HEADER HYDROLASE 15-JUL-15 5CKM
TITLE THE CUB1-EGF-CUB2 DOMAINS OF RAT MBL-ASSOCIATED SERINE PROTEASE-2
TITLE 2 (MASP-2) BOUND TO CA2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANNAN-BINDING LECTIN SERINE PEPTIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 21-297;
COMPND 5 SYNONYM: MANNAN-BINDING LECTIN SERINE PEPTIDASE 2,ISOFORM CRA_B,
COMPND 6 MANNAN-BINDING LECTIN SERINE PROTEASE 2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: MASP2, RCG_31002;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: DXB11;
SOURCE 10 EXPRESSION_SYSTEM_CELL: OVARY;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PED
KEYWDS MASP, CUB1-EGF-CUB2, COMPLEMENT ACTIVATION, LECTIN PATHWAY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.NAN,C.M.FURZE,D.W.WRIGHT,J.GOR,R.WALLIS,S.J.PERKINS
REVDAT 8 10-JAN-24 5CKM 1 HETSYN
REVDAT 7 29-JUL-20 5CKM 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE
REVDAT 6 21-NOV-18 5CKM 1 REMARK LINK
REVDAT 5 13-SEP-17 5CKM 1 REMARK
REVDAT 4 30-AUG-17 5CKM 1 REMARK
REVDAT 3 15-FEB-17 5CKM 1 JRNL
REVDAT 2 01-FEB-17 5CKM 1 JRNL
REVDAT 1 18-JAN-17 5CKM 0
JRNL AUTH R.NAN,C.M.FURZE,D.W.WRIGHT,J.GOR,R.WALLIS,S.J.PERKINS
JRNL TITL FLEXIBILITY IN MANNAN-BINDING LECTIN-ASSOCIATED SERINE
JRNL TITL 2 PROTEASES-1 AND -2 PROVIDES INSIGHT ON LECTIN PATHWAY
JRNL TITL 3 ACTIVATION.
JRNL REF STRUCTURE V. 25 364 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28111019
JRNL DOI 10.1016/J.STR.2016.12.014
REMARK 2
REMARK 2 RESOLUTION. 2.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 14028
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 704
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 22.9400 - 4.6497 1.00 2785 145 0.1844 0.2576
REMARK 3 2 4.6497 - 3.6956 1.00 2704 123 0.1710 0.2061
REMARK 3 3 3.6956 - 3.2299 1.00 2650 148 0.2060 0.2676
REMARK 3 4 3.2299 - 2.9353 1.00 2620 147 0.2394 0.3268
REMARK 3 5 2.9353 - 2.7252 0.97 2565 141 0.2740 0.3198
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.73
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 : 0.004 2302
REMARK 3 ANGLE : 0.830 3124
REMARK 3 CHIRALITY : 0.035 326
REMARK 3 PLANARITY : 0.003 408
REMARK 3 DIHEDRAL : 11.946 824
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7563 -1.3907 23.0122
REMARK 3 T TENSOR
REMARK 3 T11: 0.1895 T22: 0.0831
REMARK 3 T33: 0.1621 T12: 0.0463
REMARK 3 T13: 0.0180 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 2.9227 L22: 2.8134
REMARK 3 L33: 5.5505 L12: 0.3713
REMARK 3 L13: 0.9411 L23: 0.2883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0427 S12: -0.2427 S13: 0.0376
REMARK 3 S21: 0.1466 S22: 0.0591 S23: -0.2093
REMARK 3 S31: -0.0711 S32: 0.1629 S33: -0.0087
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4394 -15.8348 -9.9740
REMARK 3 T TENSOR
REMARK 3 T11: 0.4549 T22: 0.1019
REMARK 3 T33: 0.2848 T12: 0.0603
REMARK 3 T13: 0.0734 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 1.9760 L22: 6.4794
REMARK 3 L33: 5.3151 L12: 0.0769
REMARK 3 L13: -2.7623 L23: 2.9791
REMARK 3 S TENSOR
REMARK 3 S11: -0.2936 S12: -0.2080 S13: -0.5782
REMARK 3 S21: 0.4211 S22: -0.0670 S23: -0.4541
REMARK 3 S31: 0.5105 S32: 0.4048 S33: 0.3254
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7676 -38.4327 -27.7954
REMARK 3 T TENSOR
REMARK 3 T11: 0.3213 T22: 0.1552
REMARK 3 T33: 0.3746 T12: 0.0744
REMARK 3 T13: 0.0419 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 4.3333 L22: 4.6476
REMARK 3 L33: 6.8817 L12: -0.4044
REMARK 3 L13: -0.8588 L23: 1.0406
REMARK 3 S TENSOR
REMARK 3 S11: 0.2026 S12: 0.2589 S13: -0.3443
REMARK 3 S21: 0.1290 S22: -0.2563 S23: 0.4106
REMARK 3 S31: 0.1043 S32: -0.3908 S33: 0.0669
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 5CKM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14031
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.730
REMARK 200 RESOLUTION RANGE LOW (A) : 22.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.060
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: 1NTO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-AC PH 8 CONTAINING 40% MPD
REMARK 280 AND 200 MM SODIUM CITRATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 52.01000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.01000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.45000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.69500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.45000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.69500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.01000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.45000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.69500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.01000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.45000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.69500
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 495 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 510 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 515 LIES ON A SPECIAL POSITION.
