HEADER PROTEIN BINDING 16-AUG-18 6HCS
TITLE CRYSTAL STRUCTURE OF CAM-PEPTIDE COMPLEX CONTAINING AZF AT POSITION
TITLE 2 108
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-1;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT
COMPND 7 BETA;
COMPND 8 CHAIN: B, D, F, H;
COMPND 9 SYNONYM: CAMK-II SUBUNIT BETA;
COMPND 10 EC: 2.7.11.17;
COMPND 11 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: CALM1, CALM, CAM, CAM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 11 ORGANISM_COMMON: RAT;
SOURCE 12 ORGANISM_TAXID: 10116
KEYWDS CALMODULIN, UNNATURAL AMINO ACID, AZF, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CREON,I.JOSTS,H.TIDOW
REVDAT 3 17-JAN-24 6HCS 1 LINK
REVDAT 2 19-DEC-18 6HCS 1 REMARK
REVDAT 1 05-DEC-18 6HCS 0
JRNL AUTH A.CREON,I.JOSTS,S.NIEBLING,N.HUSE,H.TIDOW
JRNL TITL CONFORMATION-SPECIFIC DETECTION OF CALMODULIN BINDING USING
JRNL TITL 2 THE UNNATURAL AMINO ACID P-AZIDO-PHENYLALANINE (AZF) AS AN
JRNL TITL 3 IR-SENSOR.
JRNL REF STRUCT DYN V. 5 64701 2018
JRNL REFN ESSN 2329-7778
JRNL PMID 30474048
JRNL DOI 10.1063/1.5053466
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 45027
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.260
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2256
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 43.1289 - 5.0372 0.95 2771 129 0.2497 0.2849
REMARK 3 2 5.0372 - 3.9991 0.96 2672 160 0.2354 0.2639
REMARK 3 3 3.9991 - 3.4938 0.95 2640 125 0.2447 0.2503
REMARK 3 4 3.4938 - 3.1745 0.95 2599 148 0.2540 0.3092
REMARK 3 5 3.1745 - 2.9470 0.98 2673 147 0.2708 0.3273
REMARK 3 6 2.9470 - 2.7733 0.99 2716 141 0.2792 0.3126
REMARK 3 7 2.7733 - 2.6344 0.99 2667 134 0.2615 0.3043
REMARK 3 8 2.6344 - 2.5198 0.97 2645 147 0.2607 0.2850
REMARK 3 9 2.5198 - 2.4228 0.97 2647 148 0.2665 0.3040
REMARK 3 10 2.4228 - 2.3392 0.98 2667 134 0.2702 0.3352
REMARK 3 11 2.3392 - 2.2660 0.98 2670 143 0.2690 0.3159
REMARK 3 12 2.2660 - 2.2013 0.98 2638 148 0.2751 0.3105
REMARK 3 13 2.2013 - 2.1433 0.99 2725 121 0.2793 0.2895
REMARK 3 14 2.1433 - 2.0910 0.99 2654 138 0.2966 0.3066
REMARK 3 15 2.0910 - 2.0435 0.99 2707 140 0.3047 0.3428
REMARK 3 16 2.0435 - 2.0000 0.99 2680 153 0.3173 0.3488
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.590
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 : 0.007 5031
REMARK 3 ANGLE : 0.859 6711
REMARK 3 CHIRALITY : 0.046 744
REMARK 3 PLANARITY : 0.004 893
REMARK 3 DIHEDRAL : 35.148 1892
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6HCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200011316.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.917143
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45156
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
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 : 13.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
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: PHASER
REMARK 200 STARTING MODEL: 1CDM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, LITHIUM CHLORIDE, SODIUM
REMARK 280 CHLORIDE, PH 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 18.60700
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, 3, 4
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: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350
REMARK 350 BIOMOLECULE: 3
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: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
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: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 MET A 0
REMARK 465 ALA A 1
REMARK 465 MET A 76
REMARK 465 LYS A 77
REMARK 465 ASP A 78
REMARK 465 THR A 79
REMARK 465 ASP A 80
REMARK 465 SER A 81
REMARK 465 GLU A 82
REMARK 465 GLU A 83
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 LEU A 149
REMARK 465 GLU A 150
REMARK 465 GLY A 151
REMARK 465 THR A 152
