDENT PROTEIN
REMARK 900 KINASE II DELTA ISOFORM 1, CAMKD
REMARK 900 RELATED ID: 1YRU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE ADENYLYL CYCLAESCATALYTIC DOMAIN
REMARK 900 OF ADENYLYL CYCLASE TOXIN OF BORDETELLAPERTUSSIS IN PRESENCE OF C-
REMARK 900 TERMINAL CALMODULIN AND 1MMCALCIUM CHLORIDE
REMARK 900 RELATED ID: 1WRZ RELATED DB: PDB
REMARK 900 CALMODULIN COMPLEXED WITH A PEPTIDE FROM A HUMAN DEATH-ASSOCIATED
REMARK 900 PROTEIN KINASE
REMARK 900 RELATED ID: 2V02 RELATED DB: PDB
REMARK 900 RECOMBINANT VERTEBRATE CALMODULIN COMPLEXED WITH BA
REMARK 900 RELATED ID: 1XFZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULLEF-CAM WITH 1 MM CALCIUM
REMARK 900 RELATED ID: 1XFW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULL-EF-CAM COMPLEXED WITH CAMP
REMARK 900 RELATED ID: 2V01 RELATED DB: PDB
REMARK 900 RECOMBINANT VERTEBRATE CALMODULIN COMPLEXED WITH PB
REMARK 900 RELATED ID: 1PK0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EF3-CAM COMPLEXED WITH PMEAPP
REMARK 900 RELATED ID: 2BE6 RELATED DB: PDB
REMARK 900 2.0 A CRYSTAL STRUCTURE OF THE CAV1.2 IQ DOMAIN-CA/CAMCOMPLEX
REMARK 900 RELATED ID: 1ZOT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE CYAA/C- CAM WITH PMEAPP
REMARK 900 RELATED ID: 2VAY RELATED DB: PDB
REMARK 900 CALMODULIN COMPLEXED WITH CAV1.1 IQ PEPTIDE
REMARK 900 RELATED ID: 1SW8 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN N60DCALMODULIN
REMARK 900 REFINED WITH PARAMAGNETISM BASED STRATEGY
REMARK 900 RELATED ID: 1AJI RELATED DB: PDB
REMARK 900 APO-CALMODULIN IN COMPLEX WITH BRUSH BORDER MYOSIN I IQ MOTIF,
REMARK 900 THEORETICAL MODEL
DBREF 2WEL A -1 0 PDB 2WEL 2WEL -1 0
DBREF 2WEL A 11 335 UNP Q13557 KCC2D_HUMAN 11 335
DBREF 2WEL D -1 -1 PDB 2WEL 2WEL -1 -1
DBREF 2WEL D 1 149 UNP P62158 CALM_HUMAN 1 149
SEQRES 1 A 327 SER MET THR ASP GLU TYR GLN LEU PHE GLU GLU LEU GLY
SEQRES 2 A 327 LYS GLY ALA PHE SER VAL VAL ARG ARG CYS MET LYS ILE
SEQRES 3 A 327 PRO THR GLY GLN GLU TYR ALA ALA LYS ILE ILE ASN THR
SEQRES 4 A 327 LYS LYS LEU SER ALA ARG ASP HIS GLN LYS LEU GLU ARG
SEQRES 5 A 327 GLU ALA ARG ILE CYS ARG LEU LEU LYS HIS PRO ASN ILE
SEQRES 6 A 327 VAL ARG LEU HIS ASP SER ILE SER GLU GLU GLY PHE HIS
SEQRES 7 A 327 TYR LEU VAL PHE ASP LEU VAL THR GLY GLY GLU LEU PHE
SEQRES 8 A 327 GLU ASP ILE VAL ALA ARG GLU TYR TYR SER GLU ALA ASP
SEQRES 9 A 327 ALA SER HIS CYS ILE GLN GLN ILE LEU GLU SER VAL ASN
SEQRES 10 A 327 HIS CYS HIS LEU ASN GLY ILE VAL HIS ARG ASP LEU LYS
SEQRES 11 A 327 PRO GLU ASN LEU LEU LEU ALA SER LYS SER LYS GLY ALA
SEQRES 12 A 327 ALA VAL LYS LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL
SEQRES 13 A 327 GLN GLY ASP GLN GLN ALA TRP PHE GLY PHE ALA GLY THR
SEQRES 14 A 327 PRO GLY TYR LEU SER PRO GLU VAL LEU ARG LYS ASP PRO
SEQRES 15 A 327 TYR GLY LYS PRO VAL ASP MET TRP ALA CYS GLY VAL ILE
SEQRES 16 A 327 LEU TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP
SEQRES 17 A 327 GLU ASP GLN HIS ARG LEU TYR GLN GLN ILE LYS ALA GLY