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 CB CYS A 53 SG CYS A 71 1.72
REMARK 500 O THR A 78 O HOH A 401 1.84
REMARK 500 CB CYS A 133 SG CYS A 146 1.85
REMARK 500 O SER A 166 O HOH A 402 1.90
REMARK 500 O HOH A 521 O HOH A 531 1.91
REMARK 500 CB CYS A 165 SG CYS A 192 1.91
REMARK 500 NH2 ARG A 37 O HOH A 403 1.93
REMARK 500 O HOH A 480 O HOH A 530 1.97
REMARK 500 OE1 GLU A 219 O HOH A 404 1.98
REMARK 500 O THR A 261 O HOH A 405 1.99
REMARK 500 SG CYS A 133 CB CYS A 146 1.99
REMARK 500 NZ LYS A 2 O HOH A 406 1.99
REMARK 500 O SER A 100 O HOH A 407 2.01
REMARK 500 O HOH A 474 O HOH A 535 2.03
REMARK 500 O ALA A 163 O HOH A 408 2.05
REMARK 500 NZ LYS A 2 O HOH A 409 2.09
REMARK 500 O HOH A 455 O HOH A 527 2.09
REMARK 500 O THR A 86 O HOH A 410 2.10
REMARK 500 N SER A 276 O HOH A 411 2.12
REMARK 500 O HOH A 413 O HOH A 490 2.14
REMARK 500 N GLY A 151 O HOH A 412 2.16
REMARK 500 NE ARG A 52 O HOH A 413 2.16
REMARK 500 SG CYS A 222 CB CYS A 240 2.17
REMARK 500 O SER A 89 O HOH A 414 2.18
REMARK 500 SG CYS A 165 CB CYS A 192 2.19
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 507 O HOH A 533 6545 1.84
REMARK 500 O HOH A 518 O HOH A 536 4555 1.85
REMARK 500 O HOH A 465 O HOH A 523 3555 2.01
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 TYR A 55 -72.28 -75.41
REMARK 500 THR A 76 -165.32 -126.97
REMARK 500 ASP A 101 -149.20 -85.32
REMARK 500 HIS A 135 -87.32 -114.48
REMARK 500 HIS A 159 -43.96 -137.68
REMARK 500 ASP A 213 86.57 -156.42
REMARK 500 GLU A 219 -77.95 -102.05
REMARK 500 GLN A 221 -74.69 -74.81
REMARK 500 TYR A 224 -71.57 -88.51
REMARK 500 THR A 231 -136.80 -101.39
REMARK 500
REMARK 500 REMARK: NULL
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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 48 OE2
REMARK 620 2 ASP A 56 OD1 94.0
REMARK 620 3 ASP A 56 OD2 84.2 52.8
REMARK 620 4 ASP A 101 OD1 99.3 69.9 122.6
REMARK 620 5 SER A 103 O 87.3 153.5 153.2 83.8
REMARK 620 6 ASN A 104 OD1 85.8 129.0 76.5 160.4 77.6
REMARK 620 7 HOH A 479 O 172.4 93.3 101.9 81.4 85.3 91.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 119 OD1
REMARK 620 2 ASP A 119 OD2 45.9
REMARK 620 3 VAL A 120 O 78.7 73.0
REMARK 620 4 GLU A 122 OE1 131.2 133.8 63.3
REMARK 620 5 ASN A 139 OD1 120.1 74.7 76.8 81.2
REMARK 620 6 TYR A 140 O 79.2 76.7 149.7 145.9 96.9
REMARK 620 7 GLY A 143 O 134.6 133.9 145.4 83.6 89.3 62.4
