HEADER SUGAR BINDING PROTEIN 05-FEB-07 2OS9
TITLE CRYSTAL STRUCTURE OF THE TRIMERIC NECK AND CARBOHYDRATE RECOGNITION
TITLE 2 DOMAIN OF HUMAN SURFACTANT PROTEIN D IN COMPLEX WITH MYOINOSITOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PULMONARY SURFACTANT-ASSOCIATED PROTEIN D;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: HEAD AND NECK DOMAIN;
COMPND 5 SYNONYM: SP-D, PSP-D, LUNG SURFACTANT PROTEIN D;
COMPND 6 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: SFTPD, PSPD, SFTP4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTABLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET30A(+)
KEYWDS SURFACTANT PROTEIN, CARBOHYDRATE RECOGNITION DOMAIN, TRIMERIC, SUGAR
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.HEAD
REVDAT 3 30-AUG-23 2OS9 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2OS9 1 VERSN
REVDAT 1 08-MAY-07 2OS9 0
JRNL AUTH E.CROUCH,B.MCDONALD,K.SMITH,M.ROBERTS,T.MEALY,B.SEATON,
JRNL AUTH 2 J.HEAD
JRNL TITL CRITICAL ROLE OF ARG/LYS343 IN THE SPECIES-DEPENDENT
JRNL TITL 2 RECOGNITION OF PHOSPHATIDYLINOSITOL BY PULMONARY SURFACTANT
JRNL TITL 3 PROTEIN D.
JRNL REF BIOCHEMISTRY V. 46 5160 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17417879
JRNL DOI 10.1021/BI700037X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 61994
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.200
REMARK 3 FREE R VALUE TEST SET COUNT : 5502
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4045
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 316
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 515
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : 1.16000
REMARK 3 B33 (A**2) : -1.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.104
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.907
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3586 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4859 ; 1.216 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 449 ; 5.259 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 171 ;37.145 ;25.965
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 585 ;12.536 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;12.702 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 542 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2723 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1746 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2511 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 397 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 21 ; 0.070 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 32 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.200 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