REMARK 465 GLY A 153
REMARK 465 LEU A 154
REMARK 465 GLU A 155
REMARK 465 VAL A 156
REMARK 465 LEU A 157
REMARK 465 PHE A 158
REMARK 465 GLN A 159
REMARK 465 GLY A 160
REMARK 465 HIS A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 465 HIS A 166
REMARK 465 LEU B 290
REMARK 465 LYS B 291
REMARK 465 LYS B 292
REMARK 465 ASN B 312
REMARK 465 PHE B 313
REMARK 465 SER B 314
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 LYS C 77
REMARK 465 ASP C 78
REMARK 465 THR C 79
REMARK 465 ASP C 80
REMARK 465 SER C 81
REMARK 465 GLU C 82
REMARK 465 ALA C 147
REMARK 465 LYS C 148
REMARK 465 LEU C 149
REMARK 465 GLU C 150
REMARK 465 GLY C 151
REMARK 465 THR C 152
REMARK 465 GLY C 153
REMARK 465 LEU C 154
REMARK 465 GLU C 155
REMARK 465 VAL C 156
REMARK 465 LEU C 157
REMARK 465 PHE C 158
REMARK 465 GLN C 159
REMARK 465 GLY C 160
REMARK 465 HIS C 161
REMARK 465 HIS C 162
REMARK 465 HIS C 163
REMARK 465 HIS C 164
REMARK 465 HIS C 165
REMARK 465 HIS C 166
REMARK 465 LEU D 290
REMARK 465 LYS D 291
REMARK 465 LYS D 292
REMARK 465 SER D 314
REMARK 465 MET E 0
REMARK 465 ALA E 1
REMARK 465 LYS E 77
REMARK 465 ASP E 78
REMARK 465 THR E 79
REMARK 465 ASP E 80
REMARK 465 SER E 81
REMARK 465 GLU E 82
REMARK 465 GLU E 83
REMARK 465 ALA E 147
REMARK 465 LYS E 148
REMARK 465 LEU E 149
REMARK 465 GLU E 150
REMARK 465 GLY E 151
REMARK 465 THR E 152
REMARK 465 GLY E 153
REMARK 465 LEU E 154
REMARK 465 GLU E 155
REMARK 465 VAL E 156
REMARK 465 LEU E 157
REMARK 465 PHE E 158
REMARK 465 GLN E 159
REMARK 465 GLY E 160
REMARK 465 HIS E 161
REMARK 465 HIS E 162
REMARK 465 HIS E 163
REMARK 465 HIS E 164
REMARK 465 HIS E 165
REMARK 465 HIS E 166
REMARK 465 LEU F 290
REMARK 465 LYS F 291
REMARK 465 LYS F 292
REMARK 465 ARG F 311
REMARK 465 ASN F 312
REMARK 465 PHE F 313
REMARK 465 SER F 314
REMARK 465 MET G 0
REMARK 465 ALA G 1
REMARK 465 LYS G 77
REMARK 465 ASP G 78
REMARK 465 THR G 79
REMARK 465 ASP G 80
REMARK 465 SER G 81
REMARK 465 GLU G 82
REMARK 465 GLU G 83
REMARK 465 ALA G 147
REMARK 465 LYS G 148
REMARK 465 LEU G 149
REMARK 465 GLU G 150
REMARK 465 GLY G 151
REMARK 465 THR G 152
REMARK 465 GLY G 153
REMARK 465 LEU G 154
REMARK 465 GLU G 155
REMARK 465 VAL G 156
REMARK 465 LEU G 157
REMARK 465 PHE G 158
REMARK 465 GLN G 159
REMARK 465 GLY G 160
REMARK 465 HIS G 161
REMARK 465 HIS G 162
REMARK 465 HIS G 163
REMARK 465 HIS G 164
REMARK 465 HIS G 165
REMARK 465 HIS G 166
REMARK 465 LEU H 290
REMARK 465 LYS H 291
REMARK 465 LYS H 292
REMARK 465 ARG H 311
REMARK 465 ASN H 312
REMARK 465 PHE H 313
REMARK 465 SER H 314
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 MET E 76 CG SD CE
REMARK 470 MET G 76 CG SD CE
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 N2 4II G 108 OG1 THR H 306 1.64
REMARK 500 O THR C 146 O HOH C 301 2.13
REMARK 500 N2 4II G 108 O ALA H 302 2.14
REMARK 500 N PHE F 293 O HOH F 401 2.16
REMARK 500 O HOH C 356 O HOH D 406 2.17
REMARK 500 O THR E 146 O HOH E 301 2.18
REMARK 500 O HOH A 345 O HOH A 379 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 107 O - C - N ANGL. DEV. = -12.6 DEGREES
REMARK 500 4II A 108 O - C - N ANGL. DEV. = -12.8 DEGREES
REMARK 500 HIS C 107 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 4II C 108 O - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 MET E 109 C - N - CA ANGL. DEV. = 20.1 DEGREES
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 ARG D 311 54.44 -144.34
REMARK 500 ASN D 312 -128.84 65.42
REMARK 500 ASP E 20 73.61 -66.53
REMARK 500 ASN E 42 79.33 -118.36
REMARK 500 THR E 62 -166.30 -127.75
REMARK 500 GLN G 3 -167.94 -173.39
REMARK 500 ASP G 56 88.06 -68.01
REMARK 500 ASP G 93 85.10 -67.42
REMARK 500 ASN G 97 2.49 -68.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 HIS A 107 16.49
REMARK 500 HIS C 107 11.13
REMARK 500 HIS E 107 -10.17