REMARK 620 8 HOH A 464 O 72.7 117.3 85.3 74.5 154.5 107.6 95.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 215 OE1
REMARK 620 2 ASP A 225 OD1 90.4
REMARK 620 3 ASP A 225 OD2 78.5 48.2
REMARK 620 4 ASP A 262 OD1 84.0 66.1 111.0
REMARK 620 5 SER A 264 O 77.4 146.3 151.5 81.3
REMARK 620 6 HOH A 463 O 75.7 121.5 73.2 158.1 86.2
REMARK 620 N 1 2 3 4 5
DBREF 5CKM A 2 278 UNP A2VCV7 A2VCV7_RAT 21 297
SEQRES 1 A 277 LYS TRP PRO GLU PRO VAL PHE GLY ARG LEU VAL SER PRO
SEQRES 2 A 277 GLY PHE PRO GLU LYS TYR GLY ASN HIS GLN ASP ARG SER
SEQRES 3 A 277 TRP THR LEU THR ALA PRO PRO GLY PHE ARG LEU ARG LEU
SEQRES 4 A 277 TYR PHE THR HIS PHE ASN LEU GLU LEU SER TYR ARG CYS
SEQRES 5 A 277 GLU TYR ASP PHE VAL LYS LEU THR SER GLY THR LYS VAL
SEQRES 6 A 277 LEU ALA THR LEU CYS GLY GLN GLU SER THR ASP THR GLU
SEQRES 7 A 277 ARG ALA PRO GLY ASN ASP THR PHE TYR SER LEU GLY PRO
SEQRES 8 A 277 SER LEU LYS VAL THR PHE HIS SER ASP TYR SER ASN GLU
SEQRES 9 A 277 LYS PRO PHE THR GLY PHE GLU ALA PHE TYR ALA ALA GLU
SEQRES 10 A 277 ASP VAL ASP GLU CYS ARG THR SER LEU GLY ASP SER VAL
SEQRES 11 A 277 PRO CYS ASP HIS TYR CYS HIS ASN TYR LEU GLY GLY TYR
SEQRES 12 A 277 TYR CYS SER CYS ARG VAL GLY TYR ILE LEU HIS GLN ASN
SEQRES 13 A 277 LYS HIS THR CYS SER ALA LEU CYS SER GLY GLN VAL PHE
SEQRES 14 A 277 THR GLY ARG SER GLY PHE LEU SER SER PRO GLU TYR PRO
SEQRES 15 A 277 GLN PRO TYR PRO LYS LEU SER SER CYS ALA TYR ASN ILE
SEQRES 16 A 277 ARG LEU GLU GLU GLY PHE SER ILE THR LEU ASP PHE VAL
SEQRES 17 A 277 GLU SER PHE ASP VAL GLU MET HIS PRO GLU ALA GLN CYS
SEQRES 18 A 277 PRO TYR ASP SER LEU LYS ILE GLN THR ASP LYS ARG GLU
SEQRES 19 A 277 TYR GLY PRO PHE CYS GLY LYS THR LEU PRO PRO ARG ILE
SEQRES 20 A 277 GLU THR ASP SER ASN LYS VAL THR ILE THR PHE THR THR
SEQRES 21 A 277 ASP GLU SER GLY ASN HIS THR GLY TRP LYS ILE HIS TYR
SEQRES 22 A 277 THR SER THR ALA
HET CA A 301 1
HET CA A 302 1
HET CA A 303 1
HET NAG A 304 14
HETNAM CA CALCIUM ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 CA 3(CA 2+)
FORMUL 5 NAG C8 H15 N O6
FORMUL 6 HOH *141(H2 O)
HELIX 1 AA1 SER A 50 GLU A 54 5 5
SHEET 1 AA1 4 PHE A 8 VAL A 12 0
SHEET 2 AA1 4 GLY A 110 ASP A 119 -1 O ALA A 113 N LEU A 11
SHEET 3 AA1 4 PHE A 36 ASN A 46 -1 N TYR A 41 O PHE A 114
SHEET 4 AA1 4 PHE A 87 TYR A 88 -1 O PHE A 87 N LEU A 40
SHEET 1 AA2 4 ASP A 25 THR A 31 0
SHEET 2 AA2 4 SER A 93 HIS A 99 -1 O LEU A 94 N LEU A 30