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): 2288 ; 0.972 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3557 ; 1.366 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1437 ; 2.151 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1302 ; 3.425 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 2OS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041522.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-05
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 : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI 111 DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69027
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 27.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : 0.26000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2GGU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150MM NACL, 10MM CACL2, 12% PEG 8000,
REMARK 280 100MM HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290K
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 54.34600
REMARK 290 SMTRY3 2 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 300 REMARK: THE SINGLE TRIMER OF HEAD AND NECK DOMAINS PRESENT IN THE
REMARK 300 ASYMMETRIC UNIT IS THE FUNCTIONAL UNIT.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 ALA A 196
REMARK 465 MET A 197
REMARK 465 ALA A 198
REMARK 465 ASP A 199
REMARK 465 ILE A 200
REMARK 465 GLY A 201
REMARK 465 SER A 202
REMARK 465 ASP A 203
REMARK 465 VAL A 204
REMARK 465 ALA B 196
REMARK 465 MET B 197
REMARK 465 ALA B 198
REMARK 465 ASP B 199
REMARK 465 ILE B 200
REMARK 465 GLY B 201
REMARK 465 SER B 202
REMARK 465 ASP B 203
REMARK 465 VAL B 204
REMARK 465 ALA C 196
REMARK 465 MET C 197
REMARK 465 ALA C 198
REMARK 465 ASP C 199
REMARK 465 ILE C 200
REMARK 465 GLY C 201
REMARK 465 SER C 202
REMARK 465 ASP C 203
REMARK 465 VAL C 204
REMARK 465 ALA C 205
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 SER A 328 56.81 -156.91
REMARK 500 SER B 328 43.43 -151.62
REMARK 500 ASN C 316 48.14 -143.10
REMARK 500 SER C 328 46.80 -153.73
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 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 297 OD2
REMARK 620 2 ASP A 297 OD1 49.6
REMARK 620 3 GLU A 301 OE1 79.3 94.5
REMARK 620 4 GLU A 301 OE2 73.1 119.7 52.9
REMARK 620 5 ASP A 324 OD1 150.7 158.1 86.0 77.7
REMARK 620 6 GLU A 329 O 123.3 88.9 150.5 145.6 80.3
REMARK 620 7 ASP A 330 OD1 112.3 72.0 73.6 124.9 87.2 79.7
REMARK 620 8 HOH A 651 O 78.3 101.7 132.7 80.7 93.8 74.6 153.7
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 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 301 OE1
REMARK 620 2 ASP A 330 OD1 74.4
REMARK 620 3 ASP A 330 OD2 115.6 52.0
REMARK 620 4 HOH A 637 O 81.8 105.7 81.4
REMARK 620 5 HOH A 666 O 77.2 97.1 134.9 143.4
REMARK 620 6 HOH A 688 O 92.5 166.6 139.8 74.6 76.8
REMARK 620 7 HOH A 788 O 142.7 86.7 72.7 135.0 73.6 102.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 321 OE1
REMARK 620 2 ASN A 323 OD1 75.6
REMARK 620 3 GLU A 329 OE1 148.2 77.0
REMARK 620 4 ASN A 341 OD1 68.7 143.0 139.9
REMARK 620 5 ASP A 342 OD1 75.5 84.4 86.0 95.6