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 398 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A 399 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH A 400 DISTANCE = 8.21 ANGSTROMS
REMARK 525 HOH C 393 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH C 394 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH E 317 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH E 318 DISTANCE = 7.73 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 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 74.7
REMARK 620 3 ASP A 24 OD1 84.4 73.0
REMARK 620 4 THR A 26 O 87.5 151.1 83.0
REMARK 620 5 GLU A 31 OE1 110.0 128.5 156.0 78.7
REMARK 620 6 GLU A 31 OE2 96.7 77.0 148.5 128.5 51.6
REMARK 620 7 HOH A 342 O 158.1 86.3 79.6 105.2 90.2 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 A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 76.8
REMARK 620 3 ASN A 60 OD1 89.2 78.8
REMARK 620 4 THR A 62 O 79.5 150.5 83.5
REMARK 620 5 GLU A 67 OE1 103.3 121.1 158.2 81.4
REMARK 620 6 GLU A 67 OE2 83.3 73.2 152.0 121.2 49.0
REMARK 620 7 HOH A 312 O 151.6 78.1 98.9 128.3 78.6 76.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 84.7
REMARK 620 3 ASN A 97 OD1 84.0 76.8
REMARK 620 4 TYR A 99 O 88.6 155.6 79.1
REMARK 620 5 GLU A 104 OE1 99.5 76.1 152.2 128.3
REMARK 620 6 GLU A 104 OE2 105.0 127.8 153.8 76.7 51.8
REMARK 620 7 HOH A 313 O 170.3 86.1 90.7 98.4 81.4 83.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 79.8
REMARK 620 3 ASP A 133 OD1 86.4 76.3
REMARK 620 4 GLN A 135 O 84.7 152.2 79.9
REMARK 620 5 GLU A 140 OE1 89.5 76.7 153.0 126.3
REMARK 620 6 GLU A 140 OE2 112.4 127.8 150.5 79.5 54.0
REMARK 620 7 HOH A 311 O 161.6 86.5 78.5 102.7 99.2 85.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 20 OD1
REMARK 620 2 ASP C 22 OD1 75.4
REMARK 620 3 ASP C 24 OD1 87.6 71.9
REMARK 620 4 THR C 26 O 84.1 148.1 83.2
REMARK 620 5 GLU C 31 OE1 109.5 133.7 151.2 76.0
REMARK 620 6 GLU C 31 OE2 95.0 81.6 151.8 124.9 52.4
REMARK 620 7 HOH C 320 O 159.8 85.2 80.9 110.8 88.0 87.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 56 OD1
REMARK 620 2 ASP C 58 OD1 77.0
REMARK 620 3 ASN C 60 OD1 91.4 80.9
REMARK 620 4 THR C 62 O 83.0 155.0 84.7
REMARK 620 5 GLU C 67 OE1 100.1 116.8 160.5 81.2
REMARK 620 6 GLU C 67 OE2 81.6 69.4 150.3 122.5 48.3
REMARK 620 7 HOH C 307 O 149.6 75.3 96.3 126.8 81.7 77.3
REMARK 620 8 HOH C 347 O 146.5 131.2 78.3 64.4 83.5 122.0 63.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 93 OD1
REMARK 620 2 ASP C 95 OD1 82.4
REMARK 620 3 ASN C 97 OD1 86.4 76.7
REMARK 620 4 TYR C 99 O 90.0 156.2 80.4
REMARK 620 5 GLU C 104 OE1 95.2 76.2 152.4 127.1
REMARK 620 6 GLU C 104 OE2 102.9 127.6 154.6 76.1 51.4
REMARK 620 7 HOH C 312 O 167.5 85.3 92.9 102.2 79.7 82.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 129 OD1
REMARK 620 2 ASP C 131 OD1 79.6
REMARK 620 3 ASP C 133 OD1 85.7 76.2
REMARK 620 4 GLN C 135 O 85.2 151.4 78.6
REMARK 620 5 GLU C 140 OE1 91.1 79.8 156.0 124.8
REMARK 620 6 GLU C 140 OE2 114.9 129.1 148.2 79.3 52.9
REMARK 620 7 HOH C 306 O 159.2 85.1 77.1 102.4 100.0 85.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 20 OD1
REMARK 620 2 ASP E 22 OD1 67.4
REMARK 620 3 ASP E 24 OD1 69.5 70.0
REMARK 620 4 THR E 26 O 71.2 136.0 82.3
REMARK 620 5 GLU E 31 OE1 110.9 126.3 163.2 82.1
REMARK 620 6 GLU E 31 OE2 93.6 69.6 139.6 128.0 56.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 56 OD2
REMARK 620 2 ASN E 60 OD1 71.0
REMARK 620 3 THR E 62 O 82.1 62.7
REMARK 620 4 GLU E 67 OE1 107.5 149.2 86.5
REMARK 620 5 GLU E 67 OE2 74.8 145.4 118.1 49.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 93 OD2
REMARK 620 2 ASP E 95 OD1 76.2
REMARK 620 3 ASN E 97 OD1 87.5 70.5
REMARK 620 4 TYR E 99 O 99.8 149.2 78.9
REMARK 620 5 GLU E 104 OE1 90.5 82.9 153.1 127.8
REMARK 620 6 GLU E 104 OE2 112.7 134.3 149.9 75.9 53.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 129 OD1