SHEET 3 AA2 4 PHE A 57 SER A 62 -1 N THR A 61 O LYS A 95
SHEET 4 AA2 4 LYS A 65 LEU A 70 -1 O LEU A 70 N VAL A 58
SHEET 1 AA3 2 TYR A 136 TYR A 140 0
SHEET 2 AA3 2 GLY A 143 SER A 147 -1 O TYR A 145 N HIS A 138
SHEET 1 AA4 2 TYR A 152 LEU A 154 0
SHEET 2 AA4 2 CYS A 161 ALA A 163 -1 O SER A 162 N ILE A 153
SHEET 1 AA5 5 GLN A 168 PHE A 170 0
SHEET 2 AA5 5 SER A 191 ARG A 197 1 O ASN A 195 N PHE A 170
SHEET 3 AA5 5 LYS A 254 THR A 260 -1 O PHE A 259 N CYS A 192
SHEET 4 AA5 5 SER A 226 GLN A 230 -1 N GLN A 230 O THR A 256
SHEET 5 AA5 5 GLU A 235 PHE A 239 -1 O TYR A 236 N ILE A 229
SHEET 1 AA6 4 GLY A 175 SER A 178 0
SHEET 2 AA6 4 LYS A 271 THR A 277 -1 O ILE A 272 N LEU A 177
SHEET 3 AA6 4 SER A 203 PHE A 208 -1 N ASP A 207 O HIS A 273
SHEET 4 AA6 4 ILE A 248 GLU A 249 -1 O ILE A 248 N LEU A 206
SSBOND 1 CYS A 53 CYS A 71 1555 1555 2.03
SSBOND 2 CYS A 123 CYS A 137 1555 1555 2.03
SSBOND 3 CYS A 133 CYS A 146 1555 1555 2.01
SSBOND 4 CYS A 148 CYS A 161 1555 1555 2.03
SSBOND 5 CYS A 165 CYS A 192 1555 1555 2.03
SSBOND 6 CYS A 222 CYS A 240 1555 1555 2.03
LINK ND2 ASN A 84 C1 NAG A 304 1555 1555 1.42
LINK OE2 GLU A 48 CA CA A 301 1555 1555 2.33
LINK OD1 ASP A 56 CA CA A 301 1555 1555 2.56
LINK OD2 ASP A 56 CA CA A 301 1555 1555 2.36
LINK OD1 ASP A 101 CA CA A 301 1555 1555 2.35
LINK O SER A 103 CA CA A 301 1555 1555 2.54
LINK OD1 ASN A 104 CA CA A 301 1555 1555 2.43
LINK OD1 ASP A 119 CA CA A 302 1555 1555 2.60
LINK OD2 ASP A 119 CA CA A 302 1555 1555 2.94
LINK O VAL A 120 CA CA A 302 1555 1555 2.39
LINK OE1 GLU A 122 CA CA A 302 1555 1555 2.79
LINK OD1 ASN A 139 CA CA A 302 1555 1555 2.35
LINK O TYR A 140 CA CA A 302 1555 1555 2.44
LINK O GLY A 143 CA CA A 302 1555 1555 2.55
LINK OE1 GLU A 215 CA CA A 303 1555 1555 2.68
LINK OD1 ASP A 225 CA CA A 303 1555 1555 2.73
LINK OD2 ASP A 225 CA CA A 303 1555 1555 2.63
LINK OD1 ASP A 262 CA CA A 303 1555 1555 2.23
LINK O SER A 264 CA CA A 303 1555 1555 2.50
LINK CA CA A 301 O HOH A 479 1555 1555 2.43
LINK CA CA A 302 O HOH A 464 1555 1555 2.39
LINK CA CA A 303 O HOH A 463 1555 1555 2.46
CISPEP 1 PHE A 16 PRO A 17 0 4.56
CISPEP 2 TYR A 182 PRO A 183 0 3.98
CISPEP 3 GLY A 237 PRO A 238 0 4.48
CRYST1 82.900 119.390 104.020 90.00 90.00 90.00 C 2 2 21 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 0.012063 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009614 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