REMARK 620 6 ASP A 342 O 127.2 140.3 69.1 73.1 73.3
REMARK 620 7 INS A 631 O1 71.9 80.8 119.0 79.3 146.7 133.8
REMARK 620 8 INS A 631 O6 133.6 117.9 74.4 82.1 144.9 72.5 67.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 297 OD2
REMARK 620 2 ASP B 297 OD1 49.9
REMARK 620 3 GLU B 301 OE2 71.6 119.9
REMARK 620 4 GLU B 301 OE1 78.7 98.9 51.8
REMARK 620 5 ASP B 324 OD1 149.2 159.5 77.7 83.7
REMARK 620 6 GLU B 329 O 128.4 90.7 143.7 148.4 77.4
REMARK 620 7 ASP B 330 OD1 111.1 72.6 126.7 75.8 88.5 78.5
REMARK 620 8 HOH B 643 O 80.1 99.5 80.7 132.0 93.6 74.9 152.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 301 OE1
REMARK 620 2 ASP B 330 OD2 118.2
REMARK 620 3 ASP B 330 OD1 76.2 52.5
REMARK 620 4 HOH B 648 O 90.9 78.1 109.1
REMARK 620 5 HOH B 655 O 83.6 108.2 73.8 173.1
REMARK 620 6 HOH B 674 O 84.7 154.7 151.7 91.7 83.6
REMARK 620 7 HOH B 697 O 164.3 76.6 112.8 97.8 86.6 82.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 321 OE1
REMARK 620 2 ASN B 323 OD1 74.3
REMARK 620 3 GLU B 329 OE1 145.8 75.2
REMARK 620 4 ASN B 341 OD1 69.2 141.6 143.1
REMARK 620 5 ASP B 342 OD1 75.1 83.8 86.7 97.6
REMARK 620 6 ASP B 342 O 128.9 143.1 72.3 72.9 77.3
REMARK 620 7 INS B 632 O1 72.1 73.1 112.9 84.6 143.9 136.4
REMARK 620 8 INS B 632 O1 130.1 112.7 76.6 83.3 151.9 76.2 64.2
REMARK 620 9 INS B 632 O6 129.5 111.4 76.6 84.1 153.0 77.5 63.1 1.4
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 297 OD1
REMARK 620 2 ASP C 297 OD2 50.2
REMARK 620 3 GLU C 301 OE1 98.5 80.3
REMARK 620 4 GLU C 301 OE2 122.0 73.9 52.4
REMARK 620 5 ASP C 324 OD1 155.8 151.3 81.8 77.4
REMARK 620 6 GLU C 329 O 90.7 129.7 144.0 144.1 76.1
REMARK 620 7 ASP C 330 OD1 73.0 111.8 73.5 124.5 84.1 76.1
REMARK 620 8 HOH C 642 O 101.4 81.1 133.5 81.5 95.4 77.3 152.8
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 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 301 OE1
REMARK 620 2 ASP C 330 OD2 120.3
REMARK 620 3 ASP C 330 OD1 74.5 52.4
REMARK 620 4 HOH C 644 O 82.7 103.6 73.7
REMARK 620 5 HOH C 648 O 89.4 85.4 109.8 170.2
REMARK 620 6 HOH C 674 O 85.0 154.0 151.2 84.0 89.6
REMARK 620 7 HOH C 685 O 162.5 75.1 114.6 85.8 100.5 80.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 321 OE1
REMARK 620 2 ASN C 323 OD1 73.3
REMARK 620 3 GLU C 329 OE1 148.1 77.7
REMARK 620 4 ASN C 341 OD1 67.5 139.0 143.1
REMARK 620 5 ASP C 342 O 128.5 144.9 72.3 73.5
REMARK 620 6 ASP C 342 OD1 76.5 85.6 88.3 96.4 75.9
REMARK 620 7 INS C 633 O1 129.6 117.2 76.1 81.0 72.8 147.9
REMARK 620 8 INS C 633 O6 131.5 116.4 74.1 82.8 72.3 147.0 2.1
REMARK 620 9 INS C 633 O1 70.2 75.2 115.0 80.5 134.3 145.1 66.4 67.6
REMARK 620 N 1 2 3 4 5 6 7 8
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INS A 631
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INS B 632
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INS C 633