REMARK 620 2 ASP E 131 OD1 77.9
REMARK 620 3 ASP E 133 OD1 93.2 86.4
REMARK 620 4 GLN E 135 O 77.5 145.8 71.7
REMARK 620 5 GLU E 140 OE1 90.1 76.0 161.0 127.2
REMARK 620 6 GLU E 140 OE2 105.3 123.1 147.5 86.2 47.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 20 OD1
REMARK 620 2 ASP G 22 OD2 128.2
REMARK 620 3 THR G 26 O 74.7 154.4
REMARK 620 4 GLU G 31 OE1 116.1 95.8 80.7
REMARK 620 5 GLU G 31 OE2 98.2 71.0 121.9 50.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 56 OD1
REMARK 620 2 ASP G 58 OD1 65.4
REMARK 620 3 ASN G 60 OD1 85.0 71.8
REMARK 620 4 THR G 62 O 84.8 143.3 85.2
REMARK 620 5 GLU G 67 OE1 103.6 122.9 164.9 83.2
REMARK 620 6 GLU G 67 OE2 75.8 69.4 141.0 125.4 54.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 93 OD2
REMARK 620 2 ASP G 95 OD1 123.2
REMARK 620 3 ASN G 97 OD1 88.7 92.9
REMARK 620 4 TYR G 99 O 99.2 137.5 88.3
REMARK 620 5 GLU G 104 OE1 94.5 61.9 151.7 118.8
REMARK 620 6 GLU G 104 OE2 108.3 94.4 153.3 69.2 49.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 129 OD1
REMARK 620 2 ASP G 131 OD1 77.4
REMARK 620 3 ASP G 133 OD2 84.0 79.7
REMARK 620 4 GLN G 135 O 88.9 146.1 68.0
REMARK 620 5 GLU G 140 OE1 92.8 80.7 160.4 131.4
REMARK 620 6 GLU G 140 OE2 99.8 133.3 146.9 79.2 52.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 204
DBREF 6HCS A 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6HCS B 290 314 UNP P08413 KCC2B_RAT 291 315
DBREF 6HCS C 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6HCS D 290 314 UNP P08413 KCC2B_RAT 291 315
DBREF 6HCS E 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6HCS F 290 314 UNP P08413 KCC2B_RAT 291 315
DBREF 6HCS G 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6HCS H 290 314 UNP P08413 KCC2B_RAT 291 315
SEQADV 6HCS 4II A 108 UNP P0DP23 VAL 109 ENGINEERED MUTATION
SEQADV 6HCS LEU A 149 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU A 150 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY A 151 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS THR A 152 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY A 153 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU A 154 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU A 155 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS VAL A 156 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU A 157 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS PHE A 158 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLN A 159 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY A 160 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS A 161 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS A 162 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS A 163 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS A 164 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS A 165 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS A 166 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS 4II C 108 UNP P0DP23 VAL 109 ENGINEERED MUTATION
SEQADV 6HCS LEU C 149 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU C 150 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY C 151 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS THR C 152 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY C 153 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU C 154 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU C 155 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS VAL C 156 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU C 157 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS PHE C 158 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLN C 159 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY C 160 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS C 161 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS C 162 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS C 163 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS C 164 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS C 165 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS C 166 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS 4II E 108 UNP P0DP23 VAL 109 ENGINEERED MUTATION