SEQRES 18 A 327 ALA TYR ASP PHE PRO SER PRO GLU TRP ASP THR VAL THR
SEQRES 19 A 327 PRO GLU ALA LYS ASP LEU ILE ASN LYS MET LEU THR ILE
SEQRES 20 A 327 ASN PRO ALA LYS ARG ILE THR ALA SER GLU ALA LEU LYS
SEQRES 21 A 327 HIS PRO TRP ILE CYS GLN ARG SER THR VAL ALA SER MET
SEQRES 22 A 327 MET HIS ARG GLN GLU THR VAL ASP CYS LEU LYS LYS PHE
SEQRES 23 A 327 ASN ALA ARG ARG LYS LEU LYS GLY ALA ILE LEU THR THR
SEQRES 24 A 327 MET LEU ALA THR ARG ASN PHE SER ALA ALA LYS SER LEU
SEQRES 25 A 327 LEU LYS LYS PRO ASP GLY VAL LYS GLU SER THR GLU SER
SEQRES 26 A 327 SER ASN
SEQRES 1 D 150 SER MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU
SEQRES 2 D 150 PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP
SEQRES 3 D 150 GLY THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG
SEQRES 4 D 150 SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP
SEQRES 5 D 150 MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE
SEQRES 6 D 150 ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET
SEQRES 7 D 150 LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE
SEQRES 8 D 150 ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA
SEQRES 9 D 150 ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS
SEQRES 10 D 150 LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA
SEQRES 11 D 150 ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE
SEQRES 12 D 150 VAL GLN MET MET THR ALA LYS
HET K88 A 600 26
HET EDO A 700 4
HET EDO A 701 4
HET EDO A 702 4
HET EDO A 703 4
HET EDO A 704 4
HET EDO A 705 4
HET PO4 A 706 5
HET PO4 A 707 5
HET CA D 600 1
HET CA D 601 1
HET CA D 602 1
HET CA D 603 1
HETNAM K88 (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-
HETNAM 2 K88 2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 K88 C19 H21 N3 O3 S
FORMUL 4 EDO 6(C2 H6 O2)
FORMUL 10 PO4 2(O4 P 3-)
FORMUL 12 CA 4(CA 2+)
FORMUL 16 HOH *405(H2 O)
HELIX 1 1 SER A -1 GLU A 13 1 5
HELIX 2 2 LYS A 48 LEU A 50 5 3
HELIX 3 3 SER A 51 LEU A 68 1 18
HELIX 4 4 GLU A 97 GLU A 106 1 10
HELIX 5 5 SER A 109 ASN A 130 1 22
HELIX 6 6 LYS A 138 GLU A 140 5 3
HELIX 7 7 ASP A 157 ALA A 161 5 5
HELIX 8 8 THR A 177 LEU A 181 5 5
HELIX 9 9 SER A 182 ARG A 187 1 6
HELIX 10 10 LYS A 193 GLY A 210 1 18
HELIX 11 11 ASP A 218 GLY A 229 1 12
HELIX 12 12 THR A 242 LEU A 253 1 12
HELIX 13 13 THR A 262 LEU A 267 1 6
HELIX 14 14 HIS A 269 GLN A 274 1 6
HELIX 15 15 ASN A 295 ALA A 316 1 22
HELIX 16 16 THR D 6 ASP D 21 1 16
HELIX 17 17 THR D 29 LEU D 40 1 12
HELIX 18 18 THR D 45 ASP D 57 1 13
HELIX 19 19 ASP D 65 ALA D 74 1 10
HELIX 20 20 LYS D 78 ASP D 94 1 17
HELIX 21 21 SER D 102 LEU D 113 1 12
HELIX 22 22 THR D 118 ASP D 130 1 13
HELIX 23 23 TYR D 139 MET D 146 1 8
SHEET 1 AA 5 TYR A 14 GLY A 23 0
SHEET 2 AA 5 SER A 26 LYS A 33 -1 O SER A 26 N GLY A 23
SHEET 3 AA 5 GLU A 39 ASN A 46 -1 O TYR A 40 N CYS A 31
SHEET 4 AA 5 PHE A 85 PHE A 90 -1 O HIS A 86 N ILE A 45
SHEET 5 AA 5 LEU A 76 GLU A 82 -1 N HIS A 77 O VAL A 89