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GGU RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH MALTOTRIOSE
REMARK 900 RELATED ID: 2ORJ RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH N-ACETYL-D-MANNOSAMINE
REMARK 900 RELATED ID: 2ORK RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH MYO-INOSITOL-1-PHOSPHATE
DBREF 2OS9 A 203 355 UNP P35247 SFTPD_HUMAN 223 375
DBREF 2OS9 B 203 355 UNP P35247 SFTPD_HUMAN 223 375
DBREF 2OS9 C 203 355 UNP P35247 SFTPD_HUMAN 223 375
SEQADV 2OS9 ALA A 196 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 MET A 197 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ALA A 198 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ASP A 199 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ILE A 200 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 GLY A 201 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 SER A 202 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ALA B 196 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 MET B 197 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ALA B 198 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ASP B 199 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ILE B 200 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 GLY B 201 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 SER B 202 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ALA C 196 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 MET C 197 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ALA C 198 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ASP C 199 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 ILE C 200 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 GLY C 201 UNP P35247 CLONING ARTIFACT
SEQADV 2OS9 SER C 202 UNP P35247 CLONING ARTIFACT
SEQRES 1 A 160 ALA MET ALA ASP ILE GLY SER ASP VAL ALA SER LEU ARG
SEQRES 2 A 160 GLN GLN VAL GLU ALA LEU GLN GLY GLN VAL GLN HIS LEU
SEQRES 3 A 160 GLN ALA ALA PHE SER GLN TYR LYS LYS VAL GLU LEU PHE
SEQRES 4 A 160 PRO ASN GLY GLN SER VAL GLY GLU LYS ILE PHE LYS THR
SEQRES 5 A 160 ALA GLY PHE VAL LYS PRO PHE THR GLU ALA GLN LEU LEU
SEQRES 6 A 160 CYS THR GLN ALA GLY GLY GLN LEU ALA SER PRO ARG SER
SEQRES 7 A 160 ALA ALA GLU ASN ALA ALA LEU GLN GLN LEU VAL VAL ALA
SEQRES 8 A 160 LYS ASN GLU ALA ALA PHE LEU SER MET THR ASP SER LYS
SEQRES 9 A 160 THR GLU GLY LYS PHE THR TYR PRO THR GLY GLU SER LEU
SEQRES 10 A 160 VAL TYR SER ASN TRP ALA PRO GLY GLU PRO ASN ASP ASP
SEQRES 11 A 160 GLY GLY SER GLU ASP CYS VAL GLU ILE PHE THR ASN GLY
SEQRES 12 A 160 LYS TRP ASN ASP ARG ALA CYS GLY GLU LYS ARG LEU VAL
SEQRES 13 A 160 VAL CYS GLU PHE
SEQRES 1 B 160 ALA MET ALA ASP ILE GLY SER ASP VAL ALA SER LEU ARG
SEQRES 2 B 160 GLN GLN VAL GLU ALA LEU GLN GLY GLN VAL GLN HIS LEU
SEQRES 3 B 160 GLN ALA ALA PHE SER GLN TYR LYS LYS VAL GLU LEU PHE
SEQRES 4 B 160 PRO ASN GLY GLN SER VAL GLY GLU LYS ILE PHE LYS THR