SEQADV 6HCS LEU E 149 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU E 150 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY E 151 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS THR E 152 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY E 153 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU E 154 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU E 155 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS VAL E 156 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU E 157 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS PHE E 158 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLN E 159 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY E 160 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS E 161 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS E 162 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS E 163 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS E 164 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS E 165 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS E 166 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS 4II G 108 UNP P0DP23 VAL 109 ENGINEERED MUTATION
SEQADV 6HCS LEU G 149 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU G 150 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY G 151 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS THR G 152 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY G 153 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU G 154 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLU G 155 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS VAL G 156 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS LEU G 157 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS PHE G 158 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLN G 159 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS GLY G 160 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS G 161 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS G 162 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS G 163 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS G 164 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS G 165 UNP P0DP23 EXPRESSION TAG
SEQADV 6HCS HIS G 166 UNP P0DP23 EXPRESSION TAG
SEQRES 1 A 167 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 167 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 167 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 167 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 167 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 167 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 A 167 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 167 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 167 GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 167 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 A 167 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 167 GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU
SEQRES 13 A 167 VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 25 LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA
SEQRES 2 B 25 ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER
SEQRES 1 C 167 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 C 167 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 C 167 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 C 167 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 C 167 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 C 167 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 C 167 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 C 167 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 C 167 GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 C 167 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 C 167 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 C 167 GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU
SEQRES 13 C 167 VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 25 LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA
SEQRES 2 D 25 ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER
SEQRES 1 E 167 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 E 167 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 E 167 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 E 167 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 E 167 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 E 167 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 E 167 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 E 167 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 E 167 GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 E 167 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 E 167 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 E 167 GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU
SEQRES 13 E 167 VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 F 25 LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA
SEQRES 2 F 25 ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER
SEQRES 1 G 167 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 G 167 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 G 167 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 G 167 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 G 167 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 G 167 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 G 167 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 G 167 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 G 167 GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 G 167 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 G 167 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 G 167 GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU
SEQRES 13 G 167 VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 H 25 LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA
SEQRES 2 H 25 ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER
MODRES 6HCS 4II A 108 VAL MODIFIED RESIDUE
MODRES 6HCS 4II C 108 VAL MODIFIED RESIDUE
MODRES 6HCS 4II E 108 VAL MODIFIED RESIDUE
MODRES 6HCS 4II G 108 VAL MODIFIED RESIDUE
HET 4II A 108 14
HET 4II C 108 14
HET 4II E 108 14
HET 4II G 108 14
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA A 204 1
HET CA C 201 1
HET CA C 202 1
HET CA C 203 1
HET CA C 204 1
HET CA E 201 1
HET CA E 202 1
HET CA E 203 1
HET CA E 204 1
HET CA G 201 1
HET CA G 202 1
HET CA G 203 1
HET CA G 204 1
HETNAM 4II (2~{S})-2-AZANYL-3-(4-AZIDOPHENYL)PROPANOIC ACID
HETNAM CA CALCIUM ION
FORMUL 1 4II 4(C9 H10 N4 O2)
FORMUL 9 CA 16(CA 2+)
FORMUL 25 HOH *243(H2 O)
HELIX 1 AA1 THR A 5 ASP A 20 1 16
HELIX 2 AA2 THR A 28 LEU A 39 1 12
HELIX 3 AA3 THR A 44 ASP A 56 1 13
HELIX 4 AA4 ASP A 64 LYS A 75 1 12
HELIX 5 AA5 ILE A 85 ASP A 93 1 9
HELIX 6 AA6 SER A 101 LEU A 112 1 12
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 TYR A 138 THR A 146 1 9
HELIX 9 AA9 ASN B 294 THR B 310 1 17
HELIX 10 AB1 THR C 5 ASP C 20 1 16
HELIX 11 AB2 THR C 28 LEU C 39 1 12
HELIX 12 AB3 THR C 44 ASP C 56 1 13
HELIX 13 AB4 ASP C 64 ARG C 74 1 11
HELIX 14 AB5 GLU C 84 ASP C 93 1 10
HELIX 15 AB6 SER C 101 LEU C 112 1 12
HELIX 16 AB7 THR C 117 ASP C 129 1 13
HELIX 17 AB8 TYR C 138 THR C 146 1 9
HELIX 18 AB9 ASN D 294 THR D 310 1 17