SHEET 1 AB 2 ILE A 132 VAL A 133 0
SHEET 2 AB 2 ILE A 162 GLU A 163 -1 O ILE A 162 N VAL A 133
SHEET 1 AC 2 LEU A 142 LEU A 144 0
SHEET 2 AC 2 VAL A 153 LEU A 155 -1 O LYS A 154 N LEU A 143
SHEET 1 DA 2 TYR D 100 ILE D 101 0
SHEET 2 DA 2 VAL D 137 ASN D 138 -1 O VAL D 137 N ILE D 101
LINK OD1 ASP D 21 CA CA D 600 1555 1555 2.18
LINK OD2 ASP D 23 CA CA D 600 1555 1555 2.31
LINK OD1 ASP D 25 CA CA D 600 1555 1555 2.49
LINK O THR D 27 CA CA D 600 1555 1555 2.35
LINK OE1 GLU D 32 CA CA D 600 1555 1555 2.60
LINK OE2 GLU D 32 CA CA D 600 1555 1555 2.61
LINK OD1 ASP D 57 CA CA D 601 1555 1555 2.15
LINK OD1 ASP D 59 CA CA D 601 1555 1555 2.51
LINK OD1 ASN D 61 CA CA D 601 1555 1555 2.36
LINK O THR D 63 CA CA D 601 1555 1555 2.45
LINK OE1 GLU D 68 CA CA D 601 1555 1555 2.47
LINK OE2 GLU D 68 CA CA D 601 1555 1555 2.75
LINK OD1 ASP D 94 CA CA D 602 1555 1555 2.28
LINK OD1 ASP D 96 CA CA D 602 1555 1555 2.36
LINK OD1 ASN D 98 CA CA D 602 1555 1555 2.44
LINK O TYR D 100 CA CA D 602 1555 1555 2.25
LINK OE2 GLU D 105 CA CA D 602 1555 1555 2.47
LINK OE1 GLU D 105 CA CA D 602 1555 1555 2.48
LINK OD1 ASP D 130 CA CA D 603 1555 1555 2.25
LINK OD1 ASP D 132 CA CA D 603 1555 1555 2.40
LINK OD1 ASP D 134 CA CA D 603 1555 1555 2.44
LINK O GLN D 136 CA CA D 603 1555 1555 2.37
LINK OE2 GLU D 141 CA CA D 603 1555 1555 2.44
LINK OE1 GLU D 141 CA CA D 603 1555 1555 2.54
LINK CA CA D 600 O HOH D2019 1555 1555 2.37
LINK CA CA D 601 O HOH D2053 1555 1555 2.05
LINK CA CA D 602 O HOH D2104 1555 1555 2.51
LINK CA CA D 603 O HOH D2102 1555 1555 2.40
CISPEP 1 SER A 235 PRO A 236 0 -1.22
SITE 1 AC1 11 LEU A 20 VAL A 28 ALA A 41 LYS A 43
SITE 2 AC1 11 PHE A 90 ASP A 91 LEU A 92 VAL A 93
SITE 3 AC1 11 ASP A 157 EDO A 700 EDO A 701
SITE 1 AC2 3 K88 A 600 HOH A2289 HOH A2290
SITE 1 AC3 7 GLU A 61 VAL A 74 PHE A 90 ALA A 156
SITE 2 AC3 7 ASP A 157 PHE A 158 K88 A 600
SITE 1 AC4 5 GLU A 140 TYR A 180 HIS A 283 GLN A 285
SITE 2 AC4 5 HOH A2292
SITE 1 AC5 4 HIS A 55 SER A 81 LYS A 147 PO4 A 706
SITE 1 AC6 7 TYR A 14 LYS A 33 HIS A 77 PO4 A 707
SITE 2 AC6 7 HOH A2089 HOH A2293 HOH D2092
SITE 1 AC7 5 TYR A 205 PRO A 213 TYR A 231 ASP A 232
SITE 2 AC7 5 HOH A2294
SITE 1 AC8 10 THR A 47 HIS A 55 SER A 81 GLU A 82
SITE 2 AC8 10 PHE A 85 HIS A 86 SER A 148 LYS A 149
SITE 3 AC8 10 EDO A 703 HOH A2295
SITE 1 AC9 6 LYS A 69 ARG A 75 HIS A 77 EDO A 704
SITE 2 AC9 6 HOH A2089 HOH A2297
SITE 1 BC1 6 ASP D 21 ASP D 23 ASP D 25 THR D 27
SITE 2 BC1 6 GLU D 32 HOH D2019
SITE 1 BC2 6 ASP D 57 ASP D 59 ASN D 61 THR D 63
SITE 2 BC2 6 GLU D 68 HOH D2053
SITE 1 BC3 6 ASP D 94 ASP D 96 ASN D 98 TYR D 100
SITE 2 BC3 6 GLU D 105 HOH D2104
SITE 1 BC4 6 ASP D 130 ASP D 132 ASP D 134 GLN D 136
SITE 2 BC4 6 GLU D 141 HOH D2102
CRYST1 68.260 68.850 121.980 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 0.014650 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014524 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