SEQRES 5 B 160 ALA GLY PHE VAL LYS PRO PHE THR GLU ALA GLN LEU LEU
SEQRES 6 B 160 CYS THR GLN ALA GLY GLY GLN LEU ALA SER PRO ARG SER
SEQRES 7 B 160 ALA ALA GLU ASN ALA ALA LEU GLN GLN LEU VAL VAL ALA
SEQRES 8 B 160 LYS ASN GLU ALA ALA PHE LEU SER MET THR ASP SER LYS
SEQRES 9 B 160 THR GLU GLY LYS PHE THR TYR PRO THR GLY GLU SER LEU
SEQRES 10 B 160 VAL TYR SER ASN TRP ALA PRO GLY GLU PRO ASN ASP ASP
SEQRES 11 B 160 GLY GLY SER GLU ASP CYS VAL GLU ILE PHE THR ASN GLY
SEQRES 12 B 160 LYS TRP ASN ASP ARG ALA CYS GLY GLU LYS ARG LEU VAL
SEQRES 13 B 160 VAL CYS GLU PHE
SEQRES 1 C 160 ALA MET ALA ASP ILE GLY SER ASP VAL ALA SER LEU ARG
SEQRES 2 C 160 GLN GLN VAL GLU ALA LEU GLN GLY GLN VAL GLN HIS LEU
SEQRES 3 C 160 GLN ALA ALA PHE SER GLN TYR LYS LYS VAL GLU LEU PHE
SEQRES 4 C 160 PRO ASN GLY GLN SER VAL GLY GLU LYS ILE PHE LYS THR
SEQRES 5 C 160 ALA GLY PHE VAL LYS PRO PHE THR GLU ALA GLN LEU LEU
SEQRES 6 C 160 CYS THR GLN ALA GLY GLY GLN LEU ALA SER PRO ARG SER
SEQRES 7 C 160 ALA ALA GLU ASN ALA ALA LEU GLN GLN LEU VAL VAL ALA
SEQRES 8 C 160 LYS ASN GLU ALA ALA PHE LEU SER MET THR ASP SER LYS
SEQRES 9 C 160 THR GLU GLY LYS PHE THR TYR PRO THR GLY GLU SER LEU
SEQRES 10 C 160 VAL TYR SER ASN TRP ALA PRO GLY GLU PRO ASN ASP ASP
SEQRES 11 C 160 GLY GLY SER GLU ASP CYS VAL GLU ILE PHE THR ASN GLY
SEQRES 12 C 160 LYS TRP ASN ASP ARG ALA CYS GLY GLU LYS ARG LEU VAL
SEQRES 13 C 160 VAL CYS GLU PHE
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET INS A 631 12
HET CA B 401 1
HET CA B 402 1
HET CA B 403 1
HET INS B 632 24
HET CA C 401 1
HET CA C 402 1
HET CA C 403 1
HET INS C 633 24
HETNAM CA CALCIUM ION
HETNAM INS 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE
HETSYN INS MYO-INOSITOL
FORMUL 4 CA 9(CA 2+)
FORMUL 7 INS 3(C6 H12 O6)
FORMUL 16 HOH *515(H2 O)
HELIX 1 1 SER A 206 PHE A 234 1 29
HELIX 2 2 PHE A 254 ALA A 264 1 11
HELIX 3 3 SER A 273 ASN A 288 1 16
HELIX 4 4 ASP A 324 SER A 328 5 5
HELIX 5 5 ALA B 205 PHE B 234 1 30
HELIX 6 6 PHE B 254 ALA B 264 1 11
HELIX 7 7 SER B 273 ASN B 288 1 16
HELIX 8 8 ASP B 324 SER B 328 5 5
HELIX 9 9 SER C 206 PHE C 234 1 29
HELIX 10 10 PHE C 254 ALA C 264 1 11
HELIX 11 11 SER C 273 ASN C 288 1 16
HELIX 12 12 ASP C 324 SER C 328 5 5
SHEET 1 A 4 GLY A 237 VAL A 240 0
SHEET 2 A 4 LYS A 243 PRO A 253 -1 O PHE A 245 N GLN A 238
SHEET 3 A 4 LYS A 348 PHE A 355 -1 O PHE A 355 N ILE A 244
SHEET 4 A 4 GLN A 267 LEU A 268 -1 N GLN A 267 O GLU A 354
SHEET 1 B 3 ALA A 291 PHE A 292 0
SHEET 2 B 3 CYS A 331 ILE A 334 -1 O ILE A 334 N ALA A 291
SHEET 3 B 3 TRP A 340 ARG A 343 -1 O ASN A 341 N GLU A 333
SHEET 1 C 4 GLY B 237 VAL B 240 0
SHEET 2 C 4 LYS B 243 PRO B 253 -1 O PHE B 245 N GLN B 238
SHEET 3 C 4 LYS B 348 PHE B 355 -1 O CYS B 353 N LYS B 246
SHEET 4 C 4 GLN B 267 LEU B 268 -1 N GLN B 267 O GLU B 354
SHEET 1 D 3 ALA B 291 PHE B 292 0
SHEET 2 D 3 CYS B 331 ILE B 334 -1 O ILE B 334 N ALA B 291