HELIX 19 AC1 THR E 5 ASP E 20 1 16
HELIX 20 AC2 THR E 28 SER E 38 1 11
HELIX 21 AC3 THR E 44 GLU E 54 1 11
HELIX 22 AC4 PHE E 65 LYS E 75 1 11
HELIX 23 AC5 ILE E 85 ASP E 93 1 9
HELIX 24 AC6 SER E 101 ASN E 111 1 11
HELIX 25 AC7 THR E 117 ASP E 129 1 13
HELIX 26 AC8 TYR E 138 MET E 145 1 8
HELIX 27 AC9 ASN F 294 THR F 310 1 17
HELIX 28 AD1 THR G 5 ASP G 20 1 16
HELIX 29 AD2 THR G 28 LEU G 39 1 12
HELIX 30 AD3 THR G 44 ASP G 56 1 13
HELIX 31 AD4 PHE G 65 LYS G 75 1 11
HELIX 32 AD5 ILE G 85 ASP G 93 1 9
HELIX 33 AD6 SER G 101 ASN G 111 1 11
HELIX 34 AD7 THR G 117 ASP G 129 1 13
HELIX 35 AD8 ASN G 137 MET G 145 1 9
HELIX 36 AD9 ASN H 294 THR H 310 1 17
SHEET 1 AA1 2 TYR A 99 ILE A 100 0
SHEET 2 AA1 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
SHEET 1 AA2 2 TYR C 99 ILE C 100 0
SHEET 2 AA2 2 VAL C 136 ASN C 137 -1 O VAL C 136 N ILE C 100
SHEET 1 AA3 2 THR E 26 ILE E 27 0
SHEET 2 AA3 2 ILE E 63 ASP E 64 -1 O ILE E 63 N ILE E 27
SHEET 1 AA4 2 TYR E 99 ILE E 100 0
SHEET 2 AA4 2 VAL E 136 ASN E 137 -1 O VAL E 136 N ILE E 100
SHEET 1 AA5 2 THR G 26 ILE G 27 0
SHEET 2 AA5 2 ILE G 63 ASP G 64 -1 O ILE G 63 N ILE G 27
LINK C HIS A 107 N 4II A 108 1555 1555 1.43
LINK C 4II A 108 N MET A 109 1555 1555 1.43
LINK C HIS C 107 N 4II C 108 1555 1555 1.42
LINK C 4II C 108 N MET C 109 1555 1555 1.43
LINK C HIS E 107 N 4II E 108 1555 1555 1.43
LINK C 4II E 108 N MET E 109 1555 1555 1.43
LINK C HIS G 107 N 4II G 108 1555 1555 1.43
LINK C 4II G 108 N MET G 109 1555 1555 1.43
LINK N3 4II G 108 O ALA H 302 1555 1555 1.30
LINK N1 4II G 108 OG1 THR H 306 1555 1555 1.30
LINK OD1 ASP A 20 CA CA A 201 1555 1555 2.38
LINK OD1 ASP A 22 CA CA A 201 1555 1555 2.48
LINK OD1 ASP A 24 CA CA A 201 1555 1555 2.41
LINK O THR A 26 CA CA A 201 1555 1555 2.21
LINK OE1 GLU A 31 CA CA A 201 1555 1555 2.54
LINK OE2 GLU A 31 CA CA A 201 1555 1555 2.44
LINK OD1 ASP A 56 CA CA A 202 1555 1555 2.28
LINK OD1 ASP A 58 CA CA A 202 1555 1555 2.44
LINK OD1 ASN A 60 CA CA A 202 1555 1555 2.44
LINK O THR A 62 CA CA A 202 1555 1555 2.45
LINK OE1 GLU A 67 CA CA A 202 1555 1555 2.64
LINK OE2 GLU A 67 CA CA A 202 1555 1555 2.65
LINK OD1 ASP A 93 CA CA A 203 1555 1555 2.26
LINK OD1 ASP A 95 CA CA A 203 1555 1555 2.34
LINK OD1 ASN A 97 CA CA A 203 1555 1555 2.51
LINK O TYR A 99 CA CA A 203 1555 1555 2.31
LINK OE1 GLU A 104 CA CA A 203 1555 1555 2.57
LINK OE2 GLU A 104 CA CA A 203 1555 1555 2.54
LINK OD1 ASP A 129 CA CA A 204 1555 1555 2.36
LINK OD1 ASP A 131 CA CA A 204 1555 1555 2.44
LINK OD1 ASP A 133 CA CA A 204 1555 1555 2.50
LINK O GLN A 135 CA CA A 204 1555 1555 2.42
LINK OE1 GLU A 140 CA CA A 204 1555 1555 2.53
LINK OE2 GLU A 140 CA CA A 204 1555 1555 2.39
LINK CA CA A 201 O HOH A 342 1555 1555 2.57
LINK CA CA A 202 O HOH A 312 1555 1555 2.46
LINK CA CA A 203 O HOH A 313 1555 1555 2.46
LINK CA CA A 204 O HOH A 311 1555 1555 2.41
LINK OD1 ASP C 20 CA CA C 201 1555 1555 2.35
LINK OD1 ASP C 22 CA CA C 201 1555 1555 2.43
LINK OD1 ASP C 24 CA CA C 201 1555 1555 2.48
LINK O THR C 26 CA CA C 201 1555 1555 2.35
LINK OE1 GLU C 31 CA CA C 201 1555 1555 2.51
LINK OE2 GLU C 31 CA CA C 201 1555 1555 2.47
LINK OD1 ASP C 56 CA CA C 202 1555 1555 2.35
LINK OD1 ASP C 58 CA CA C 202 1555 1555 2.40
LINK OD1 ASN C 60 CA CA C 202 1555 1555 2.41
LINK O THR C 62 CA CA C 202 1555 1555 2.40
LINK OE1 GLU C 67 CA CA C 202 1555 1555 2.62
LINK OE2 GLU C 67 CA CA C 202 1555 1555 2.75
LINK OD1 ASP C 93 CA CA C 203 1555 1555 2.24
LINK OD1 ASP C 95 CA CA C 203 1555 1555 2.37
LINK OD1 ASN C 97 CA CA C 203 1555 1555 2.52
LINK O TYR C 99 CA CA C 203 1555 1555 2.29
LINK OE1 GLU C 104 CA CA C 203 1555 1555 2.51
LINK OE2 GLU C 104 CA CA C 203 1555 1555 2.58
LINK OD1 ASP C 129 CA CA C 204 1555 1555 2.40
LINK OD1 ASP C 131 CA CA C 204 1555 1555 2.44
LINK OD1 ASP C 133 CA CA C 204 1555 1555 2.36
LINK O GLN C 135 CA CA C 204 1555 1555 2.45
LINK OE1 GLU C 140 CA CA C 204 1555 1555 2.42
LINK OE2 GLU C 140 CA CA C 204 1555 1555 2.48
LINK CA CA C 201 O HOH C 320 1555 1555 2.59
LINK CA CA C 202 O HOH C 307 1555 1555 2.52
LINK CA CA C 202 O HOH C 347 1555 1555 2.91
LINK CA CA C 203 O HOH C 312 1555 1555 2.39
LINK CA CA C 204 O HOH C 306 1555 1555 2.48
LINK OD1 ASP E 20 CA CA E 204 1555 1555 2.61
LINK OD1 ASP E 22 CA CA E 204 1555 1555 2.49
LINK OD1 ASP E 24 CA CA E 204 1555 1555 2.71
LINK O THR E 26 CA CA E 204 1555 1555 2.44
LINK OE1 GLU E 31 CA CA E 204 1555 1555 2.29
LINK OE2 GLU E 31 CA CA E 204 1555 1555 2.37
LINK OD2 ASP E 56 CA CA E 203 1555 1555 2.37
LINK OD1 ASN E 60 CA CA E 203 1555 1555 2.36
LINK O THR E 62 CA CA E 203 1555 1555 2.73
LINK OE1 GLU E 67 CA CA E 203 1555 1555 2.45
LINK OE2 GLU E 67 CA CA E 203 1555 1555 2.77
LINK OD2 ASP E 93 CA CA E 202 1555 1555 2.46
LINK OD1 ASP E 95 CA CA E 202 1555 1555 2.93
LINK OD1 ASN E 97 CA CA E 202 1555 1555 2.54
LINK O TYR E 99 CA CA E 202 1555 1555 2.36
LINK OE1 GLU E 104 CA CA E 202 1555 1555 2.38
LINK OE2 GLU E 104 CA CA E 202 1555 1555 2.52
LINK OD1 ASP E 129 CA CA E 201 1555 1555 2.41
LINK OD1 ASP E 131 CA CA E 201 1555 1555 2.51
LINK OD1 ASP E 133 CA CA E 201 1555 1555 2.74
LINK O GLN E 135 CA CA E 201 1555 1555 2.73
LINK OE1 GLU E 140 CA CA E 201 1555 1555 2.84
LINK OE2 GLU E 140 CA CA E 201 1555 1555 2.55
LINK OD1 ASP G 20 CA CA G 204 1555 1555 2.46
LINK OD2 ASP G 22 CA CA G 204 1555 1555 3.05
LINK O THR G 26 CA CA G 204 1555 1555 2.34
LINK OE1 GLU G 31 CA CA G 204 1555 1555 2.57
LINK OE2 GLU G 31 CA CA G 204 1555 1555 2.59
LINK OD1 ASP G 56 CA CA G 201 1555 1555 2.65
LINK OD1 ASP G 58 CA CA G 201 1555 1555 2.64
LINK OD1 ASN G 60 CA CA G 201 1555 1555 2.41
LINK O THR G 62 CA CA G 201 1555 1555 2.44
LINK OE1 GLU G 67 CA CA G 201 1555 1555 2.37
LINK OE2 GLU G 67 CA CA G 201 1555 1555 2.51
LINK OD2 ASP G 93 CA CA G 202 1555 1555 2.37
LINK OD1 ASP G 95 CA CA G 202 1555 1555 3.08
LINK OD1 ASN G 97 CA CA G 202 1555 1555 2.58
LINK O TYR G 99 CA CA G 202 1555 1555 2.20
LINK OE1 GLU G 104 CA CA G 202 1555 1555 2.47
LINK OE2 GLU G 104 CA CA G 202 1555 1555 2.73
LINK OD1 ASP G 129 CA CA G 203 1555 1555 2.42
LINK OD1 ASP G 131 CA CA G 203 1555 1555 2.47
LINK OD2 ASP G 133 CA CA G 203 1555 1555 2.40
LINK O GLN G 135 CA CA G 203 1555 1555 2.43
LINK OE1 GLU G 140 CA CA G 203 1555 1555 2.43
LINK OE2 GLU G 140 CA CA G 203 1555 1555 2.47
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A 342
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A 312
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 313
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A 311
SITE 1 AC5 6 ASP C 20 ASP C 22 ASP C 24 THR C 26
SITE 2 AC5 6 GLU C 31 HOH C 320
SITE 1 AC6 7 ASP C 56 ASP C 58 ASN C 60 THR C 62
SITE 2 AC6 7 GLU C 67 HOH C 307 HOH C 347
SITE 1 AC7 6 ASP C 93 ASP C 95 ASN C 97 TYR C 99
SITE 2 AC7 6 GLU C 104 HOH C 312
SITE 1 AC8 6 ASP C 129 ASP C 131 ASP C 133 GLN C 135
SITE 2 AC8 6 GLU C 140 HOH C 306
SITE 1 AC9 5 ASP E 129 ASP E 131 ASP E 133 GLN E 135
SITE 2 AC9 5 GLU E 140
SITE 1 AD1 5 ASP E 93 ASP E 95 ASN E 97 TYR E 99
SITE 2 AD1 5 GLU E 104
SITE 1 AD2 5 ASP E 56 ASP E 58 ASN E 60 THR E 62
SITE 2 AD2 5 GLU E 67
SITE 1 AD3 5 ASP E 20 ASP E 22 ASP E 24 THR E 26
SITE 2 AD3 5 GLU E 31
SITE 1 AD4 5 ASP G 56 ASP G 58 ASN G 60 THR G 62
SITE 2 AD4 5 GLU G 67
SITE 1 AD5 5 ASP G 93 ASP G 95 ASN G 97 TYR G 99
SITE 2 AD5 5 GLU G 104
SITE 1 AD6 5 ASP G 129 ASP G 131 ASP G 133 GLN G 135
SITE 2 AD6 5 GLU G 140
SITE 1 AD7 5 ASP G 20 ASP G 22 ASP G 24 THR G 26
SITE 2 AD7 5 GLU G 31
CRYST1 76.263 37.214 121.193 90.00 100.21 90.00 P 1 21 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 0.013113 0.000000 0.002361 0.00000
SCALE2 0.000000 0.026872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008384 0.00000
(ATOM LINES ARE NOT SHOWN.)
END