SHEET 3 D 3 TRP B 340 ARG B 343 -1 O ASN B 341 N GLU B 333
SHEET 1 E 4 GLY C 237 VAL C 240 0
SHEET 2 E 4 LYS C 243 PRO C 253 -1 O PHE C 245 N GLN C 238
SHEET 3 E 4 LYS C 348 PHE C 355 -1 O PHE C 355 N ILE C 244
SHEET 4 E 4 GLN C 267 LEU C 268 -1 N GLN C 267 O GLU C 354
SHEET 1 F 3 ALA C 291 PHE C 292 0
SHEET 2 F 3 CYS C 331 ILE C 334 -1 O ILE C 334 N ALA C 291
SHEET 3 F 3 TRP C 340 ARG C 343 -1 O ASN C 341 N GLU C 333
SSBOND 1 CYS A 261 CYS A 353 1555 1555 2.02
SSBOND 2 CYS A 331 CYS A 345 1555 1555 2.05
SSBOND 3 CYS B 261 CYS B 353 1555 1555 2.05
SSBOND 4 CYS B 331 CYS B 345 1555 1555 2.06
SSBOND 5 CYS C 261 CYS C 353 1555 1555 2.03
SSBOND 6 CYS C 331 CYS C 345 1555 1555 2.06
LINK OD2 ASP A 297 CA CA A 402 1555 1555 2.49
LINK OD1 ASP A 297 CA CA A 402 1555 1555 2.71
LINK OE1 GLU A 301 CA CA A 402 1555 1555 2.51
LINK OE2 GLU A 301 CA CA A 402 1555 1555 2.51
LINK OE1 GLU A 301 CA CA A 403 1555 1555 2.32
LINK OE1 GLU A 321 CA CA A 401 1555 1555 2.52
LINK OD1 ASN A 323 CA CA A 401 1555 1555 2.49
LINK OD1 ASP A 324 CA CA A 402 1555 1555 2.45
LINK OE1 GLU A 329 CA CA A 401 1555 1555 2.48
LINK O GLU A 329 CA CA A 402 1555 1555 2.48
LINK OD1 ASP A 330 CA CA A 402 1555 1555 2.41
LINK OD1 ASP A 330 CA CA A 403 1555 1555 2.54
LINK OD2 ASP A 330 CA CA A 403 1555 1555 2.44
LINK OD1 ASN A 341 CA CA A 401 1555 1555 2.41
LINK OD1 ASP A 342 CA CA A 401 1555 1555 2.35
LINK O ASP A 342 CA CA A 401 1555 1555 2.60
LINK CA CA A 401 O1 INS A 631 1555 1555 2.54
LINK CA CA A 401 O6 INS A 631 1555 1555 2.66
LINK CA CA A 402 O HOH A 651 1555 1555 2.49
LINK CA CA A 403 O HOH A 637 1555 1555 2.41
LINK CA CA A 403 O HOH A 666 1555 1555 2.31
LINK CA CA A 403 O HOH A 688 1555 1555 2.37
LINK CA CA A 403 O HOH A 788 1555 1555 2.45
LINK OD2 ASP B 297 CA CA B 402 1555 1555 2.44
LINK OD1 ASP B 297 CA CA B 402 1555 1555 2.67
LINK OE2 GLU B 301 CA CA B 402 1555 1555 2.54
LINK OE1 GLU B 301 CA CA B 402 1555 1555 2.54
LINK OE1 GLU B 301 CA CA B 403 1555 1555 2.34
LINK OE1 GLU B 321 CA CA B 401 1555 1555 2.51
LINK OD1 ASN B 323 CA CA B 401 1555 1555 2.42
LINK OD1 ASP B 324 CA CA B 402 1555 1555 2.58
LINK OE1 GLU B 329 CA CA B 401 1555 1555 2.40
LINK O GLU B 329 CA CA B 402 1555 1555 2.47
LINK OD1 ASP B 330 CA CA B 402 1555 1555 2.38
LINK OD2 ASP B 330 CA CA B 403 1555 1555 2.46
LINK OD1 ASP B 330 CA CA B 403 1555 1555 2.55
LINK OD1 ASN B 341 CA CA B 401 1555 1555 2.44
LINK OD1 ASP B 342 CA CA B 401 1555 1555 2.30
LINK O ASP B 342 CA CA B 401 1555 1555 2.52
LINK CA CA B 401 O1 AINS B 632 1555 1555 2.68
LINK CA CA B 401 O1 BINS B 632 1555 1555 2.63
LINK CA CA B 401 O6 AINS B 632 1555 1555 2.60
LINK CA CA B 401 O6 BINS B 632 1555 1555 2.59
LINK CA CA B 402 O HOH B 643 1555 1555 2.57
LINK CA CA B 403 O HOH B 648 1555 1555 2.37
LINK CA CA B 403 O HOH B 655 1555 1555 2.47
LINK CA CA B 403 O HOH B 674 1555 1555 2.38
LINK CA CA B 403 O HOH B 697 1555 1555 2.52
LINK OD1 ASP C 297 CA CA C 402 1555 1555 2.60
LINK OD2 ASP C 297 CA CA C 402 1555 1555 2.54
LINK OE1 GLU C 301 CA CA C 402 1555 1555 2.49
LINK OE2 GLU C 301 CA CA C 402 1555 1555 2.45
LINK OE1 GLU C 301 CA CA C 403 1555 1555 2.35
LINK OE1 GLU C 321 CA CA C 401 1555 1555 2.60
LINK OD1 ASN C 323 CA CA C 401 1555 1555 2.45
LINK OD1 ASP C 324 CA CA C 402 1555 1555 2.59
LINK OE1 GLU C 329 CA CA C 401 1555 1555 2.31
LINK O GLU C 329 CA CA C 402 1555 1555 2.44
LINK OD1 ASP C 330 CA CA C 402 1555 1555 2.46
LINK OD2 ASP C 330 CA CA C 403 1555 1555 2.43
LINK OD1 ASP C 330 CA CA C 403 1555 1555 2.54
LINK OD1 ASN C 341 CA CA C 401 1555 1555 2.40
LINK O ASP C 342 CA CA C 401 1555 1555 2.52
LINK OD1 ASP C 342 CA CA C 401 1555 1555 2.34
LINK CA CA C 401 O1 AINS C 633 1555 1555 2.65
LINK CA CA C 401 O6 BINS C 633 1555 1555 2.56
LINK CA CA C 401 O1 BINS C 633 1555 1555 2.46
LINK CA CA C 401 O6 AINS C 633 1555 1555 2.56
LINK CA CA C 402 O HOH C 642 1555 1555 2.36
LINK CA CA C 403 O HOH C 644 1555 1555 2.45
LINK CA CA C 403 O HOH C 648 1555 1555 2.30
LINK CA CA C 403 O HOH C 674 1555 1555 2.36
LINK CA CA C 403 O HOH C 685 1555 1555 2.62
CISPEP 1 PHE A 234 PRO A 235 0 -1.36
CISPEP 2 GLU A 321 PRO A 322 0 -4.28
CISPEP 3 PHE B 234 PRO B 235 0 -3.18
CISPEP 4 GLU B 321 PRO B 322 0 -1.80
CISPEP 5 PHE C 234 PRO C 235 0 -1.66
CISPEP 6 GLU C 321 PRO C 322 0 -2.88
SITE 1 AC1 6 GLU A 321 ASN A 323 GLU A 329 ASN A 341
SITE 2 AC1 6 ASP A 342 INS A 631
SITE 1 AC2 6 ASP A 297 GLU A 301 ASP A 324 GLU A 329
SITE 2 AC2 6 ASP A 330 HOH A 651
SITE 1 AC3 6 GLU A 301 ASP A 330 HOH A 637 HOH A 666
SITE 2 AC3 6 HOH A 688 HOH A 788
SITE 1 AC4 6 GLU B 321 ASN B 323 GLU B 329 ASN B 341
SITE 2 AC4 6 ASP B 342 INS B 632
SITE 1 AC5 6 ASP B 297 GLU B 301 ASP B 324 GLU B 329
SITE 2 AC5 6 ASP B 330 HOH B 643
SITE 1 AC6 6 GLU B 301 ASP B 330 HOH B 648 HOH B 655
SITE 2 AC6 6 HOH B 674 HOH B 697
SITE 1 AC7 6 GLU C 321 ASN C 323 GLU C 329 ASN C 341
SITE 2 AC7 6 ASP C 342 INS C 633
SITE 1 AC8 6 ASP C 297 GLU C 301 ASP C 324 GLU C 329
SITE 2 AC8 6 ASP C 330 HOH C 642
SITE 1 AC9 6 GLU C 301 ASP C 330 HOH C 644 HOH C 648
SITE 2 AC9 6 HOH C 674 HOH C 685
SITE 1 BC1 9 GLU A 321 ASN A 323 GLU A 329 ASN A 341
SITE 2 BC1 9 ASP A 342 ARG A 343 CA A 401 HOH A 710
SITE 3 BC1 9 HOH A 724
SITE 1 BC2 13 GLU B 321 ASN B 323 GLU B 329 ASN B 341
SITE 2 BC2 13 ASP B 342 ARG B 343 CA B 401 HOH B 689
SITE 3 BC2 13 HOH B 711 HOH B 724 HOH B 743 HOH B 751
SITE 4 BC2 13 HOH B 783
SITE 1 BC3 13 GLU C 321 ASN C 323 ASP C 325 GLU C 329
SITE 2 BC3 13 ASN C 341 ASP C 342 ARG C 343 CA C 401
SITE 3 BC3 13 HOH C 681 HOH C 734 HOH C 740 HOH C 743
SITE 4 BC3 13 HOH C 769
CRYST1 55.564 108.692 55.774 90.00 91.49 90.00 P 1 21 1 6
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 0.017997 0.000000 0.000468 0.00000
SCALE2 0.000000 0.009200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017936 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
